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Effects on properties of a thiol protease from Xenopus embryos of changes in substrate and assay conditions.
Author(s) -
Miyata Shohei,
Nishibe Yasuo,
Kihara Hirozi K.
Publication year - 1995
Publication title -
cell biology international
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.932
H-Index - 77
eISSN - 1095-8355
pISSN - 1065-6995
DOI - 10.1006/cbir.1995.1076
Subject(s) - xenopus , protease , proteolysis , cytoplasm , yolk , biochemistry , biology , embryo , polyacrylamide gel electrophoresis , proteolytic enzymes , microbiology and biotechnology , chemistry , enzyme , gene , ecology
A protease was purified from Xenopus embryos. Proteolytic activity of the protease against BSA had an optimum pH of 3.8 in acetate buffer and was not detectable at neutral pH. However, when embryonic proteins were used as substrates and digested in phosphate buffer, proteolysis of embryonic proteins was enhanced and was detectable from pH 5.0 to pH 7.0. Digestion of three proteins were mainly detected in digestion of total embryonic proteins. The proteins digested had the same mobilities (on SDS polyacrylamide gel) as yolk proteins. The protease was present in the cytoplasm and around yolk granules. We propose that this protease mainly cleaves a certain yolk proteins in the cytoplasm of Xenopus embryos.