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[Skin high-molecular-weight protease. 2. Biochemical properties]
1Department of Dermatology, Juntendo University School of Medicine.
Nihon Hifuka Gakkai Zasshi. the Japanese Journal of Dermatology
|September 1, 1990
Summary
High-Molecular-Weight Protease from Wistar Rat skin exhibits significant activity and is stimulated by sodium dodecyl sulphate (SDS). Both serine and cysteine residues are crucial for its enzymatic function.
Area of Science:
- Biochemistry
- Enzymology
Context:
- The study builds upon previous purification of High-Molecular-Weight Protease from Wistar Rat skin.
- Investigates the enzymatic properties and cofactor dependencies of this purified protease.
Purpose:
- To characterize the activity profile of High-Molecular-Weight Protease.
- To determine the influence of sodium dodecyl sulphate (SDS) on enzyme kinetics.
- To identify key amino acid residues involved in the protease's catalytic mechanism.
Summary:
- The enzyme demonstrates high activity towards succynyl-leucyl-leucyl-valyl-tyrosine-methylcoumarinamide (SLLVT-MCA).
- Enzyme activity is dramatically enhanced (2,000%) by 0.03% SDS, with a pH optimum shifting to 8.5.
- Inhibition studies reveal that both serine protease inhibitors (e.g., diisopropylfluorophosphate) and SH protease inhibitors (e.g., N-ethylmaleimide, iodoacetamide) affect activity, alongside chymostatin.
Impact:
- Elucidates the dual catalytic nature of the protease, involving both serine and cysteine residues.
- Provides insights into the regulation of protease activity by detergents and pH.
- Contributes to understanding protease mechanisms in biological systems.