Quantitative Determination Of Proteins Research Articles

Quantitative determination of several pleural fluid proteins.

Quantitative determination of several pleural fluid proteins.

Radioactive labeling of protein in vitro by acetylation with 14C- N-(acetoxy)-succinimide. A new method for quantitative determination of protein in the presence of polynucleotides

FEBS LettersVolume 22, Issue 1 p. 89-90 Full-length articleFree Access Radioactive labeling of proteinin vitro by acetylation with14C-N-(acetoxy)-succinimide. A new method for quantitative determination of protein in the presence of polynucleotides V.P. Demushkin, V.P. Demushkin Shemyakin Institute for Chemistry of Natural Products, USSR Academy of Sciences, Moscow, USSRSearch for more papers by this authorE.I. Budowsky, E.I. Budowsky Shemyakin Institute for Chemistry of Natural Products, USSR Academy of Sciences, Moscow, USSRSearch for more papers by this author V.P. Demushkin, V.P. Demushkin Shemyakin Institute for Chemistry of Natural Products, USSR Academy of Sciences, Moscow, USSRSearch for more papers by this authorE.I. Budowsky, E.I. Budowsky Shemyakin Institute for Chemistry of Natural Products, USSR Academy of Sciences, Moscow, USSRSearch for more papers by this author First published: April 15, 1972 https://doi.org/10.1016/0014-5793(72)80226-6Citations: 5AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL No abstract is available for this article. References 1 R.W. Helmkamp, M.A. Contreras, W.F. Bale, Int. J. Appl. Radiat. Isotopes, 18, (1967), 737. 2 R.H. Riese, G.B. Means, J. Biol. Chem., 246, (1971), 831. 3 V.P. Demushkin, O.D. Nelidova, E.I. Budowsky, Molekul. Biol., 5, (1971), 858. 4 S. Gutsho, Biochim. Biophys. Acta, 157, (1968), 76. 5 I. Gillam, D. Blew, R.C. Warrington, Biochemistry, 7, (1968), 3459. 6 S. Nishimura, G.D. Novelli, Biochim. Biophys. Acta, 80, (1964), 547. Citing Literature Volume22, Issue1April 15, 1972Pages 89-90 ReferencesRelatedInformation

Single Radial Immunodiffusion of Undiluted Serum Proteins

Abstract A simple method is described for quantitative determination of IgG, IgA, IgM, α2M, and other proteins without dilution of the sample. Strips of gelatinized cellulose acetate spread with antiserum are used as a supporting medium. The method is accurate, highly reproducible, and seems particularly suitable for routine work because it permits determination of hypo-, normal, and hyperglobulinemia on a single strip.

Quantitative determination of individual serum proteins by radio-electroimmuno and use of 125 I-labelled antibodies (application to C-reactive protein).

The sensitivity of quantitative electrophoresis into agarose gel containing antibodies was increased about 60-fold by incorporation of radioactive antibodies in the precipitates. The precipitates were visualised by autoradiography. The technique was exemplified with the use of rabbit-anti-CRP-gammaglobulin-125I in the quantification of CRP. The method, which can measure the proteins down to a concentration of 0.01 mg/1, invariably demonstrated CRP in apparently healthy blooddonors.

Quantitative bestimmung einzelner harnproteine mittels einfacher radialen immundiffusion

A method is described for quantitative determination of urinary proteins (albumin, haptoglobin, transferrin, γG- and γA-globulins) with specific antisera on the basis of single radial immundiffusion with agargel Partigen plates. The analysis is performed with urines, which were concentrated against collodion membranes to a concentration of 2 g/100 ml urine. The method enables a simple, simultaneous, quantitative determination of urine and serum proteins in the same operation.

Spontaneous Renal Lesions and Glomerular Deposits of IgG and Complement in Guinea Pigs

Abstract During recent studies on immunologically induced renal tubular disease (1), we noted a high incidence of spontaneous deposits of IgG and complement (C3) in glomeruli of untreated guinea pigs (2–4). We now describe the immunohistochemical, morphologic and functional status of kidneys of untreated guinea pigs of various ages. Materials and Methods. Twelve female guinea pigs of the Albany strain3 were studied in each of the following age groups: near-term fetus, 3 weeks, 3, 6, 12, 18 and 24 months. Six female guinea pigs, 16 months of age, were surveyed from each of the following closed colonies:4 Rockefeller, Dunkin, Camm and Fort Detrick Hartleys, and English Short Hairs. Three strain 2 and six strain 13 female guinea pigs,5 one year of age, were studied. Three 24-hr quantitative urinary protein determinations (5) were made on all animals 6 months of age or older.

Quantitative determination of soluble and membrane proteins through their native fluorescence.

Quantitative determination of soluble and membrane proteins through their native fluorescence.

Quantitative determination of protein in saliva

abstract – Seven methods for quantitative protein analysis were evaluated for the analysis of protein in saliva. The degree of interference from dialyzable components and from components retarded on Sephadex G‐50 was determined. Parotid saliva protein was fractionated into a glycoprotein‐rich and an amylase‐rich fraction on Sephadex G‐75, and the relative contributions from these protein fractions in the various protein tests were compared. Ultraviolet absorption at 215 mμ was recommended for the determination of total protein in salivary samples.

Quantitative Determination of Water-Soluble Proteins in Meconium

A quantitative microcomplement fixation assay and quantitative protein determinations were used to determine albumin as a percentage of total soluble proteins in meconium. Significant differences (p < 0.001 ) were found between the meconium from infants who develop the symptoms of cystic fibrosis (CF) and between healthy siblings of known patients with CF or normal controls. No statistical differences were seen between newborn infants with CF requiring surgical intervention due to meconium ileus and those not requiring surgery.

Abnormal Proteinuria in Malignant Diseases

Publisher Summary Of the many metabolic products of tumors, polypeptides, which belong to the family of immunoglobulins, are perhaps the most readily recognized and have consequently aroused the greatest interest. Secreted in varying amounts by the vast majority of plasmacytic and certain other neoplasms, these proteins can often be detected in the urine and have been the object of intensive investigation since the earliest days of protein chemistry. It is now apparent that numerous proteins associated with the metabolism of malignant cells are excreted in the urine, and, indeed, rather than containing merely “physiological garbage,” the urine has provided a source of “limitless treasure” for investigators in this field. Methods employed for the quantitative determination of proteins in the urine usually vary depending on the protein concentration, whereas the qualitative evaluation of urinary proteins requires a variety of procedures, including electrophoresis in various media, such as filter paper, cellulose acetate, starch gel, immunoelectrophoresis, single or double immunodiffusion analysis, and ultracentrifugation.

Changes in Serum Protein During the Molt and Reproductive Cycles of the American Lobster (Homarus americanus)

The variations in the serum proteins of lobsters were studied by quantitative protein determinations, starch gel and cellulose acetate electrophoresis, and immunodiffusion. A series of bleedings from 15 lobsters provided serum samples for each stage of the molt cycle. Total serum protein was highest before the molt and lowest directly after the molt. The total serum protein averaged 2.5 g/100 ml in the intermolt lobsters and variation among individuals was limited. Variation of serum proteins in an individual during the molt cycle included changes in the electrophoretic and immunodiffusion pattern. Quantitative changes during the cycle indicate a relative shift in the concentrations of various proteins. One component of serum protein was associated only with the development of eggs and another component was present only during premolt and directly after molt.

Protein-bacteriophage conjugates: application in detection of antibodies and antigens.

Covalent attachment of proteins to bacteriophage yielded modified phage preparations with which it is possible to detect antibodies to proteins at concentrations as low as 0.5 to 2.0 nanograms per milliliter. Similarly, antibodies may be linked covalently to phage, and the resulting antibody-phage conjugate is useful in detecting proteins. An alternative method for quantitative determination of proteins is suggested, in which the inactivation of protein-phage by antibodies to protein is inhibited by the protein tested. With rabbit immunoglobulin G as the protein, as little as 0.3 nanogram per milliliter could he determind.

Immunochemical Quantitation of Proteins in Single Cells: I. Carbon Anhydrase B, β-Chain Hemoglobin and γ-Chain Hemoglobin in Some Normal and Abnormal Erythrocytes

Abstract An immunochemical method for the quantitative determination of specific soluble proteins in individual erythrocytes has been described. Application of the method revealed: 1. From 0.5 to 0.9 per cent of the normal adult erythrocytes studied contained small amounts of γ-chains, from 2.5 to 12.5 µµg. as hemoglobin per cell. 2. In cord blood of normal infants of 38 weeks’ gestation, significant numbers of erythrocytes were found which contained either γ-chains or β-chains or both, independently of carbonic anhydrase B. 3. Once initiated within a given erythrocyte, β-chain synthesis in that cell rapidly approached adult rates. Derepression of carbonic anhydrase B synthesis was independent of derepression of hemoglobin synthesis, and in fetal cells which contained carbonic anhydrase B the amount found was well below that of most adult erythrocytes. 4. In 4 patients homozygous for hemoglobin S and in 2 persons heterozygous for thalassemia, an increase in F hemoglobin was associated with an increase in γ-chain content of individual erythrocytes as well as an increase in the number of erythrocytes containing γ-chains; in 2 patients homozygous for thalassemia, an unusual distribution of cells with increased γ-chain content was observed.

A new immunodiffusion method for quantitative determination of proteins in biological fluids based on a separate application of antibody and antigen to small agar discs

A new immunodiffusion method for quantitative determination of proteins in biological fluids based on a separate application of antibody and antigen to small agar discs

Determination of serum and body fluid proteins by membrane chromatography on nitrocellulose filters: synpor, sartorius and millipore

Different types of nitrocellulose membranes filters, viz. Snypor, Sartorius and Millipore, were tested as a carrier medium for chromatography and electrophoresis of proteins. All the membranes displayed a characteristics strong adsorptivity towards proteins which could be prevented by an impregnation with neutral detergents ( e.g. the Tweens). Some important differences in chromatography on various types of membranes were also found and discussed. Rapid quantitative protein determinations could be obtained by radial membrane chromatography of solutions containing concentrations of 0.001–6 % of various proteins.

Densitometric determination of proteins in small volumes

An analytical method of quantitative determination of proteins in small volumes is described. The method is based upon the densitometric evaluation of colour tests in agar-gel. The quantity of proteins is determined by graphical integration of densitometric curves and, in the arrangement described, it is possible to assay proteins in volumes of the order 10−3 ml.

Absorption and excretion of mercury in man. XII. Relationship between urinary mercury and proteinuria.

Using a sensitive method for the quantitative determination of total urinary protein, a mild proteinuria has been demonstrated in a working population chronically exposed to a relatively high concentration of the vapors and dusts of mixed organic (phenyl) and inorganic mercury compounds. The mean urinary protein content (9 mg/100 ml) of this exposed group was significantly higher than the mean urinary protein content (5.3 mg/100 ml) of a control unexposed group. For the exposed group, the urinary protein levels correlated well with the urinary mercury contents (with a statistical probability of such correlation less than 1%, as determined by the Spearman rank order correlation method). For the exposed group, the urinary protein levels showed a weak correlation (significance between 5% and 10%) with blood mercury contents. In both instances the correlation was found only on a group basis.

A method for sequential quantitative separation and determination of protein, RNA, DNA, lipid, and glycogen from a single rat liver homogenate or from a subcellular fraction

A procudure is described for the quantitative separation and estimation of protein, RNA, DNA, lipid, and glycogen from a single sample of rat liver or from a subcellular fraction. The method includes alkaline extraction of RNA from the perchloric acid insoluble portion of the sample, extraction of DNA by acid hydrolysis, and then recovery of lipids by solvent extraction. The procedure recommended prevents losses of protein and nucleotides into the lipid solvents and increases the recoveries of lipids. The simultaneous measurement of incorporation of each of the radioactive labels from glycine-C 14, adenine-H 3, and orthophosphate-P 32 into the chemical components studies is described. The usefulness of this procedure as an over-all screen of the functioning of the metabolic machinery is indicated.

Quantitative determination of soluble cellular proteins by radial diffusion in agar gels containing antibodies

Radial diffusion of protein antigens through gels containing antibodies has been used to quantitate proteins derived from cellular origins. For quantitation, the diameters of radial precipitin zones formed by tissue extracts were compared with zones formed by known concentrations of the standard proteins. The method employs immunological features of specific proteins to measure concentrations within the range of sensitivity usually obtained only with enzymic analyses.

A linear relationship between kidney function and kidney structure in growing and hypertrophied kidneys

The prevalence and significance of proteinuria in children has not been well documented. Approximately 4,000 students from 6 to 18 years of age have been tested for proteinuria during the past two years, utilizing a stix (Hema Combistix) for initial screening. One hundred and seventy-five students with urine protein concentration of 30 mg. per cent or greater on the first screening test were subjected to complete history-taking and physical examinations, as well as 12 hour day and 12 hour night urine collections for quantitative protein determinations. Similar studies were carried out with 100 students of various ages who had no detectable protein on the first screening test. Initial screening revealed that approximately 250 children had 1+ or greater proteinuria, an incidence of 7 per ceut. In the 100 students who tested negative for urinary protein, the mean daytime urine protein was 55 mg. per 12 hours and the mean of the nighttime was 42 mg. per 12 hours. In children testing 1+ or greater for protein, the day 12 hour urine protein was 90 mg. and the night was 48 mg. Clinical evaluation and family histories of the two groups did not reveal any significant differences. Six children with proteinuria in excess of 250 mg. for any 12 hour period have undergone complete evaluation. The renal biopsies revealed minimal alterations by light microscopy, ranging from slight focal hypercellularity to focal thickening of the basement membranes of the glomerular capillaries. These studies quantitate urine protein excretion in children at various ages and demonstrate that there is a significant incidence of proteinuria as measured by qualitative screening, as well as by quantitative methods.