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Studies on self association of proteins. Self assocition of alpha-chymotrypsin at its isoelectric point in buffer solutions of ionic strength 0.1.

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Title Studies on self association of proteins. Self assocition of alpha-chymotrypsin at its isoelectric point in buffer solutions of ionic strength 0.1.
 
Creator Pandit, M. W.
Narasinga Rao, M. S.
 
Subject 03 Proteins
 
Description The self-association of a-chymotrypsin at its
isoelectric point has been studied in two buffer solutions of
p (ionic strength) = 0.1: phosphate buffer (pH 6.9) and
Tris buffer (pH 8.3). The weight-average molecular weight
(by the Archibald method) and sedimentation coefficient
were determined as a function of protein concentration. The
molecular weights measured were the same in both the buffers. In sedimentation velocity experiments unimodal
peaks were obtained at all the protein concentrations. The
molecular weight data could be fitted to a nonideal indefinite
self-association equilibrium or a hexamerization equilibrium
with all the intermediate species coexisting. The
sedimentation data could be fitted to an octamerization
equilibrium.
 
Date 1975
 
Type Article
PeerReviewed
 
Format pdf
 
Language en
 
Identifier http://ir.cftri.com/5691/1/Biochemistry%2C%20Volume-14%28%20%281975%29%204106-4110.pdf
Pandit, M. W. and Narasinga Rao, M. S. (1975) Studies on self association of proteins. Self assocition of alpha-chymotrypsin at its isoelectric point in buffer solutions of ionic strength 0.1. Biochemistry, 14. pp. 4106-4110.