Linked Life Data

2165489

Source:http://linkedlifedata.com/resource/pubmed/id/2165489

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
22
pubmed:dateCreated
1990-9-4
pubmed:abstractText
The retinoic acid binding activity in the lumen of the rat epididymis (Ong, D., and Chytil, F. (1988) Arch. Biochem. Biophys. 267, 474-478) has been purified to homogeneity. The protein exists in two forms, one form having an additional three amino acids at the amino terminus. The amino acid sequence of the protein was determined to 20 amino acids and proved to be identical to that of the major androgen-dependent proteins from rat epididymis as deduced from the cDNA sequence. These proteins are thought to play a role in sperm maturation, perhaps, it can be suggested now, by delivering retinoic acid to the sperm. The retinoic acid-binding protein has sequence homology to the serum retinol-binding protein and is predicted to have the same overall fold of the polypeptide chain. The epididymal retinoic acid-binding protein has been crystallized from 39 to 43% saturated ammonium sulfate, 10 mm Tris, pH 8.0. The crystals are space group P2(1), with a = 39.4, b = 58.9, c = 65.4 a, beta = 105 degrees 16 min.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
265
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
12876-9
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
Purification and crystallization of a retinoic acid-binding protein from rat epididymis. Identity with the major androgen-dependent epididymal proteins.
pubmed:affiliation
Department of Biochemistry, Vanderbilt University, Nashville, Tennessee 37232.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.