Effects on properties of a thiol protease from Xenopus embryos of changes in substrate and assay conditions.
Version of Record online: 2 JAN 2013
© The Author(s) Journal compilation © 1995 International Federation for Cell Biology
Cell Biology International
Volume 19, Issue 4, pages 333–338, April 1995
How to Cite
Miyata, S., Nishibe, Y. and Kihara, H. K. (1995), Effects on properties of a thiol protease from Xenopus embryos of changes in substrate and assay conditions. Cell Biology International, 19: 333–338. doi: 10.1006/cbir.1995.1076
- Issue online: 2 JAN 2013
- Version of Record online: 2 JAN 2013
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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.