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

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.

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Abstract

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.

Item Type:	Article
Uncontrolled Keywords:	self-association, alpha-chymotrypsin, isoelectric point, buffer solutions
Subjects:	600 Technology > 08 Food technology > 16 Nutritive value > 03 Proteins
Divisions:	Protein Chemistry and Technology
Depositing User:	Food Sci. & Technol. Information Services
Date Deposited:	28 Mar 2018 05:51
Last Modified:	28 Mar 2018 05:51
URI:	http://ir.cftri.res.in/id/eprint/5691

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