Document Detail

The structure and function of acid proteases. VII. Distribution and some properties of acid proteases in monkey tissues.
MedLine Citation:
PMID:  14947     Owner:  NLM     Status:  MEDLINE    
1. The distribution of acid protease activity in various tissues of Japanese monkey (Macaca fuscata fuscata) was investigated with hemoglobin as a substrate at pH 3.0. The activity per protein weight in crude extracts was highest in spleen and lung, and decreased in the order: spleen, lung greater than kidney, testis greater than brain greater than liver, placenta greater than thyroid gland, muscle. The activity in crude muscle extract was about one-tenth those of spleen and lung. The activity per wet tissue weight was in roughly the same order except for a lower activity per wet weight of brain. 2. Upon chromatography of each crude extract on a Sephadex G-100 column, one major activity peak was eluted at a position corresponding to a molecular weight of about 41,000. This enzyme activity is attributed to cathepsin D [EC]. In addition, a minor activity peak was eluted in the case of spleen, lung and kidney at the break-through position, corresponding to a molecular weight of more than 100,000. This activity peak is presumably due to cathepsin E. These acid protease activities were, in most cases, strongly inhibited by pepstatin, an acid protease-specific peptide inhibitor. 3. The distribution of acid protease activity was investigated in the brain of crab-eating monkey (Macaca fascicularis). The activity was fairly evenly distributed among several regions of the brain, and its distribution was similar to those of other acid hydrolases, especially N-acetyl-beta-D-glucosaminidase [EC] and acid phosphatase [EC], which are marker enzymes of lysosomes.
K Sogawa; K Takahashi
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Journal of biochemistry     Volume:  81     ISSN:  0021-924X     ISO Abbreviation:  J. Biochem.     Publication Date:  1977 Feb 
Date Detail:
Created Date:  1977-05-27     Completed Date:  1977-05-27     Revised Date:  2007-12-19    
Medline Journal Info:
Nlm Unique ID:  0376600     Medline TA:  J Biochem     Country:  JAPAN    
Other Details:
Languages:  eng     Pagination:  423-9     Citation Subset:  IM    
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MeSH Terms
Acetylglucosaminidase / metabolism
Acid Phosphatase / metabolism
Brain / enzymology
Hemoglobins / metabolism
Hydrogen-Ion Concentration
Kidney / enzymology
Lung / enzymology
Molecular Weight
Pepstatins / pharmacology
Peptide Hydrolases / metabolism*
Spleen / enzymology
Reg. No./Substance:
0/Hemoglobins; 0/Pepstatins; EC Phosphatase; EC; EC 3.4.-/Peptide Hydrolases

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

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