1964
DOI: 10.1021/bi00900a015
|View full text |Cite
|
Sign up to set email alerts
|

On the Heterogeneity of Three-Times-crystallized α-Chymotrypsin*

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1
1
1
1

Citation Types

3
18
0

Year Published

1971
1971
2019
2019

Publication Types

Select...
8
2

Relationship

0
10

Authors

Journals

citations
Cited by 55 publications
(21 citation statements)
references
References 22 publications
3
18
0
Order By: Relevance
“…Aliquots were withdrawn at various times and titrated directly with CI. A plot of log (% CI activity remaining) versus time of reaction was obviously biphasic, with a component representing 29% of the initial enzyme losing activity with a rate constant k = 0.086 min-' , and the rest of the enzyme losing activity with a rate constant k = 0.0045 min-' , Similar plots were reported by Erlanger et al [8] for the thermal denaturation of chymotrypsin.…”
Section: Resultssupporting
confidence: 82%
“…Aliquots were withdrawn at various times and titrated directly with CI. A plot of log (% CI activity remaining) versus time of reaction was obviously biphasic, with a component representing 29% of the initial enzyme losing activity with a rate constant k = 0.086 min-' , and the rest of the enzyme losing activity with a rate constant k = 0.0045 min-' , Similar plots were reported by Erlanger et al [8] for the thermal denaturation of chymotrypsin.…”
Section: Resultssupporting
confidence: 82%
“…The level of uninhibited trypsin activity in the reaction mixture was assessed using N a-benzoyl-DLarginine-p-nitroanilide as substrate (Kakade et al 1969) and the level of uninhibited chymotrypsin was evaluated using glutaryl-1-phenylalanine-p-nitroanilide as substrate (Erlanger et al 1964). Trypsin and chymotrypsin inhibitory activity was expressed as g enzyme inhibited/kg original raw meal and the protease-inhibitor contents of the test diets calculated on the basis of the level of raw seed meal inclusion in the diet.…”
Section: Materials a N D Methodsmentioning
confidence: 99%
“…Chymotrypsin activity was determined photometrically a t 405 nm with gluratyl-L-phenylalaninep-nitroanilide as substrate [2]. The reaction mixture contained 400 p1 4 mM substrate in 0.2 M Tris-HC1 pH 8.…”
Section: Measurement Of Enzymatic Activitiesmentioning
confidence: 99%