Linked Life Data

6792194

Source:http://linkedlifedata.com/resource/pubmed/id/6792194

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
19
pubmed:dateCreated
1981-11-22
pubmed:abstractText
Purified, apoprostaglandin synthetase was prepared from sheep vesicular gland and studied in terms of its heme-binding properties. The enzyme binds a single heme group per enzyme monomer, Mr = 70,000. When reconstituted with heme, the enzyme has an absorption maximum at 412 nm and an absorption coefficient, epsilon 412 nm, of 120 mM-1 cm-1. The binding of heme to the apoenzyme was accompanied by a proportional increase in enzyme activity up to the point of heme-binding saturation. This reconstituted holoenzyme forms prostaglandin H2 from arachidonate. We conclude that prostaglandin synthetase possesses the heme-binding properties of a "typical" heme protein and that a single heme group mediates both the oxygenase and the peroxidase activities of the enzyme.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
256
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
10018-22
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1981
pubmed:articleTitle
The heme-binding properties of prostaglandin synthetase from sheep vesicular gland.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't