Document Detail

Studies on the subunit and polypeptide structure of a polymeric form of pregnancy-specific beta 1-glycoprotein.
MedLine Citation:
PMID:  6974240     Owner:  NLM     Status:  MEDLINE    
The structure of a high-molecular-weight form of Pregnancy-Specific beta 1-Glycoprotein designated PSB1G-I that had been previously isolated from maternal serum was studied by gel chromatography in guanidine hydrochloride dissociating solvent. Evidence was obtained that subunits of identical size (bonded together non-covalently) but of differing polypeptide compositions constitute the PSB1G-I molecule. The subunits of PSB1G-I have been designated alpha and beta subunits. Reduction of PSB1G-I results in an intact alpha chain and two beta chains (beta 1 and beta 2) that are linked in the parent beta subunit by covalent bonds. The collective molecular weights of the alpha, beta 1 and beta 2 chains are equal to 97 800 which is assumed to represent the 'true' molecular weight of 'native' serum PSB1G.
B W Griffiths; A Godard
Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Journal of reproductive immunology     Volume:  3     ISSN:  0165-0378     ISO Abbreviation:  J. Reprod. Immunol.     Publication Date:  1981 Jun 
Date Detail:
Created Date:  1981-11-22     Completed Date:  1981-11-22     Revised Date:  2008-11-21    
Medline Journal Info:
Nlm Unique ID:  8001906     Medline TA:  J Reprod Immunol     Country:  NETHERLANDS    
Other Details:
Languages:  eng     Pagination:  131-6     Citation Subset:  IM    
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MeSH Terms
Chemical Phenomena
Chromatography, Gel
Electrophoresis, Polyacrylamide Gel
Molecular Weight
Peptides / analysis*
Pregnancy Proteins / blood*
Pregnancy-Specific beta 1-Glycoproteins / analysis,  blood*
Reg. No./Substance:
0/Peptides; 0/Pregnancy Proteins; 0/Pregnancy-Specific beta 1-Glycoproteins

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