Characterization of proteolytic activities in embryos of Xenopus laevis.
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.
Miyata
S
S
Laboratory of Research for Biosynthesis and Metabolism, Keio University, School of Medicine, Tokyo, Japan.
Kihara
H K
HK
D000818:Animals; D003546:Cysteine Endopeptidases / Q000302:isolation & purification / Q000378:metabolism; D003609:Dactinomycin / Q000494:pharmacology; D004229:Dithiothreitol / Q000494:pharmacology; D004625:Embryo, Nonmammalian / Q000201:enzymology; D006863:Hydrogen-Ion Concentration; D008970:Molecular Weight; D010447:Peptide Hydrolases / Q000302:isolation & purification* / Q000378:metabolism; D014982:Xenopus laevis / Q000378:metabolism*
D003609:Dactinomycin; D010447:Peptide Hydrolases; D003546:Cysteine Endopeptidases; D004229:Dithiothreitol