Human Ovarian Cyst Fluids Research Articles

Optimized derivative fast Fourier transform with high resolution and low noise from encoded time signals: Ovarian NMR spectroscopy

The unfiltered derivative fast Fourier transform (dFFT) of degrees higher than two fails flagrantly for encoded time signals. These data are always dominated by noise at larger times of encodings. Such a breakdown is due to processing the unweighted product of the time signal and the time power function. The latter is generated by the frequency derivative operator applied to the fast Fourier transform (FFT). As a result, the unfiltered dFFT cannot separate the overlapped resonances and it dramatically decreases signal-to-noise ratio (SNR) relative to the FFT. This problem is solved by a derivative-adapted optimization with the properly attenuated filters. The ensuing optimized dFFT achieves the long sought simultaneous enhancement of both resolution and SNR. It uncovers the genuine resonances hidden within overlapping peaks to enable quantitative interpretations. It does not impose any model on the input time signals nor on the output lineshape in the spectra. It is computationally expedient as it uses the Cooley-Tukey fast algorithm. The present applications deal with time signals encoded by in vitro NMR spectroscopy from human malignant ovarian cyst fluid. A remarkably successful performance of the optimized dFFT is demonstrated for reconstructed spectra of potentially added value in clinical decision-making.

Glycan structures and their recognition roles in the human blood group ABH/Ii, Lea, b, x, y and Sialyl Lea,x active cyst glycoproteins.

Human ovarian cyst glycoproteins (HOC, cyst gps) isolated from pseudomucinous type of human ovarian cyst fluids is one of the richest and pioneer sources for studying biosynthesis, structures and functional roles of blood group ABH, Lea,b,x,y, sLea and sLex active glycoproteins. After 70+ years of exploration, four top highlights are shared. (i) an updated concept of glycotopes and their internal structures in cyst gps was composited; (ii) the unknown codes of new genes in secreted cyst gps were unlocked as Lex and Ley; (iii) recognition profiles of cyst glycans and a sialic acid-rich (18%) glycan with lectins and antibodies were shown. (iv) Co-expression of Blood Group A/ A-Leb/y and B/B-Leb/y active Glycotopes in the same glycan chains were isolated and illustrated. These are the most advanced achievements since 1980.

Identification of blood group A/A‐Leb/y and B/B‐Leb/y active glycotopes co‐expressed on the O‐glycans isolated from two distinct human ovarian cyst fluids

Although the individual human blood group A and B determinants are well defined, their co-expression pattern on a particular glycan carrier in individuals of blood group AB status has not been delineated. To address this issue, complex O-glycans were isolated from two distinct sources of human ovarian cyst glycoproteins (HOC 89 and Cyst 19) and profiled by advanced MS analyses, in conjunction with defining their binding characteristics against a panel of lectins and monoclonal antibodies. The major O-glycans of HOC 89 were found to correspond to sialyl Tn, mono- and di-sialyl T structures, whereas those of Cyst 19 were apparently more heterogeneous and extended to larger sizes. A minimal structure that carries both A and B determinants on the same molecule was identified, in which the A epitope is attached directly to the core GalNAc, whereas the B epitope is preferentially located on the six arms of a core 2 structure. Both arms can be further extended with internal fucosylation that appears to be restricted to those non-sialylated chains already carrying the terminal ABH determinants, thus giving rise to rather prominent A/B-Le(b/y) glycotopes on larger O-glycans.

Carbohydrate specificity of an agglutinin isolated from the root of Richosanthes kirilowii

The root of Trichosanthes kirilowii, which has been used as Chinese folk medicine for more than two thousand years, contains a Gal specific lectin (TKA). In order to elucidate its binding roles, the carbohydrate specificities of TKA were studied by enzyme linked lectinosorbent assay (ELLSA) and by inhibition of lectin-glycoform binding. Among glycoproteins (gp) tested, TKA reacted strongly with complex carbohydrates with Galβ1 → 4GlcNAc clusters as internal or core structures (human blood group ABH active glycoproteins from human ovarian cyst fluids, hog gastric mucin, and fetuin), porcine salivary glycoprotein and its asialo product, but it was inactive with heparin and mannan (negative control). Of the sugar inhibitors tested for inhibition of binding, Neu5Acα2 → 3/6Galβ1 → 4Glc was the best and about 4, 14.6 and 27.7 times more active than Galβ1 → 4GlcNAc(II), Galβ1 → 3GalNAc(T) and Gal, respectively. From these results, it is suggested that this agglutinin is specific for terminal or internal polyvalent Galβ1 → 4GlcNAcβ1→, terminal Neu5Acα2 → 3/6Galβ1 → 4Glc and cluster forms of Galβ1 → 3GalNAcα residues. The unusual affinity of TKA for terminal and internal Galβ1 → glycotopes may be used to explain the possible attachment roles of this agglutinin in this folk medicine to target cells.

MUC-6 mucin is a major component of ‘blood group substance’ from human ovarian cyst fluid

Ovarian cyst fluid has been a valuable source of the mucins (traditionally termed ‘blood group substances’) that were used for the elucidation of the structures of the ABO Lewis blood group determinants, but the identity of the mucin peptide core(s) carrying these carbohydrate specificities is not known. An ovarian cyst fluid mucin was purified, deglycosylated with HF and digested with trypsin or chymotrypsin to yield a number of peptides. Amino acid sequencing of these peptides yielded five different sequences which showed complete or partial homology to the MUC-6 apomucin deduced from DNA sequencing. As no other sequences were identified, it is concluded that MUC-6 is the major mucin core structure of ovarian cyst fluid mucin.

Synthesis of Oligosaccharides Designed to form Micelles, Corresponding to Structures Found in Ovarian Cyst Fluid

ABSTRACT The syntheses of α-D-GlcpNAc-(1→4)-β-D-Galp-(1→4)-β-D-GlcNAc-(1→O)-(CH2)15CH3 (1) and fragments thereof, corresponding to structures found in human ovarian cyst fluid, are described. Silver triflate promoted coupling of 3,4,6-tri-O-acetyl-2-azido-2-deoxy-β-D-glucopyranosyl bromide (12) and galactose acceptor (11) gave a disaccharide donor (13), which was readily transformed into the corresponding bromo-derivative 18. For the synthesis of disaccharide β-D-Galp-(1→4)-D-GlcNAc, several differently protected glucosamine acceptors were prepared. It was found that cetyl alcohol needed to be introduced after the formation of the β-galactoside bond. Glycosylation of pent-4-enyl 3,6-di-O-benzyl-2-deoxy-2-tetrachlorophthalimido-β-D-glucopyranoside (30) with (3,4,6-tri-O-acetyl-2-azido-2-deoxy-α-D-glucopyranosyl)-(1→4)-2,3,6-tri-O-benzoyl-α-D-galactopyranosyl bromide (18) by use of silver triflate as promoter gave the desired trisaccharide 31. Finally 31 was transformed via coupling to the long alkyl chain aglycon and deprotection into the title compound 1.

Binding properties of a blood group Le(a +) active sialoglycoprotein, purified from human ovarian cyst, with applied lectins

Studies on the structures and binding properties of the glycoproteins, purified from human ovarian cyst fluids, will aid the understanding of the carbohydrate alterations occurring during the biosynthesis of blood group antigens and neoplasm formation. These glycoproteins can also serve as important biological materials to study blood group A, B, H, Le a, Le b, Le x, Le y, T and Tn determinants, precursor type I and II sequences and cold agglutinin I and i epitopes. In this study, the binding property of a cyst glycoprotein from a human blood group Le(a +) nonsecretor individual, that contains an unusually high amount (18%) of sialic acid (HOC 350) was characterized by quantitative precipitin assay with a panel of lectins exhibiting a broad range of carbohydrate-binding specificities. Native HOC 350 reacted well only with three out of nineteen lectins tested. It precipitated about 80% of Ricinus communis (RCA 1), 50% of Triticum vulgaris (WGA) and 37% of Bauhinia purpurea aba (BPA) agglutinins, respectively. However, its asialo product had dramatically enhanced reactivity and reacted well with many I/II (Gal β1 → 3 /4GcNAc), T (Gal β1 → 3GalNAc) and Tn (GaNlAc α 1 → Ser/Thr) active lectins. It bound best to Jacalin, BPA, and abrin-a and completely precipitated all the lectins added. Asialo-HOC 350 also reacted strongly with Wistaria floribunda, Abrus precatorius agglutinin, ricin and RCA 1 and precipitated over 75% of the lectin nitrogen added, and moderately with Arachis hypogaea, Maclura pomifera, WGA, Vicia viosa-B4, Codium fragile tomentosoides and Ulex europaeus-II. But native HOC 350 and its asialo product reacted not at all or poorly with Dolichos biflorus, Helix pomatia, Lotus tetra-gonolobus, Ulex europaeus-I, Lens culinaris lectins and Con A. The lectin-glycoform interactions through bioactive sugars were confirmed by precipitin inhibition assay. Mapping the precipitation profiles of the interactions have led to the conclusion that HOC 350 contains a large number of receptors for I/II, T, and Tn active lectins. But in the untreated (or native) substance, most of these determinants are masked by sialic acids.

Affinity of Bandeiraea (Griffonia) simplicifolia Lectin-I, Isolectin-B4 (BSI-B4) for Galα1→4Gal Ligand

The affinity of Bandeiraea (Griffonia) simplicifolia lectin-I isolectin B-4 (BSI-B-4) for the isomer of human blood group B active disaccharide (B, Galα1→3Gal), the Galα1→4Gal galabiose ligand, was studied by quantitative precipitin(QPA) and precipitin-inhibition assays. When human blood group B, P1 and H active glycoproteins were tested by QPA. BSI-B4 reacted strongly with both the B active glycoprotein purified from human ovarian cyst fluid and a P1 active glycoprotein isolated from sheep hydatid fluid and precipitated over 86% of the lectin nitrogen added. The P1 active glycoprotein-BSI-B4 interaction was inhibited by both Galα1→3Galα1→methyl and Galα1→4Gal disaccharide indicating that BSI-B4 is not only reacting with Gal α1→3Gal disaccharide, but also recognizing Galα1→4Gal. The galabiose sequence is frequently found in the carbohydrate chains of many glycosphingolipids located at the mammalian cell membranes such as intestinal and red blood cell membranes, for E. coli ligand binding and toxin attachment.

Serous ovarian cyst fluids contain high levels of endometrial placental protein 14.

This paper reports the detection and characterization of endometrial placental protein 14 (PP14) in human ovarian cyst fluids. PP14 from ovarian cyst fluid has the same molecular size as PP14 purified from human amniotic fluid. No clear difference was found in the PP14 concentrations between benign, borderline and malignant cyst fluids, but serous ovarian cyst fluids had significantly higher PP14 concentrations (median 253.3 micrograms/l) than mucinous cyst fluids (median 17.5 micrograms/l).

Biochemical characterization of glycoprotein components in human ovarian cyst fluids by lectins

1. 1. Perchloric acid-soluble glycoprotein fractions (PASFs) were separated, in yields of 180 ~ 610 mg per 100 ml of cyst fluid, from the cyst fluids of human ovarian cystadenomas (OCAs) in benign and borderline and ovarian clear cell carcinoma (OCC) in malignant, and then identified as glycoproteins with 19.1 ~ 69.5% carbohydrate by their chemical composition analyses. 2. 2. These PASFs reacted with anti-A, -B, -Le a and /or -Le b sera, but did not react with anti-H, -M and -N sera. All of the PASFs reacted with Ricinus communis lectin (RCA-I). Among these PASFs, PASFs from the cyst fluids of OCA in benign did not react with Arachis hypogaea anti-T lectin (PNA) and both of the anti-N lectins of Vicia graminea (VGA) and Vicia unijuga (VUA), and PASFs from OCA in borderline reacted with only PNA and PASFs from OCC in malignant reacted with the three lectins, PNA, VGA and VUA. However, none of PASFs from human normal sera and various normal organ tissues reacted with any of RCA, PNA, VGA and VUA. 3. 3. The above-mentioned results seem to show that the examination of glycoproteins of ovarian cyst fluids by the combined use of RCA-I, PNA and VGA (or VUA) permits biochemical diagnosis of the canceration degree of ovarian cystomas.

Structural concepts of the human blood group A, B, H, Le(a), Le(b), I and i active glycoproteins purified from human ovarian cyst fluid.

Regardless of the A, B, H, Le(a), Le(b), I and i activity, purified water-soluble blood group glycoproteins from human ovarian cyst fluid have a similar overall structure. They are polydisperse macromolecules (Mr 2.0 x 10(5) to several million) of similar composition (75 to 85% carbohydrate, 15 to 20% protein) and consist of multiple heterosaccharide side chains attached by an O-glycosidic linkage at their internal reducing ends to serine or threonine of the polypeptide backbone. About 90% of these carbohydrate side chains range in size from one to less than twenty-four sugar residues (twelve sugars in the internal structure and twelve key sugars specific as blood group determinants). Three-fourths of these side chains contain fewer than twelve sugars. A generalized blood group active carbohydrate chain is shown above. Three disaccharide units-Type I chain (Gal beta 1----3GlcNAc beta 1----3), Type II chain (Gal beta 1----4GlcNAc beta 1----6) and T determinant [Gal beta 1----3GalNAc alpha 1----Ser(Thr)]-are used to elucidate the internal structure of the carbohydrate chains. The complete internal structure is considered to have a core structure with four branches, to which the blood group key sugars are attached at the appropriate locations. The core structure is a tetrasaccharide, composed of one unit of Type I chain at the nonreducing end and the T determinant at the other end, linked to Ser or Thr of the protein moiety. Branch I is Type I chain and Branch II is Type II chain. They are linked to Gal at the nonreducing end of the core structure. Branch III is usually a Type II chain, but may sometimes be a Type I chain, linked to the GalNAc of the reducing end. The length of Branch III can be increased by adding one or more monosaccharides of Type I chain sequence such as Gal beta 1----3GlcNAc beta 1----3Gal beta 1----4GlcNAc beta 1----6GalNAc alpha 1----Ser(Thr), a combination of Type I and Type II chains. A new Branch IV is made up of Type II chain, which in turn is linked to the Gal end of the T determinant. The Type II chains react with the antibody to the type XIV pneumococcal capsular polysaccharide and with the anti-I(Ma) cold agglutinin.(ABSTRACT TRUNCATED AT 400 WORDS)

Immunochemical studies on blood groups. Purification and characterization of radioactive 3H-reduced di- to hexasaccharides produced by alkaline beta-elimination-borohydride 3H reduction of Smith degraded blood group A active glycoproteins.

Treatment of blood group A active glycoprotein from human ovarian cyst fluid by one stage of Smith degradation followed by alkaline beta-elimination in the presence of NaB[ 3H4 ] (Carlson degradation) liberated tritiated oligosaccharide alditols. The carbohydrate mixture was fractionated by gel filtration, elution from charcoal, paper chromatography, and high pressure liquid chromatography. Structures were established based on sugar composition, periodate oxidation, methylation analysis, and analysis of oligosaccharide alditols as permethylated and N-trifluoroacetylated derivatives by gas-liquid chromatography-mass spectrometry. The following structures have been deduced: Gal beta 1----3GalNAc-ol, GlcNAc beta 1---- 6GalNAc -ol, Gal beta 1---- 3GlcNAc beta 1----6(3-deoxy)GalNAc-ol, Gal beta 1---- 3GlcNAc beta 1---- 6GalNAc -ol, Gal beta 1----4GlcNAc beta 1---- 6GalNAc -ol, GlcNAc beta 1----3Gal beta 1----3GalNAc-ol, Gal beta 1----3[GlcNAc beta 1----6]GalNAc-ol, Gal beta 1----3[Gal beta 1----4GlcNAc beta 1----6]GalNAc-ol, Gal beta 1---- 3GlcNAc beta 1----3Gal beta 1----3GalNAc-ol, GlcNAc beta 1----3Gal beta 1----4GlcNAc beta 1---- 6GalNAc -ol, GlcNAc beta 1----3Gal beta 1----3[Gal beta 1----4GlcNAc beta 1----6]GalNAc-ol, Gal beta 1---- 3GlcNAc beta 1----3Gal beta 1---- 3GlcNAc beta 1----3Gal beta 1----3Gal beta 1----3GalNAc-ol, Gal beta 1---- 3GlcNAc beta 1----3[Gal beta 1----4GlcNAc beta 1----6]Gal beta 1----3GalNAc-ol, Gal beta 1---- 3GlcNAc beta 1----3Gal beta 1----3[Gal beta 1----4GlcNAc beta 1----6]GalNAc-ol. The smaller structures represent pieces of the larger structures. Together they provide direct evidence for the core structure of the carbohydrate side chains in the blood group substances as proposed by K. O. Lloyd and E. A. Kabat [1968) Proc. Natl. Acad. Sci. U.S.A. 61, 1470-1477). Oligosaccharides previously isolated after Carlson degradation of intact human ovarian cyst fluid HLeb , Lea, and B substances and from human and horse B substances contained various alpha-linked L- fucopyranose and alpha-linked Gal substitutions on the composite structure.(ABSTRACT TRUNCATED AT 400 WORDS)

Natural antibodies in human sera directed against blood‐group‐related determinants expressed on colon cancer cells

Sera from 136 normal males and 33 members of families at high risk for colon cancer were tested for reactivity with six colon cancer cell lines by the protein A-mixed hemadsorption assay. Ninety-one sera had antibodies to colon cancer cell line HT-29. In 89 cases the antibodies were absorbed by human A and B erythrocytes or sheep erythrocytes. Antibodies in the remaining two sera, which were from sisters in the high-risk group, were not absorbed by red cells but could be absorbed by tumor cells expressing A or B blood-group determinants. Their reactivity was inhibited by some soluble blood-group glycoproteins. One serum (No. 4) was inhibited by A-active glycoproteins from human saliva and ovarian cyst fluids and from porcine mucosa, as well as by a polysaccharide derived from gastric cancer; it has an anti-A-like specificity. The other serum (No. 6) was inhibited by A and B glycoproteins, by a blood group precursor glycoprotein and by the same gastric cancer polysaccharide; it seems to have a wider specificity directed towards both A- and B-like structures. It is not known what caused production of these antibodies but it may be significant that they occurred in members of a family at high risk for developing colon cancer.

Partial deglycosylation of blood-group-specific glycoproteins

The time course for the partial deglycosylation of blood-group-specific glycoproteins from human ovarian-cyst fluids with 0.25 M-H2SO4/acetic acid and 6 M-HCl in methanol was studied. Either reagent readily removed about 80% of the carbohydrate from the glycoproteins to leave non-diffusible glycopeptides that contain N-acetylgalactosamine as the predominant sugar. Some changes in amino acid distribution were observed during the deglycosylation, which were attributed to an accelerated break-up of the nonglycosylated regions of the parent glycoprotein. The N-acetylgalactosaminyl-peptides isolated were judged to be polydisperse by gel filtration, and ion-exchange chromatography divided the glycopeptide population into several fractions with differing amino acid compositions. A Lumbricus terrestris hexosaminidase preparation was successful in removing almost all the remaining sugar from the glycopeptides, but caused further rupture of the peptide. When a per O-acetylated glycoprotein was treated with the H2SO4/acetic acid reagent the glycopeptide contained, in addition to N-acetylgalactosamine, about 50% of the sialic acid present in the parent glycoprotein, indicating that most of this sugar is located near the peptide end of the carbohydrate chains.

Changes of Serological Activity by α-L-Fucosidase Isolated from Streptococcus sanguis ATCC 10557

alpha-L-Fucosidase isolated from the growth culture of Streptococcus sanguis ATCC 10557 acted on H- and Leb-blood group substances in porcine gastric lining, human gastric lining, human ovarian cyst fluid and human whole saliva, with consequent loss of H- and Leb -activities and a concomitant increase of Lea activity.

STUDIES ON SECRETOR SPECIFIC ACTIVE SITE H (Se) OF HUMAN WATER-SOLUBLE BLOOD GROUP SUBSTANCE

1. Blood group H activity against chicken and eel anti-H agglutinins of H substances from human stomach mucosa and ovarian cyst fluid was destroyed by partial alkaline hydrolysis with aqueous methanolic triethylamine. The triethylamine treated H substances lost H(Se) activity against eel anti-H(Se) preicpitin and Leb activity by partial acid hydrolysis with hydrochloric acid.2. Three oligosaccharides were isolated from the triethylamine hydolysis products of a H substance from human ovarian cyst. H active and fucose-containing trisaccharide was characterized as α-Fuc-(1→2)-β-Gal-(1→4)-GlcNTAc, which had type II chain.3. Application of the hydrochloric acid to the partial hydrolysis of the H(Se) substance resulted in the liberation of H (Se) active sugar-peptides. Five oligosaccharides were isolated from the sugar-peptide pool by the treatment of alkaline sodium borohydride. Pentasaccharide containing a- (1→2) -fucosyl residue was characterized as a-Fuc-(1→2)-β-Gal-(1→3)-β-GlcNAc-(1→4)-β-Gal(1→3)-GalNAc, which had type I chain. The pentasaccharide with a β- (1→4) -linkage between N-acetylglucosamine and galactose has not been found in fucose containing oligosaccharides previously isolated and characterized from human blood-group substances. The pentasaccharide did not inhibit the precipitation of anti-H(Se) eel serum but inhibited the agglutination of eel and chicken anti-H. The serological results indicated that the H (Se) activity of the pentasaccharide structure displayed in sugar-peptide or H substance, and eel and chicken anti-H agglutinins could not differentiate α-Fuc-(1→2)-Gal structure of type I and type II oligosaccharides.

A study of the specificity of Bandeiraea simplicifolia lectin I by competitive-binding assay with blood-group substances and with blood-group A and B active and other oligosaccharides

The specificity of Bandeiraea simplicifolia lectin 1 (BS I) has been studied by competitive-binding assays (CBA) using tritium-labeled human B and hog A substances. Blood-group B substances isolated from horse gastric mucosae and from human ovarian-cyst fluids were much better inhibitors of binding of tritiated blood-group B substance to insoluble BS I-Sepharose 2B than were human blood-group A substances from saliva and ovarian-cyst fluid. A and B active blood-group substances showed the same range of potency in inhibiting binding of tritium-labeled hog A substance to BS I-Sepharose 2B. CBA with BS I-Sepharose 2B, labeled human blood-group B substance, and human blood-group A and B active oligosaccharides separated the haptens into two groups differing in slope. Group 1, containing methyl α- d-GalNAc p, d-GalNac p, and an A active pentasaccharide AR L 0.52, with 3, 19, and 25 nmol respectively needed for 50% inhibition of binding, has a lower slope than group 2, which contains α- d-GalNAc p-(1→3)-2-acetamido-2-deoxy- d-galactitol and p-nitrophenyl α- d-GalNAc p, with 3 nmol of each required for 50% inhibition of binding, as well as ten glycosides with terminal, nonreducing, α-linked d-Gal p. The most potent inhibitors of this group were p-nitrophenyl α- d-gal p, α- d-Gal p-(1→3)- d-Gal p, α- d-Gal p-(1→6)- d-Glc p, and methyl α- d-Gal p, with 5, 7.4, 9.6, and 11 nmol respectively needed to inhibit binding by 50%. The difference in slopes was explainable in terms of a recent finding that BS I exists as a mixture of five isolectins composed of two subunits having different specificities; subunit A is most specific for α-linked, terminal, nonreducing d-GalNAc p, but it also reacts with α-linked, terminal, non-reducing d-Gal p, whereas subunit B tends to be more specific for terminal, nonreducing, α-linked d-Gal p.

STUDIES ON SECRETOR SPECIFIC H (Se) ANTIGEN OF WATER SOLUBLE BLOOD GROUP SUBSTANCES

The presence of two precipitins against blood group H substances from human gastric linings and ovarian cyst fluids was demonstrated in natural eel serum by immunodiffusion techniques in agal gel. One of them which form the precipitation band to antigen side was the known anti-H precipitin containing anti-H agglutinin activity. Reaction of the anti-H precipitin with H substance was inhibited by L-fucose. This anti-H precipitin reacted well with H substance from hog gastric linings but did not show clear precipitation bands with H substances from saliva, meconium, semen and intestines. The other precipitin which form the precipitation band to antiserum side in agar gel reacted well with H substances from human secretions and tissues but not reacted with hog H substances from gastric linings and submaxillary gland. This precipitin did not agglutinate O red cells and was not absorbed by O red cells. The reaction of the precipitin with H substances was not inhibited by L-fucose. Because this precipitin reacted with water soluble H substances from human “secretor”, the antigen named H (Se) and antibody anti-H (Se).

Antigens common to human ovarian mucinous cyst fluid and gastric mucosa

Ovarian mucinous cysts, but not ovarian cysts of other histological types, contain common antigens with normal gastric mucosa. By immunodiffusion, antigens of both extracts give identical reactions. Immunofluorescence experiments localize these antigens in the epithelial coat of ovarian mucinous cysts and in the mucous cells of the surface epithelium of the fundic and pyloric gastric mucosa.

Inhibitory effect of alpha-globulins of different origin on the cell-mediated immune responses in mice.

alpha-Globulins prepared from different biological sources (human and bovine sera, mouse ascitic fluid, human ovarian cyst fluid) were separated by ion exchange chromatography on DEAE-cellulose into fractions A, B and C. Whereas fractions A and B had no immunosuppressive activity, fraction C injected into mice shortly before antigen administration, but not after, significantly inhibited the contact sensitivity to oxazolone. Single high doses were preferential over divided doses given on several occasions. In transfer experiments when cells of animals sensitized to oxazolone were injected into recipients treated previously with fraction C, the response was also inhibited. Fraction C, when administered into F1 hybrid mice before injection of parental splenocytes, prevented the development of GVH reaction. The authors point out that the critical concentration of alpha-globulins at the time of antigen administration is necessary to make T-lymphocytes hyporesponsive, and when once triggered by antigen they become refractory to alpha-globulins action.