Document Detail

Characterization of proteolytic activities in embryos of Xenopus laevis.
MedLine Citation:
PMID:  3066576     Owner:  NLM     Status:  MEDLINE    
1. Proteolytic activities in early embryos of Xenopus laevis exhibited maximum levels at pH 3.2, 5.6 and 7.2 when 3H-BSA was used as substrate, and the maximum proteolytic activity at pH 3.2 was several thousand-fold higher during the tail bud stage than in the unfertilized egg. 2. The proteolytic activity at pH 3.2 was separated into two fractions by gel chromatography. One fraction corresponded to a mol. wt of about 40,000 and its activity was inhibited by thiol protease inhibitors. The other appeared to be a protease of much higher mol. wt. 3. The maximum activities at pH 5.6 and 7.2 appear to correspond to proteins of mol. wt greater than 1,000,000.
S Miyata; H K Kihara
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Comparative biochemistry and physiology. B, Comparative biochemistry     Volume:  91     ISSN:  0305-0491     ISO Abbreviation:  Comp. Biochem. Physiol., B     Publication Date:  1988  
Date Detail:
Created Date:  1989-03-30     Completed Date:  1989-03-30     Revised Date:  2007-11-15    
Medline Journal Info:
Nlm Unique ID:  2984730R     Medline TA:  Comp Biochem Physiol B     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  651-6     Citation Subset:  IM    
Laboratory of Research for Biosynthesis and Metabolism, Keio University, School of Medicine, Tokyo, Japan.
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MeSH Terms
Cysteine Endopeptidases / isolation & purification,  metabolism
Dactinomycin / pharmacology
Dithiothreitol / pharmacology
Embryo, Nonmammalian / enzymology
Hydrogen-Ion Concentration
Molecular Weight
Peptide Hydrolases / isolation & purification*,  metabolism
Xenopus laevis / metabolism*
Reg. No./Substance:
3483-12-3/Dithiothreitol; 50-76-0/Dactinomycin; EC 3.4.-/Peptide Hydrolases; EC 3.4.22.-/Cysteine Endopeptidases

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