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Kinetics of alpha-chymotrypsin dimerization
The Journal of Biological Chemistry
Jan 25, 1976
M J Gilleland, Marissa L Bender
PMID: 1397
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Abstract
A method has been devised which permits the observation of the loss of active sites promoted by aggregation of alpha-chymotrypsin. When alpha-chymotrypsin in unbuffered solution at pH 7 is mixed with buffered proflavin by stopped flow instrumentation to give a final pH of 3.89, a decrea...read more
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Mathematics
Hydrogen-Ion Concentration
Proflavine
Avazyme
Plasma Protein Binding Capacity
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Kinetics of alpha-chymotrypsin dimerization
Abstract
A method has been devised which permits the observation of the loss of active sites promoted by aggregation of alpha-chymotrypsin. When alpha-chymotrypsin in unbuffered solution at pH 7 is mixed with buffered proflavin by stopped flow instrumentation to give a final pH of 3.89, a decrea...read more
Mentioned in this Paper
Mathematics
Hydrogen-Ion Concentration
Proflavine
Avazyme
Plasma Protein Binding Capacity
Related Papers
Paper Details
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