Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P02774 (Gc-globulin)
 196 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The beta-D-galactoside-specific lectin from Allomyrina dichotoma reacts with serum proteins which contain the corresponding carbohydrate moieties. By affinity chromatography of human serum using the insolubilized lectin coupled to Sepharose, it is possible to fractionate human serum proteins in 2 groups: those which react with the lectin (alpha 1-acid glycoprotein, haptoglobin, etc.) and those which do not (albumin, Gc-globulin, etc.). IgG is the only serum protein that can be found in both groups.
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PMID:Affinity chromatography of human serum proteins using immobilized lectin from Allomyrina dichotoma. 402 67

An improved method of group-specific component (Gc) typing was conducted electrophoretically on agarose gel. Individual bloodstains randomly collected from different individual donors over a five-year period at intervals of approximately one month were checked for Gc activity. Group-specific component was typed accurately in dried bloodstains stored at room temperature up to 43 months in age. From 100 different donors, bloodstains ranging in age from 38 to 43 months were tested by the methods described and 73% of the samples were interpretable for Gc.
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PMID:Detectability of group-specific component (Gc) in aged bloodstains. 403 46

Urine was collected from 6 healthy male adults at rest and from 20 male adults after a marathon race (25 miles). The concentrated urines were quantitatively analyzed, by single radial immunodiffusion, for their content in 12 different plasma proteins: tryptophan-rich prealbumin, albumin, alpha(1)-acid glycoprotein, alpha(1)-antitrypsin, ceruloplasmin, haptoglobin, Gc-globulin, transferrin, hemopexin, beta(2)-glycoprotein I, gammaA-globulin, and gammaG-globulin.Albumin, gammaA-globulin, and gammaG-globulin represent the major part of the plasma proteins detected in normal urine excreted by humans at rest (12, 0.5, and 2.5 mg respectively, out of a total excretion of 17.5 mg of plasma proteins per 24 hr). The other plasma proteins were excreted at a lower rate (< 0.4 mg/24 hr). The relative content of tryptophan-rich prealbumin, alpha(1)-antitrypsin, Gc-globulin, transferrin, and gammaG-globulin was lower in normal urine than in normal serum, whereas that of alpha(1)-acid glycoprotein, beta(2)-glycoprotein I, and gammaA-globulin was higher. The ratio of gammaG-globulin to gammaA-globulin was 4.9:1. When plotted on a logarithmic scale, no direct relationship between the molecular weight of a protein and the value of its renal clearance could be observed.Strenuous exercise increased (up to 50-fold) the excretion of plasma proteins which represent 82% of the total proteins found in urine, instead of 57% in urine collected from humans at rest. There was particularly a significant rise of tryptophan-rich albumin, albumin, alpha(1)-acid glycoprotein, transferrin, gammaA-globulin, and gammaG-globulin (0.26, 127, 11.8, 3.3, 1.2, and 2.0 mug respectively, out of a total excretion of 167 mug of plasma proteins per min). The ratio of gammaG-globulin to gammaA-globulin was 16:1. After exercise, the renal clearance of proteins increased from 2 to 40 times, but, as for the urine of normal subjects at rest, no direct relationship between molecular weight and renal clearance could be observed.
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PMID:Quantitative immunological determination of 12 plasma proteins excreted in human urine collected before and after exercise. 417 Mar 90

The development of new analytic and preparative techniques in the field of protein chemistry has essentially extended our knowledge about the variety of human plasma proteins in the last 15 years. In many cases plasma proteins have been particularly determined by immunologic techniques, partially highly purified and physicochemically well characterized, before knowing the biological function. To these proteins belong among others the alpha 1-antitrypsin, Cl-inactivator, alpha 2-macroglobulin, Gc-globulin and the cold-insoluble globulin. Today we know more than 100 proteins being isolated from human plasma and among these are nearly 20, of which the biological function is not yet known. To this group are belonging proteins, which are known since many years, like the alpha 1-acid glycoprotein and the C-reactive proteins as well as proteins, which have only been described in the last years and which partially have an interesting chemical structure, e.g. the histidinerich 3,8S-alpha 2-glycoprotein and the leucine-rich 3,1S-alpha 2-glycoprotein, of which every fifth amino acid is formed by leucine. It is to be hoped that the special chemical structure of some of these human plasma proteins as well as the quantitative immunologic determination in different patient sera will give hints to their biological function.
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PMID:Purified human plasma proteins of unknown function. 617 5

We have grown a human hepatoma cell line, designated as HA22T/VGH, from a 52-yr-old male hepatoma patient since July 1, 1980. This cell line has been subcultured more than 100 passages. The chromosome analysis of HA22T/VGH indicated that the chromosome numbers varied from 70 to 146, with the mode of 73. Methylcellulose soft agar assay showed that approximately 40% of the HA22T/VGH cells formed colonies. The HA22T/VGH produced tumors in nude mice. Histopathological studies of the tumor revealed the arrangement of hepatoma. Detected by the complement fixation method HA22T/VGH cells secreted ceruloplasmin, Factor B, C3, C4, Gc-globulin and alpha 1-acid-glycoprotein. These cells contained the liver associated enzymes: alanine amino transferase, tyrosine amino transferase and gamma-glutamyl transferase. HBsAg and alpha-fetoprotein were not detectable in the HA22T/VGH culture media or cell lysates by the radioimmunoassay.
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PMID:[A new human hepatoma cell line: establishment and characterization]. 629 75

Immunologic analyses of urinary proteins in patients with gestosis and related obstetrical conditions were performed and urinary protein patterns were compared with blood plasma protein patterns. Many kinds of proteins could be detected in urine of patients with gestosis beside albumin. Therefore, "proteinuria" should be chosen to characterise this state instead of the term "albuminuria". Generally speaking, when a total volume of protein contained in urine increases, its types or subfractions also increase in urine. Next to albumin, the most commonly detected proteins in urine of patients with gestosis were transferrin, IgG, inter-alpha-trypsin inhibitor, alpha 1-antitrypsin, IgA, alpha 2-HS-glycoprotein, alpha 1-acid glycoprotein, Gc-globulin, alpha 1-antichymotrypsin, hemopexin, ceruloplasmin, prealbumin, haptoglobin, anti-thrombin III, Cl-inactivator, IgM, and alpha 2-macroglobulin, in the descending order of their occurrence. Proteins that promptly became negative in urine of gestosis patients after delivery were inter-alpha-trypsin inhibitor, IgA, and ceruloplasmin. On the other hand, proteins most apt to persist in urine were albumin, alpha 2-HS-glycoprotein, and IgG. Generally speaking, lower molecular weight proteins were likely to persist in urine after delivery. Simultaneous determination of blood plasma and urinary proteins was performed for 18 kinds or subfractions of protein. A prognostic value of renal protein clearance was discussed.
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PMID:A study on proteins contained in urine of gestosis patients. 641 21

In the present study, it is shown that the pattern of the isoelectric focusing with immunofixation changes markedly in the presence of substances such as platelet extract, trypsin, chymotrypsin, vitamin D3 and neuraminidase. It has been recently found that the factor of platelet extract is actin (K. Shinomiya et al., Jpn. J. Legal Med., 36 (1982) 542-549; J. Biochem., 92 (1982) 1163-1171), and Gc globulin is bound by actin (H. Van Baelen et al., J. Biol. Chem., 255 (1980) 2270-2272). The Gc-actin complex appeared as supplementary bands of Gc-globulin near by the anode band of Gc1F-1F or Gc1S-1S. As to the Gc2-2, the supplementary band of Gc-actin complex appeared on the cathode side of the original anode band of Gc1F-1F or Gc1S-1S. Concerning Gc1F-1F (or Gc1S-1S), two supplementary bands of Gc-actin complex appeared on the anode side of the original band. Each product originated from the digestion of Gc-globulins of common phenotypes by trypsin appeared as four characteristic bands on the anode side of the original band. On the other hand, each product obtained by treatment of Gc-globulins of common phenotypes with chymotrypsin appeared as two characteristic bands on the anode side near the anode band of Gc1F-1F. The results obtained in this study give useful information to distinguish the pattern between original and supplementary bands which were altered by the action of factors.
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PMID:[Influence of the factors altering the electrophoretic migration of the alpha 2 Gc globulin in the diagram of iso-electric focusing of the Gc type]. 654 Nov 79

Isoelectric focussing (IEF) in thin layer polyacrylamide gels pH range 4-6.5 has been used to analyse the GC phenotypes of 4233 individuals from 28 different population groups in the Asian, Pacific, and Australian area. Because this technique reveals subtypes of the common GC*1 allele, there is almost a two-fold increase in the mean heterozygosity at the GC locus using IEF compared with conventional electrophoresis. The highest frequency (above 50%) of the GC*1S allele was encountered in Indian populations, reflecting genetic affinities with Europeans. By comparison, east and south east Asians are unique offing maximum values of the GC*1F allele (50%). With the exception of a few Pacific populations which show similar frequencies to east Asians, all other groups in the Pacific area, including Australia, have values of GC*1F similar to GC*1S ranging from 27% to 40%. The GC*2 frequency in most populations varies from 20% to 30%. However, some Polynesian groups have values up to 40% and Australian Aborigines less than 10%. Among other alleles, GC*1A1 is found to be widely distributed among Australian Aborigines and Melanesians and occurs sporadically in Polynesians, Micronesians, and in the Lesser Sunda Islands. Four new alleles, GC*1C24, GC*1C35 Aborigine, GC*1A21, and GC*1A22 are described. The gene frequency data at the GC locus has been used to calculate Nei genetic distances between the populations studied.
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PMID:Population genetics of the vitamin D binding protein (GC) subtypes in the Asian-Pacific area: description of new alleles at the GC locus. 654 32

A routine method for the analysis of Vitamin D-binding protein (Gc-globulin) phenotypes has been developed. The assay is based on isoelectric focusing in a narrow pH interval (4.5-5.4) using Agarose IEF (1%) or polyacrylamide (T5% C3%) gels, followed by immunofixation. When focused in this pH gradient the anodal and cathodal bands of the phenotype Gc 1-2 are separately by 16-18 mm. The "fast" and "slow" bands of the phenotype Gc 1-1 can also be easily distinguished from each other. The isoelectric focusing technique which has been developed resolves the Vitamin D-binding protein phenotypes in a fast, convenient and reproducible manner. Since agarose gels are so easy to cast and process, Agarose IEF is recommended as the matrix of choice.
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PMID:High resolution isoelectric focusing in a narrow pH interval for the phenotyping of vitamin D-binding protein (Gc-globulin). 654 78

A new chromatofocusing medium, MonoP, was used for fast (60 min or less) separations of human serum proteins. Separations in the broad pH interval 6.0-3.8 were analysed by fused rocket immunoelectrophoresis to identify a number of proteins, and by gradient gel electrophoresis to determine the molecular weight distribution of the eluted material. To illustrate further the high resolving power of chromatofocusing, narrow pH intervals of about 0.5 pH units were used to study the microheterogeneity of alpha 1-antitrypsin and Gc-globulin. Due to its high resolving power and preparative capacity, chromatofocusing is attractive as the first dimension in two-dimensional techniques for the resolution of complex protein mixtures.
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PMID:Fast chromatofocusing of human serum proteins with special reference to alpha 1-antitrypsin and Gc-globulin. 660 53


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