Document Detail

Isolation of cathepsin D from human leucocytes.
MedLine Citation:
PMID:  831834     Owner:  NLM     Status:  MEDLINE    
Acid and neutral protease activities were determined in the granule fractions of polymorpho and mononuclear leucocytes, separated from human blood by means of a discontinuous density gradient centrifugation. The mononuclear leucocytes contained only acid protease while preparations from polymorphonuclear leucocytes showed a predominant activity at neutral pH with a small peak in the acid range. A separation of the acid from the neutral enzyme could be obtained in the granule fraction of polymorphonuclear leucocytes by means of DEAE chomatography. The acid enzyme was then purified from a mixture of leucocytes, more than 400 times, by means of gel chromatography with Sephadex G-200 superfine. The purified acid protease showed an optimum pH of 3.6, had a molecular weight at 42 000 and was characterized by a single protein band (Rf = 0.31) by disc-gel electrophoresis. With all probability this enzyme can be classified as cathepsin D (EC
I Ishikawa; G Cimasoni
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Biochimica et biophysica acta     Volume:  480     ISSN:  0006-3002     ISO Abbreviation:  Biochim. Biophys. Acta     Publication Date:  1977 Jan 
Date Detail:
Created Date:  1977-03-31     Completed Date:  1977-03-31     Revised Date:  2004-11-17    
Medline Journal Info:
Nlm Unique ID:  0217513     Medline TA:  Biochim Biophys Acta     Country:  NETHERLANDS    
Other Details:
Languages:  eng     Pagination:  228-40     Citation Subset:  IM    
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MeSH Terms
Cathepsins / blood*,  isolation & purification
Cytoplasmic Granules / enzymology
Leukocytes / enzymology*
Monocytes / enzymology*
Neutrophils / enzymology*
Reg. No./Substance:
EC 3.4.-/Cathepsins

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

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