Document Detail

Amino acid oxidase of leukocytes in relation to H 2 O 2 -mediated bacterial killing.
MedLine Citation:
PMID:  4397948     Owner:  NLM     Status:  MEDLINE    
D-Amino acid oxidase and L-amino acid oxidase have been measured in sucrose homogenates of polymorphonuclear leukocytes (PMN) obtained from guinea pigs and humans. Subcellular distribution patterns and studies on latency indicate that these oxidases are soluble enzymes. Their hydrogen peroxide-generating capacity was verified. Chronic granulomatous disease PMN, which lack a respiratory burst and fail to generate H(2)O(2) during phagocytosis and do not kill catalase positive bacteria, had peroxide-generating amino acid oxidase activity equal to that found in PMN homogenates from patients with bacterial infections. The precise metabolic and bactericidal role of amino acid oxidases in PMN remains uncertain.
M R Eckstein; R L Baehner; D G Nathan
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  The Journal of clinical investigation     Volume:  50     ISSN:  0021-9738     ISO Abbreviation:  J. Clin. Invest.     Publication Date:  1971 Sep 
Date Detail:
Created Date:  1971-10-14     Completed Date:  1971-10-14     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  7802877     Medline TA:  J Clin Invest     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  1985-91     Citation Subset:  AIM; IM    
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MeSH Terms
Amino Acid Oxidoreductases / blood*
Cell Fractionation
D-Amino-Acid Oxidase / blood*
Granuloma / blood
Guinea Pigs
Hydrogen Peroxide / metabolism
Infection / blood
Lymphadenitis / blood
NAD / metabolism
Neutrophils / enzymology*,  metabolism
Oxygen Consumption
Reg. No./Substance:
53-84-9/NAD; 7722-84-1/Hydrogen Peroxide; EC 1.4.-/Amino Acid Oxidoreductases; EC Oxidase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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