RGD Reference Report - Purification and characterisation of leukotriene A4 hydrolase from rat neutrophils. - Rat Genome Database

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Purification and characterisation of leukotriene A4 hydrolase from rat neutrophils.

Authors: Evans, JF  Dupuis, P  Ford-Hutchinson, AW 
Citation: Evans JF, etal., Biochim Biophys Acta. 1985 May 29;840(1):43-50.
RGD ID: 2316605
Pubmed: PMID:3995081   (View Abstract at PubMed)

Leukotriene A4 hydrolase was rapidly and extensively purified from rat neutrophils using anion exchange and gel filtration high-pressure liquid chromatography. The enzyme which converts the allylic epoxide leukotriene A4 to the 5,12-dihydroxyeicosatetraenoic acid leukotriene B4 was localized in the cytosolic fraction and exhibited an optimum activity at pH 7.8 and an apparent Km for leukotriene A4 between 2 X 10(-5) and 3 X 10(-5) M. The purified leukotriene A4 hydrolase was shown to have a molecular weight of 68 000 on sodium dodecylsulfate polyacrylamide gel electrophoresis and of 50 000 by gel filtration. The molecular weight and monomeric native form of this enzyme are unique characteristics which distinguish leukotriene A4 hydrolase from previously purified epoxide hydrolases.



Gene Ontology Annotations    Click to see Annotation Detail View

Biological Process

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
Lta4hRatleukotriene metabolic process  IDA  RGD 

Molecular Function

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
Lta4hRatleukotriene-A4 hydrolase activity  IDA  RGD 

Objects Annotated

Genes (Rattus norvegicus)
Lta4h  (leukotriene A4 hydrolase)


Additional Information