Abstract |
Protease Q, a recently discovered subtilisin-like protease, exhibited unusual stability in 10% sodium dodecyl sulfate (SDS) and 8 M urea solutions. In 2% SDS it exhibited higher activity than the control, and in 10% SDS it retained 50% of its original activity when azocoll was used as substrate. Kinetic studies showed that the decrease in the activity of protease Q in SDS solutions followed a first order kinetics with a half-life of 446, 278, 78, and 24 h in 1%, 2%, 5%, and 10% SDS, respectively, at 25 degrees C. Protease Q was also stable against autolysis. In 20 mM Tris-HCl buffer (pH 8.3) containing 1.0 mM CaCl2, protease Q had a half life of 2822 h and 725 h at room temperature and at 37 degrees C, respectively. The enzyme was able to completely hydrolyze beta-lactoglobulin, beta-casein, and keratin in 8-10 M urea.
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Authors | X Q Han, S Damodaran |
Journal | Biochemical and biophysical research communications
(Biochem Biophys Res Commun)
Vol. 240
Issue 3
Pg. 839-43
(Nov 26 1997)
ISSN: 0006-291X [Print] United States |
PMID | 9398655
(Publication Type: Journal Article, Research Support, U.S. Gov't, Non-P.H.S.)
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Chemical References |
- Azo Compounds
- Caseins
- Lactoglobulins
- Oligopeptides
- Sodium Dodecyl Sulfate
- Azocoll
- Keratins
- succinyl-alanyl-alanyl-prolyl-phenylalanine-4-nitroanilide
- Urea
- Collagen
- Serine Endopeptidases
- Subtilisins
- protease Q
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Topics |
- Amino Acid Sequence
- Azo Compounds
(metabolism)
- Bacillus
(enzymology)
- Caseins
(metabolism)
- Collagen
(metabolism)
- Electrophoresis, Polyacrylamide Gel
- Enzyme Stability
- Keratins
(metabolism)
- Kinetics
- Lactoglobulins
(metabolism)
- Molecular Sequence Data
- Oligopeptides
(metabolism)
- Protein Denaturation
- Serine Endopeptidases
(chemistry, isolation & purification, metabolism)
- Sodium Dodecyl Sulfate
(pharmacology)
- Substrate Specificity
- Subtilisins
(metabolism)
- Urea
(pharmacology)
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