Effects on properties of a thiol protease from Xenopus embryos of changes in substrate and assay conditions.
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.
Miyata
S
S
Department of Chemistry, College of Humanities and Science, Nihon University, Tokyo, Japan.
Nishibe
Y
Y
Kihara
H K
HK
D000418:Albumins / Q000378:metabolism; D000818:Animals; D003546:Cysteine Endopeptidases / Q000302:isolation & purification / Q000378:metabolism*; D003593:Cytoplasm / Q000737:chemistry / Q000201:enzymology; D004527:Egg Proteins / Q000378:metabolism; D004625:Embryo, Nonmammalian / Q000201:enzymology / Q000648:ultrastructure; D005260:Female; D006863:Hydrogen-Ion Concentration; D007150:Immunohistochemistry; D013379:Substrate Specificity; D014981:Xenopus / Q000196:embryology*
D000418:Albumins; D004527:Egg Proteins; D003546:Cysteine Endopeptidases