The denaturation of trypsin

Hua Lin Wu, Craig Kundrot, Myron L. Bender

Research output: Contribution to journalArticlepeer-review

6 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)742-745
Number of pages4
JournalBiochemical and Biophysical Research Communications
Issue number2
Publication statusPublished - 1982 Jul 30

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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