Mechanistic studies on carboxypeptidase A from goat pancreas Part II: Evidence for carboxyl group.
J Biosci
;
1985 Sept; 9(1&2): 91-97
Article
in English
| IMSEAR
| ID: sea-160482
ABSTRACT
Studies with substrate analogues and the pH optimum indicated the involvement of carboxyl group in the active site of goat carboxypeptidase A. Chemical modification of the enzyme with 1-cyclohexyl-3-(2-morpholinoethyl) carbodiimide methoI -p-toluene sulphonate, a carboxyl specific reagent, led to loss of both esterase and peptidase activities. Protection studies showed that this carboxyl group was in the active site and was protected by ßphenylpropionic acid and glycyl-L-tyrosine. Kinetic studies also confirmed the involvement of carboxylic group because the enzyme modification with water soluble carbodiimide was a two step reaction which excluded the possibility of tyrosine or lysine which are known to give a one step reaction with this reagent.
Full text:
Available
Index:
IMSEAR (South-East Asia)
Language:
English
Journal:
J Biosci
Year:
1985
Type:
Article
Similar
MEDLINE
...
LILACS
LIS