Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1980-10-24
pubmed:abstractText
Endometrial cells from prepuberal pigs contain an estradiol 17 beta-dehydrogenase. By differential centrifugation of homogenate fractions and isopycnic separation of the particles sedimenting in the 600 leads to 38000 x g range, accompanied by marker enzyme and electron microscopic analyses, the enzyme appears to be exclusively associated with a subpopulation of lysosomes. It displays a high affinity for estradiol with a Km = 5 x 10(-7) mol/l. Dehydrogenation of estradiol to estrone is favorably driven by NAD, poorly by NADP. The reverse reaction with estrone as substrate and either NADH or NADPH or NADPH + regenerating system as cosubstrate does not proceed beyond the detection level, but trace amounts of 6 alpha/7 alpha-hydroxyestrone are observed at pH 6.5 with the latter two cosubstrates.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0018-4888
pubmed:author
pubmed:issnType
Print
pubmed:volume
361
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
959-68
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed:year
1980
pubmed:articleTitle
Studies on the involvement of lysosomes in estrogen action, III. The dehydrogenation of estradiol to estrone by porcine endometrial lysosomes.
pubmed:publicationType
Journal Article