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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1977-7-18
pubmed:abstractText
Purified ligandin (Y-protein) a 46000-dalton protein, has been shown to consist of two subunit species (mol. wts. 22 000 and 24 000) on discontinuous polyacrylamide gel electrophoresis in sodium dodecyl sulphate. This technique was used to define further the nature of these subunits. The Y sulphobromophthalein-binding fraction of rat hepatic cytosol was shown to contain three major subunit bands designated subunit Ya, subunit Yb and subunit Yc in ascending order of size. Purified ligandin was found to comprise Ya and Yc subunit species, and also gave two bands on isoelectric focusing. The two subunit species in purified ligandin were partially separated by an additional purification step. Antiserum to ligandin reacted mono-specifically with the purified protein, as well as hepatic, renal and small intestinal mucosa cytosol, but gave lines of identity and partial identity with cytosol from testis, ovary and adrenal gland. The Y fraction of testis was found to contain only Yb and Yc species, while all three major bands were found in liver, kidney and small intestinal mucosa. Phenobarbital treatment increased the concentration of Ya and Yb in the liver, but had little effect on Yc. These findings suggest that the Ya and Yc ligandin subunits are the monomers of two proteins: YaYa and YcYc.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
27
pubmed:volume
492
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
163-75
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
1977
pubmed:articleTitle
Ligandin heterogeneity : evidence that the two non-identical subunits are the monomers of two distinct proteins.
pubmed:publicationType
Journal Article