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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1982-10-29
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pubmed:abstractText |
The glycoprotein hormone alpha-subunit was extracted and purified from the urine of a patient with undifferentiated carcinoma producing isolated alpha-subunit. Its final specific immunoactivity was 0.92 (mg alpha-subunit/mg protein). The alpha-subunit exhibited virtually identical immunoantigenicity to hCG-alpha antiserum with standard hCG-alpha. The molecular weight of the alpha-subunit determined by gel chromatography on Sephadex G-100 was greater than that of standard hCG-alpha dissociated by urea in vitro. By SDS disc electrophoresis, however, the alpha-subunit moved faster than hCG-alpha separated by mercaptoethanol reduction. The amino acid composition of the alpha-subunit was quite similar to that of standard hCG-alpha. In the isoelectric focusing, the major components of the alpha-subunit from undifferentiated carcinoma and the alpha-subunit from urine of normal pregnant women (third trimester) were distributed over the range from pH 3.5 to 6.0, while standard hCG-alpha was distributed in the fractions ranging from pH 6.0 to 8.0. The result of a combination study in vitro indicated that both alpha-subunits from undifferentiated carcinoma and from urine of normal pregnant women did not actively combine with hCG-beta. These results suggest that the alpha-subunit secreted by undifferentiated carcinoma is virtually identical with standard hCG-alpha as the protein moiety but differs in regard to carbohydrate moiety, and also suggest that the excess of alpha-subunit, which is not associated with beta-subunit, may have undergone some intracellular modification, and consequently, the electric charge of the freely secreted alpha-subunit changes and it no longer has the ability to combine with the beta-subunit.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0013-7219
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
29
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
11-9
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:6179771-Adult,
pubmed-meshheading:6179771-Amino Acids,
pubmed-meshheading:6179771-Carcinoma,
pubmed-meshheading:6179771-Chorionic Gonadotropin,
pubmed-meshheading:6179771-Chromatography, DEAE-Cellulose,
pubmed-meshheading:6179771-Chromatography, Gel,
pubmed-meshheading:6179771-Electrophoresis, Disc,
pubmed-meshheading:6179771-Female,
pubmed-meshheading:6179771-Femoral Neoplasms,
pubmed-meshheading:6179771-Glycoprotein Hormones, alpha Subunit,
pubmed-meshheading:6179771-Humans,
pubmed-meshheading:6179771-Isoelectric Focusing,
pubmed-meshheading:6179771-Lung Neoplasms,
pubmed-meshheading:6179771-Peptide Fragments,
pubmed-meshheading:6179771-Radioimmunoassay
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pubmed:year |
1982
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pubmed:articleTitle |
The characterization of alpha-subunit of glycoprotein hormone produced by undifferentiated carcinoma.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Case Reports
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