The denaturation of trypsin

Hua Lin Wu, Craig Kundrot, Myron L. Bender

研究成果: Article同行評審

6 引文 斯高帕斯(Scopus)

摘要

The denaturation of α- and β-trypsin in alkaline and neutral solution was studied. The denaturation of α-trypsin was a strict second-order reaction at neutrality. However, the denaturation of β-trypsin was not a pure secondorder reaction at the same pH. Calcium ion retarded the rate of β-trypsin denaturation to a greater extent than that of α-trypsin. In alkaline solution, trypsin has very short half life (t case1 2 < 30 minutes). On the other hand, the denaturation of immobilized trypsin in alkaline solution is a first-order reaction as is immobilized chymotrypsin. The rates of these two denaturations are similar. Calcium ion does not affect the rate of trypsin denaturation in alkaline solution.

原文English
頁(從 - 到)742-745
頁數4
期刊Biochemical and Biophysical Research Communications
107
發行號2
DOIs
出版狀態Published - 1982 七月 30

All Science Journal Classification (ASJC) codes

  • 生物物理學
  • 生物化學
  • 分子生物學
  • 細胞生物學

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