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Influence of heat and sodium dodecyl sulfate on the endopeptidase I from Bacillus sphaericus 9602.

Authors
  • Garnier, M
  • Vacheron, M J
  • Pellon, G
  • Guinand, M
  • Michel, G
Type
Published Article
Journal
Biochemical and biophysical research communications
Publication Date
Apr 30, 1984
Volume
120
Issue
2
Pages
448–453
Identifiers
PMID: 6375658
Source
Medline
License
Unknown

Abstract

Endopeptidase I from Bacillus sphaericus is a stable enzyme which retains its activity at 37 degrees C in the presence of sodium dodecyl sulfate. Polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate revealed two forms of the enzyme: an active, fast-running form, for the enzyme preheated at 37 degrees C and a denatured, slow-running form, for the enzyme preheated at 100 degrees C. Such behavior is similar to that of the "heat-modifiable" outer membrane proteins from gram-negative bacteria. In the absence of sodium dodecyl sulfate, endopeptidase I aggregated in an enzymatically active dimer, with an apparent molecular weight of 90,000 daltons, which could be the native form of the enzyme.

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