Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1988-11-30
pubmed:abstractText
12-Lipoxygenases were found in the cytosol fraction of bovine leukocytes and platelets. The bovine leukocyte enzyme was immunoprecipitable by a monoclonal antibody directed to 12-lipoxygenase of porcine leukocytes, but not by a monoclonal antibody against the human platelet enzyme. In contrast, the bovine platelet enzyme cross-reacted only with antibody against the human platelet enzyme. The leukocyte and platelet enzymes were partially purified to final specific enzyme activities of 1.1 and 0.3 mumol/min/mg protein, respectively, by immunoaffinity chromatography using each cross-reacting antibody as a ligand. The leukocyte enzyme reacted with various octadecapolyenoic acids as well as eicosapolyenoic and docosapolyenoic acids, whereas the platelet enzyme was almost inactive with octadecapolyenoic acids. Moreover, the two enzymes showed different heat-instabilities and reaction time courses. Thus, the 12-lipoxygenases of bovine leukocytes and platelets were immunologically and catalytically distinct enzymes.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0003-9861
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
266
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
613-21
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Two immunologically and catalytically distinct arachidonate 12-lipoxygenases of bovine platelets and leukocytes.
pubmed:affiliation
Department of Biochemistry, Tokushima University, School of Medicine, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't