On the stereochemistry of catalysis by serine proteases
✍ Scribed by László Polgár; Bence Asbóth
- Publisher
- Elsevier Science
- Year
- 1974
- Tongue
- English
- Weight
- 1024 KB
- Volume
- 46
- Category
- Article
- ISSN
- 0022-5193
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📜 SIMILAR VOLUMES
Quantum mechanical ab initio (RHF/6-31؉G\*//RHF/3-21G) calculations were used to simulate the formation of the tetrahedral complex intermediate (TC) in serine protease active site by substrates and transition-state analog inhibitors. The enzyme active site was simulated by an assembly of the amino a
## Abstract The work described here demonstrates the synthesis by human articular cartilage of plasminogen activator inhibitor‐1 (PAI‐1), a potent inhibitor of the serine protease tissue plasminogen activator (tPA). We also present data demonstrating an increase in PAI‐1 messenger ribonucleic acid
## BACKGROUND. Cathepsin B (CATB) and cathepsin L (CATL), which are cysteine proteases, urokinase-(UPA) and tissue-type plasminogen activator (TPA), both serine proteases, and their inhibitor type-1 (PAI-1) are believed to play an important role in colorectal carcinoma (CRC) invasion and metastasi