Hemagglutinating Activity Of Lectin Research Articles

Antinutritional effect of lectin from faveira (Parkia platycephala) seeds in tambatinga (Colossoma macropomum x Piaractus brachypomus)

This study investigated the possible antinutritional effects of Parkia platycephala lectin (0, 20, 40, or 60 mg kg-1 of diet) on tambatinga feeding for 60 days as well as methods of inactivating this protein. Weight gain, specific growth rate, and relative weight gain decreased, and the feed conversion rate increased with the increase in dietary lectin. The hepatic glycogen levels of fish fed 60 mg kg-1 were higher than those of fish fed 20 and 40 mg kg-1. Diets containing 40 and 60 mg kg-1 increased muscle glucose levels compared to the control group. Fish-fed diets containing lectin showed reduced muscle glycogen compared to those receiving the control diet. Fish fed 60 mg kg-1 presented lower muscle protein levels than those fed 20 mg kg-1. In vitro tests showed that the hemagglutination activity of lectin was inhibited by d-mannose, d-glucose, and α-methyl-d-mannopyranoside. Thermal treatment at 50–60°C was sufficient to reduce the action of lectin, as well as a pH below and above the 6–7 range. Therefore, the use of P. platycephala meals as a dietary ingredient for tambatinga with no lectin inactivation is not recommended as it can negatively affect the fish’s biochemical parameters and growth. Acid or alkaline solutions can be an alternative for inactivating the protein and improving its use by fish and other animals.

Antimicrobial Analysis of Biosynthesized Lectin-Conjugated Gold Nanoparticles

To enhance the bioactivity of molecules through nanoparticles is being tested which has potential use in sustained-release drug delivery systems and to enhance the therapeutic effectiveness of drugs. Our current investigation s is to conjugate lectin to that of a gold nanoparticle (GNP) surface without disturbing the bioactive properties and enhances the antibacterial activity of lectin. Au-lectin nanoparticles were checked for their hemagglutination activity, characterized by transmission electron microscopy (TEM) and UV-visible spectrophotometer. The antibacterial effect of nanoparticle lectin, Au salt nanoparticle, and conjugated Au-lectin was estimated by Kirby-Bauer disc method; MICs were determined by microbroth dilution and compared with ciprofloxacin. These tests were done using known species of bacterial strain of multidrug resistant. The hemagglutination activity of lectin was improved to fourfold after purification. Lectin and Au nanoparticles combined had a significant effect on the inhibition of bacterial growth. No significant differences were observed in the inhibition zone diameters from killed bacteria and its supernatant towards any of the tested organisms. Lectin-conjugated gold particles showed good efficacy as antimicrobial agents and the nanoparticle-killed bacteria to work against the viable population of the same bacterium and/or other bacterial species too.

Characterization of the C-type lectin from the marine sponge (Stylissa flexibilis)

A lectin from the marine sponge Stylissa flexibilis, designated as SFL, was purified by cold ethanol precipitation followed by ion exchange chromatography on DEAE Sepharose column and Sephacryl S-200 gel filtration. SFL is a dimeric glycoprotein of 32 kDa subunits linked by a disulfide bridge with a molecular mass of 64 kDa by SDS-PAGE and 65 kDa by Sephacryl S-200 gel filtration chromatography. The lectin preferentially agglutinated enzyme treated human A erythrocytes, whereas it did not agglutinate any type of rabbit, human B and O erythrocytes, irrespective of treatment with enzymes. The hemagglutination activity of lectin was strongly inhibited by monosaccharide, D-galactose and glycoproteins, asialo-porcine stomach mucin and asialo-fetuin, indicating that lectin is specific for O-glycans. Activity of SFL was stable over a range of pH from 5 to 8, up to 60 °C for 30 min and its activity was Ca2+ dependent, indicating that SFL was belonged to the C-type lectin family and requires metal for biological activity. SFL caused agglutination of Vibrio alginolyticus and V. parahaemolyticus in a dose dependent manner and inhibited the growth rate of these bacterial strains, suggesting that the lectin caused the agglutination through binding to the target receptor(s) on the surface of Vibrios. Thus, SFL can be considered as a good source of lectin(s) being useful as carbohydrate probe and antibacterial reagent.

Differential recognition of natural and remodeled glycotopes by three Diocleae lectins.

The carbohydrate specificities of Dioclea grandiflora lectins DGL-I1 and DGL-II, and Galactia lindenii lectin II (GLL-II) were explored by use of remodeled glycoproteins as well as by the lectin hemagglutinating activity against erythrocytes from various species with different glycomic profiles. The three lectins exhibited differences in glycan binding specificity but also showed overlapping recognition of some glycotopes (i.e. Tα glycotope for the three lectins; IIβ glycotope for DGL-II and GLL-II lectins); in many cases the interaction with distinct glycotopes was influenced by the structural context, i.e., by the neighbouring sugar residues. Our data complement and expand the existing knowledge about the binding specificity of these three Diocleae lectins, and taken together with results of previous studies, allow us to suggest a functional map of the carbohydrate recognition which illustrate the impact of modification of basic glycotopes enhancing, permiting, or inhibiting their recognition by each lectin.

Healing activity evaluation of the galactomannan film obtained from Cassia grandis seeds with immobilized Cratylia mollis seed lectin

Galactomannan films from Cassia grandis seeds, associated or not with Cramoll 1,4, were used on topical wounds of rats for the evaluation of the healing process during 14days. All of the films were evaluated by cytotoxic assay, FTIR and lectin hemagglutinating activity (HA). Forty-five male rats were submitted to aseptic dermal wounds (Ø=0.8cm) and divided in groups (n=15): control, test 1, and test 2, treated respectively with saline, galactomannan film and film with immobilized Cramoll 1,4. Macroscopic evaluations were performed by clinical observations and area measurements, and microscopic analysis by histological criteria. Epithelial cell proliferation and differentiation was immunohistochemically assessed using CK14 and PCNA. The presence of CO peaks in the FTIR spectrum confirmed the immobilization of Cramoll 1,4 in the film, while the residual HA confirmed the stability of the lectin after immobilization with 90.94% of the initial HA. The films presented non-cytotoxicity and cell viability exceeding 80%. All of the animals presented re-epithelization around 10days, furthermore test 2 group showed a diffuse response at the stromal tissue and the basal layer associated with wounds completely closed with 11days of experiment. The results suggest a promising use of the films as topical wound curatives.

THE EFFECT OF PURIFIED NIGELLA SATIVA LECTIN AGAINST TUMOR DEVELOPMENT IN FEMALE ALBINO MICE AND GENETIC POLYMORPHISM IN PUMA GENE

The purpose of this study examine whether the polymorphism in p53 upregulated modulator of apoptosis (PUMA) gene consequential treated with purified Nigella sativa lectin in tumor induced mice. Nigella sativa (N. sativa) is a widely used medicinal plant throughout the world. Possess a seed lectin that was purified by combination of ammonium sulfate precipitation and affinity chromatography on a Sepharose 4B column. The Nigella sativa strongly agglutinated human erythrocytes. The hemagglutinating activity of lectin was maintained after incubation at a wide range of temperature and pH and also was independent of divalent cations. By sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis, lectin exhibited an electrophoretic profile consisting of a single band with apparent molecular mass of 45 kDa. Experimental groups were organized into 6 groups including 10 animals per each, additionally control group, blood samples were collected form mice before and after lectin treatment for liver and kidney enzymes biochemical analysis, Data statistical analysis for mitochondrial enzymes in our study showed a very highly significant (P>0.001) difference in the mean value of serum enzymes isolated from treatments groups with the polymorphism of the PUMA gene were typed from genomic DNA, the results from PUMA showed a strong deferent between the treatments with lectin.

Investigating a galactomannan gel obtained from Cassia grandis seeds as immobilizing matrix for Cramoll lectin

Characterization, with emphasis on the rheological properties, of Cassia grandis seeds galactomannan gel containing immobilized Cramoll 1–4 is presented. The gels, with and without immobilized Cramoll 1–4, were evaluated along time by rheometry, pH, color, microbial contamination and lectin hemagglutinating activity (HA). Rheological determinations confirmed the gels to be very stable up to 30 days with variations occurring after this period. Rheological data also showed that the gel/Cramoll 1–4 immobilizing matrix loses its elastic modulus substantially after 60 days. Both gels presented no microbial contamination as well as a pH close to neutral. Colorimetric parameters demonstrated the gels transparency with occasional yellowness. The opacity of the galactomannan gel did not change significantly along the study; the same did not occur for the gel with immobilized Cramoll 1–4 as a statistically significant reduction of its opacity was observed. In what concerns immobilized Cramoll 1–4 HA, up to 90% of its initial HA was maintained after 20 days, with a decrease to 60% after 60 days. These results combined with the thickening and stabilizing characteristics of the galactomannan gel make this gel a promising immobilizing matrix for Cramoll 1–4 that can be further exploited for clinical and cosmetic applications.

Two Chitotriose-Specific Lectins Show Anti-Angiogenesis, Induces Caspase-9-Mediated Apoptosis and Early Arrest of Pancreatic Tumor Cell Cycle.

The antiproliferative activity of two chito- specific agglutinins purified from Benincasa hispida (BhL) and Datura innoxia (DiL9) of different plant family origin was investigated on various cancer cell lines. Both lectins showed chitotriose specificity, by inhibiting lectin hemagglutinating activity. On further studies, it was revealed that these agglutinins caused remarkable concentration-dependent antiproliferative effect on human pancreatic cancerous cells but not on the normal human umbilical vein endothelial cells even at higher doses determined using MTT assay. The GI50 values were approximately 8.4 μg ml-1 (0.247 μM) and 142 μg ml-1(14.8 μM) for BhL and DiL9, respectively, against PANC-1 cells. The growth inhibitory effect of these lectins on pancreatic cancer cells were shown to be a consequence of lectin cell surface binding and triggering G0/G1 arrest, mitochondrial membrane depolarization, sustained increase of the intracellular calcium release and the apoptotic signal is amplified by activation of caspases executing cell death. Interestingly, these lectins also showed anti-angiogenic activity by disrupting the endothelial tubulogenesis. Therefore, we report for the first time two chito-specific lectins specifically binding to tumor glycans; they can be considered to be a class of molecules with antitumor activity against pancreatic cancer cells mediated through caspase dependent mitochondrial apoptotic pathway.

What Is The New Tumor Marker For Detection Of Different Kidney Tumors? Modern Study To Isolation, Purification, And Characterization Of Galactose Binding Lectin From Sera Of Patients With Kidney Cancer

The present study was designed to investigate lectins in sera of patients with kidney tumors, in addition to non tumoral kidney disease patients. Fifty five patients of malignant kidney tumors were enrolled in addition to 23 patients of benign kidney tumors, and 18 patients of non tumoral kidney diseases used as control groups, in addition to 46 healthy individuals were also investigated. The age of patients and healthy individuals were 10-90 years. The measurement of total serum proteins revealed significant (p < 0.001) decrease in patients of malignant tumors when compared with those of benign, non tumoral diseases, and healthy individuals. The conditions of the hemagglutination assay of serum lectin activity were optimized. They were Tris buffer of 20 mM and pH 7.4, 60 mM CaCl2, 800 µg of defatted serum, 30 ˚C for serum samples, 60 minutes for serum samples, and human blood of group A+ suspension with 1.4 optical density. The measurement of the specific hemagglutination activity of lectins demonstrated significant (p < 0.001) elevation in patients of malignant tumors when compared with those of other patients and healthy individuals. Lectin activity was pointed out to be significantly (r = 0.767 at p < 0.0005) positively correlated with stage of malignancies. The cutoff value of the specific hemagglutination activity was found to equal 6 SHU for discriminatory malignant kidney tumors. Serum lectins activity were indicated to be inhibited by galactose, mannose, lactose, and N-acetyl galactosamine. Purification of lectin from sera of patients with malignant kidney tumors by affinity chromatography with the use of silver stain revealed galactose binding lectin (GalBL). The purified folds and the yield was 132 with 22.1. The polyacrylamide gel electrophoresis (PAGE) of purified lectin demonstrated one band consisted lectin activity. The approximate molecular weight of GalBL was determined and found to be 98.40. Purified lectin was characterized through the assessment of the capability to agglutinate RBCs, inhibition by EDTA, pH dependency, thermal dependent, and carbohydrate contents. GalBL was observed to be calcium independence lectins. These results suggest that the diagnosis of the specific hemagglutination activity of lectin is a promising biomarker for discrimination of malignant kidney tumor patients and the purified lectin could be introduced in the field of biomarkers.

Bacteriostatic activity of con a lectin from Canavalia ensiformis

The aim of this work was to explore the therapeutic applications of Con A lectin from Canavalia ensiformis and to explore its antibacterial activity. Activity of lectin was quantified by their ability to agglutinate erythrocytes using Hemagglutination assay. Characterization and purity of Con A lectin was evaluated by using SDS-PAGE analysis. The reversal of hemagglutination activity of lectin was evaluated by using the sugars namely; mannose, galactose, lactose, fructose, glucose. The antibacterial activity of lectins was tested against Streptococcus mutans, Staphylococcus aureus, Bacillus subtilis, Escherichia coli using pour plate method. Amoxycillin was used as standard. At 250mg/ml concentration Con A lectin showed good bacteriostatic activity.

What Is The New and Sensitive Tumor Marker for Detection of Different Kidney Tumors? Modern Study to Isolation, Purification and Characterization of N-Acetyl Galactosamine Binding Lectin From Sera Of Patients With Kidney Cancer

The present study was designed to investigate lectins in sera of patients with kidney tumors, in addition to non tumoral kidney disease patients. Fifty five patients of malignant kidney tumors were enrolled in addition to 23 patients of benign kidney tumors, and 18 patients of non tumoral kidney diseases used as control groups, in addition to 46 healthy individuals were also investigated. The age of patients and healthy individuals were 10-90 years. The measurement of total serum proteins revealed significant (p &lt; 0.001) decrease in patients of malignant tumors when compared with those of benign, non tumoral diseases, and healthy individuals. The conditions of the hemagglutination assay of serum lectin activity were optimized. They were Tris buffer of 20 mM and pH 7.4, 60 mM CaCl2, 800 µg of defatted serum, 30 ˚C for serum samples, 60 minutes for serum samples, and human blood of group A+ suspension with 1.4 optical density. The measurement of the specific hemagglutination activity of lectins demonstrated significant (p &lt; 0.001) elevation in patients of malignant tumors when compared with those of other patients and healthy individuals. Lectin activity was pointed out to be significantly (r = 0.767 at p &lt; 0.0005) positively correlated with stage of malignancies. The cutoff value of the specific hemagglutination activity was found to equal 6 SHU for discriminatory malignant kidney tumors. Serum lectins activity were indicated to be inhibited by galactose, mannose, lactose, and N-acetyl galactosamine. Purification of lectin from sera of patients with malignant kidney tumors by affinity chromatography with the use of silver stain revealed N-Acetyl Galactosamine Binding Lectin (GalNAcBL). The purified folds and the yield was 178 with 32.4%. The polyacrylamide gel electrophoresis (PAGE) of purified lectin demonstrated one band consisted lectin activity. The approximate molecular weight of GalNAcBL was determined and found to be 63.83. Purified lectin was characterized through the assessment of the capability to agglutinate RBCs, inhibition by EDTA, pH dependency, thermal dependent, and carbohydrate contents. GalNAcBL were observed to be calcium dependence lectins (C-type). These results suggest that the diagnosis of the specific hemagglutination activity of lectin is promising biomarker for discrimination of malignant kidney tumor patients and the purified lectin could be introduced in the field of biomarkers.

Compounds of the 1,5-di(4-R-phenyl)-3-selenopentanediones-1,5 series interaction with the Basidiomycete Lentinula edodes, lectins: Computations and Experiment

The role of spatial and electron structure, hydrophobic properties and concentration of organoselenium compounds on their interaction with fungal metabolites - extracellular lectins of Lentinula edodes, (shiitake mushroom) has been considered. By the hybrid method of density functional theory at the B3LYP/6-31G(d,p) theory level, spatial and electronic structure of the 1,5-diphenyl-3-selenopentanedione-1,5 (preparation DAPS-25), 1,5-di(4-methoxyphenyl)-3-selenopentanedione-1,5 and 1,5-di(4-ethoxyphenyl)-3-seleno- pentanedione-1,5 molecules has been studied. The above molecules have been stated to be substantially similar to each other by their electronic and spatial characteristics. By means of the QSAR properties evaluation by the atomic-additive schemes, it has been shown that the molecules of the preparation DAPS-25, its dimethoxy- and diethoxy-substituted are close to each other by the hydrophilic-lipophilic balance, whereas di-n,-octoxy derivative DAPS-25 is explicitly hydrophobic. The hemagglutinating activity of lectins in the presence of the preparation DAPS-25 and its alkyloxy-substituted increases, therewith the most effective addition is 1,5-di(4-ethoxyphenyl)-3-selenopentanedione-1,5. Apparently, the greater effectiveness of the said substance compared to DAPS −25 is caused by the formation of hydrogen bonds with a participation of unshared electron pairs of oxygen atoms from the ethoxy groups and mobile hydrogen atoms from the OH groups of glycoconjugates on erythrocytes surface. The positive effect of 1,5-di(4-n-octoxyphenyl)-3-selenopentanedione-1,5 is not so prominent, since the enlarged alkyl chain shields the aromatic fragments of organoselenium molecule participating in the binding with lectin.

Antifungal and antibacterial activities of lectin from the seeds of Archidendron jiringa Nielsen

A Archidendron jiringa Nielsen lectin was purified by aqueous extraction, 90% ammonium sulphate precipitation and concanavalinA-Sepharose 4B affinity chromatography. Its specific activity was of 88.3×102 hemagglutination unit/mg protein for a yield of 51.6% total protein. The molecular weight is of 35.7kDa. It has hemagglutinating activity against human blood group, rabbit, mouse, rat, guinea pig, geese and sheep erythrocytes. The hemagglutination activity of lectin was relatively insensitive to acidic pH above 2, had an optimal activity at pH 8, and stable below 45°C for 30min. The activity was stimulated by Ca2+, Mg2+ and Mn2+. The internal sequence indicated similarity with legume lectin family. Moreover, even at low concentrations antifungal activity was observed against Exserohilum turcicum, Fusarium oxysporum and Colletotrichum cassiicola. The minimal inhibitory concentrations were 0.227, 0.0567 and 0.0567mg/ml for Bacillus subtilis, Staphylococcus aureus, and Candida albicans, respectively.

Purification, characterization and toxicity of a mannose-binding lectin from the seeds of Treculia africana plant

In this study, a mannose-specific, homodimeric lectin from the seeds of Treculia africana was purified, characterized and its adverse effects were investigated in mice. The purification protocol involved anionic exchange chromatography on DEAE-Cellulose followed by gel filtration on Sephadex G-100. The hemagglutinating activity of lectin towards human erythrocytes was sensitive to inhibition by D-mannose. Treatment of the protein with EDTA exerted no inhibitory effect; however, analysis of metal content by atomic absorption spectroscopy revealed the presence of Cu2+, Fe3+, and Mg2+. The results obtained showed that the lectin possesses maximum hemagglutinating activity towards human erythrocytes activity over the pH range 3–7.2 and is relatively thermostable up to 50°C. Periodic acid Schiff's (PAS) reagent staining showed that the protein was non-glycosylated while its amino acid composition analysis revealed that the protein contained 155 residues per subunit. The subunit had a minimal molecular weight of 22,139 Daltons, while the native molecular weight was estimated to be 41,000 Daltons. The lectin was found to be moderately toxic to mice with an LD50 of 47.21 µg g−1 body weight while, histopathological analysis showed no treatment related effects in any of the organs examined.

What Is The New and Sensitive Tumor Marker for Detection of Different Kidney Tumors? Modern Study to Isolation, Purification and Characterization of N-Acetyl Galactosamine Binding Lectin From Sera Of Patients With Kidney Cancer

The present study was designed to investigate lectins in sera of patients with kidney tumors, in addition to non tumoral kidney disease patients. Fifty five patients of malignant kidney tumors were enrolled in addition to 23 patients of benign kidney tumors, and 18 patients of non tumoral kidney diseases used as control groups, in addition to 46 healthy individuals were also investigated. The age of patients and healthy individuals were 10-90 years. The measurement of total serum proteins revealed significant (p &lt; 0.001) decrease in patients of malignant tumors when compared with those of benign, non tumoral diseases, and healthy individuals. The conditions of the hemagglutination assay of serum lectin activity were optimized. They were Tris buffer of 20 mM and pH 7.4, 60 mM CaCl2, 800 µg of defatted serum, 30 ˚C for serum samples, 60 minutes for serum samples, and human blood of group A+ suspension with 1.4 optical density. The measurement of the specific hemagglutination activity of lectins demonstrated significant (p &lt; 0.001) elevation in patients of malignant tumors when compared with those of other patients and healthy individuals. Lectin activity was pointed out to be significantly (r = 0.767 at p &lt; 0.0005) positively correlated with stage of malignancies. The cutoff value of the specific hemagglutination activity was found to equal 6 SHU for discriminatory malignant kidney tumors. Serum lectins activity were indicated to be inhibited by galactose, mannose, lactose, and N-acetyl galactosamine. Purification of lectin from sera of patients with malignant kidney tumors by affinity chromatography with the use of silver stain revealed N-Acetyl Galactosamine Binding Lectin (GalNAcBL). The purified folds and the yield was 178 with 32.4%. The polyacrylamide gel electrophoresis (PAGE) of purified lectin demonstrated one band consisted lectin activity. The approximate molecular weight of GalNAcBL was determined and found to be 63.83. Purified lectin was characterized through the assessment of the capability to agglutinate RBCs, inhibition by EDTA, pH dependency, thermal dependent, and carbohydrate contents. GalNAcBL were observed to be calcium dependence lectins (C-type). These results suggest that the diagnosis of the specific hemagglutination activity of lectin is promising biomarker for discrimination of malignant kidney tumor patients and the purified lectin could be introduced in the field of biomarkers.

The effect of sugars and free amino acids from the freshwater prawn Macrobrachium rosenbergii hemolymph on lectin activity and on oxidative burst

We determined the effect of low molecular weight components (LMWC) from healthy juvenile and adult Macrobrachium rosenbergii hemolymph on lectin activity and oxidative burst (OB) in hemocytes. In an attempt to identify the LMWC that affect the lectin's hemagglutinating activity or oxidative burst, we determined the hemolymph carbohydrates and free amino acids (FAA) concentration. The LMWC (<2000 Da) were obtained after dialysis of the hemolymph. Our results showed that LMWC from juveniles exerted a greater inhibition on lectin than LMWC from adult hemolymph. Production of superoxide radicals by hemocytes was lower in the presence of juvenile (p<0.05) as compared to adult LMWC. FAA composition of the hemolymph and of LMWC from adults showed higher proportion of alanine (which corresponded to 25% of total FAA) and proline (>20%); whereas, in juveniles, the main FAA identified were glycine (>40%) and alanine (26%). N-Acetyl-d-glucosamine (GlcNAc) was the main sugar residue in the hemolymph and LMWC from juveniles; its concentration was 2.4 times higher than glucose (Glc), whereas, in adults, Glc was the main free sugar residue. Our results suggest that the proportion of FAA and carbohydrates in the hemolymph of M. rosenbergii seems to be correlated with the maturation process; furthermore, the high proportion of free GlcNAc and glycine regulate, in the juvenile stage, lectin activity and cellular oxidative mechanisms, respectively.

Proteolytic activity of lectins from the nitrogen-fixing bacterium Bacillus polymyxa

Two lectins (LI and LII) stripped from the surface of Bacillus polymyxa 1460 cells were found to possess proteolytic activity, which was associated with their hemagglutinating activity. The inhibition of the hemagglutinating activity of lectins by specific carbohydrate haptens changed their enzyme activities. The inhibition of hemagglutinating activity by glucuronic acid or fructose 1,6-diphosphate decreased the proteolytic activities of both lectins, whereas the blocking of this activity with D-glucosamine or D-galactosamine increased the proteolytic activity of LII. The molecules of the B. polymyxa lectins are suggested to contain two active centers responsible for hemagglutinating and proteolytic activities.

Isolation and characterization of lectins from stem and leaves of Korean mistletoe (Viscum album var.coloratum) by affinity chromatography

We attempted to isolate and characterize the lectins from stem and leaves of Korean mistletoe (Viscum album var.coloratum) by affinity chromatography. Lectin I was isolated only from stem. Lectin II was not isolated from Korean mistletoe, whereas lectin III was isolated from the stem and leaves. The hemagglutinating activity of lectin I was 16HU and inhibited by D-galactose, lactose, and N-acetyl-D-galactosamine. The lectin I has molecular weight of 60,000D being composed of two basic subunits with molecular weights of 32,000 D and 28,000 D which are linked by a disufide bond. The lectin III from stem has molecular weight of 66,000D being two basic subunits which have molecular weights of 34,000D and 29,000D and are linked by a disufide bond. The activity of lectin I was stable at the pH range of 4.00 approximately 8.50, and at a wide range of temperature (0 approximately 42 degrees C). The lectin I showed more potent mitogenic activity to murine lymphocytes than concanavalin A.

Further biochemical and biophysical characterisation of scyllin, Scylla serrata hemolymph lectin.

The amino acid and carbohydrate analysis of scyllin, a low molecular weight lectin purified from Scylla serrata (edible crab) haemolymph reveal that scyllin is rich in acidic and neutral amino acids and contains high amount of mannose. UV absorption of scyllin is perturbed by DMSO at 272 nm showing the presence of tryptophan molecule in scyllin exposed and accessible to the solvent. The oxidation of tryptophan molecule by N-bromosuccinimide results in loss of haemagglutinating activity of lectin. The study of thermodynamic parameters of scyllin-glycoproteins interaction suggests that ceruloplasmin is the most potent inhibitors of scyllin of all the glycoproteins studied.

Isolation and characterization of a soluble lactose‐binding lectin from postnatal chicken retina

We investigated the presence of endogenous lectins in postnatal chicken retinal tissue assaying the hemagglutinating activity of crude soluble extracts of the tissue that was homogenized in a buffer supplemented with different sugars. Lactose was the most effective sugar to extract an hemagglutinating activity. Using similar extraction conditions, other sugars, such as glucose, N-acetylglucosamine, mannose, fucose, glucuronic and sialic acid, were ineffective to extract any significant hemagglutinating activity. The lectin was purified by affinity chromatography on lactosyl-Sepharose. SDS-PAGE and isoelectric focusing analyses showed that it has a subunit molecular weight of 16 kDa and a pI about 4.5. The retinal lectin cross-reacted immunologically with a rabbit antiserum raised against a lectin purified from adult chicken liver, which is a CLL-I (Beyer et al.: J Biol Chem 255:4236-4239, 1980) or C-16 (Sakakura et al.: J Biol Chem 265:21573-21579, 1990) form of chicken endogenous soluble lactose-binding lectins. Gel filtration studies showed that the oligomeric structure of the retinal lectin is dependent on the ionic strength of the elution buffer. The lectin hemagglutinating activity and the amount of lectin protein reached their highest levels at late developmental stages of the retinal tissue, suggesting that retinal lectin might have a functional role during terminal differentiation of retinal cells.