Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1981-11-22
pubmed:abstractText
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0165-0378
pubmed:author
pubmed:issnType
Print
pubmed:volume
3
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
131-6
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1981
pubmed:articleTitle
Studies on the subunit and polypeptide structure of a polymeric form of pregnancy-specific beta 1-glycoprotein.
pubmed:publicationType
Journal Article