1. Digestion of the basic trypsin inhibitor of bovine pancreas by thermolysin
- Author
-
Beatrice Kassell and Tsun-Wen Wang
- Subjects
Electrophoresis ,Paper ,Conformational change ,Protein Denaturation ,Hot Temperature ,Chemical Phenomena ,Trypsin inhibitor ,Biophysics ,Bacillus ,Biochemistry ,chemistry.chemical_compound ,Aprotinin ,Thermolysin ,Endopeptidases ,medicine ,Trypsin ,Molecular Biology ,Chromatography ,Kunitz STI protease inhibitor ,Cell Biology ,Chemistry ,medicine.anatomical_structure ,chemistry ,Ninhydrin ,Indicators and Reagents ,Digestion ,Pancreas - Abstract
Extensive digestion of the basic trypsin inhibitor by thermolysin at 60–80° has been demonstrated by loss of inhibitory activity, increase in ninhydrin positive material and separation of the breakdown products by electrophoresis. Formation of the inhibitor-trypsin complex does not protect the inhibitor from digestion by thermolysin; both components are digested. Between 40° and 80° the inhibitor undergoes a reversible transition involving a slight conformational change; this may account for its susceptibility to thermolysin.
- Published
- 1970