Document Detail

Purification and partial characterization of cathepsin D from porcine (Sus scrofa) liver using affinity chromatography.
MedLine Citation:
PMID:  9713704     Owner:  NLM     Status:  MEDLINE    
Cathepsin D, a lysosomal aspartic protease, has been purified from porcine liver using a combination of pepstatin-A agarose and Affi-Gel Blue affinity chromatography, followed by size-exclusion chromatography. The purified protein consists of two polypeptide chains of 15 and 30 kDa, and has an isoelectric point of 6.8. Porcine liver cathepsin D has maximum activity at pH 2.5-3.0 as determined by its activity against hemoglobin, with a Kcat of 14.3 s-1 and a kcat/KM of 2.70 x 10(6) s-1M-1 as determined by the hydrolysis of a fluorogenic peptide substrate.
F Canduri; R J Ward; W F de Azevedo Júnior; R A Gomes; R K Arni
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Biochemistry and molecular biology international     Volume:  45     ISSN:  1039-9712     ISO Abbreviation:  Biochem. Mol. Biol. Int.     Publication Date:  1998 Jul 
Date Detail:
Created Date:  1998-10-19     Completed Date:  1998-10-19     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  9306673     Medline TA:  Biochem Mol Biol Int     Country:  AUSTRALIA    
Other Details:
Languages:  eng     Pagination:  797-803     Citation Subset:  IM    
Departamento de Física, IBILCE/UNESP, São José do Rio Preto, Brazil.
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MeSH Terms
Cathepsin D / chemistry,  isolation & purification*,  metabolism*
Chromatography, Affinity*
Electrophoresis, Polyacrylamide Gel
Hemoglobins / metabolism
Hydrogen-Ion Concentration
Isoelectric Point
Liver / enzymology*
Molecular Weight
Peptides / metabolism
Reg. No./Substance:
0/Hemoglobins; 0/Pepstatins; 0/Peptides; 0/Triazines; 11076-29-2/Streptomyces pepsin inhibitor; 12236-82-7/Cibacron Blue F 3GA; 39324-30-6/pepstatin; EC D

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

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