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Preparation and kinetic properties of a new form of chymotrypsin which is active at alkaline pH: 1 -chymotrypsin.
| Content Provider | Semantic Scholar |
|---|---|
| Author | Valenzuela, Pablo D. T. Bender, M. Lionel |
| Copyright Year | 1973 |
| Abstract | Abstract The preparation of a new stable and active form of chymotrypsin is described. The enzyme possesses threonine-147 instead of alanine-149 as the NH2-terminal group of the C chain and has been called α1-chymotrypsin. The conformational transition that affects chymotrypsins at alkaline pH was investigated and compared with that of α- and δ-chymotrypsins by studying the kinetic constants and their pH dependencies for the hydrolysis of various specific ester substrates. The κcat values obtained with α1-chymotrypsin are similar to those of α- and δ-chymotrypsins. The Km values showed a progressive increase toward the alkaline pH region. The shape of the Km-pH profiles closely resemble those of δ-chymotrypsin and differ considerably from the behavior of α-chymotrypsin. The results strongly implicate the participation of the alanine-149 amino group in the reversible inactivation of α-chymotrypsin at high pH. |
| File Format | PDF HTM / HTML |
| PubMed reference number | 4736884 |
| Journal | Medline |
| Volume Number | 248 |
| Issue Number | 14 |
| Alternate Webpage(s) | http://www.jbc.org/content/248/14/4909.full.pdf |
| Journal | The Journal of biological chemistry |
| Language | English |
| Access Restriction | Open |
| Content Type | Text |
| Resource Type | Article |