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Physicochemical investigation of bovine alpha n-crystallin at low pH

Authors :
A. Bonavolontà
P. Rebuffat
Rita Santamaria
Source :
Biochimica et biophysica acta. 54
Publication Year :
1961

Abstract

Bovine α n -crystallin was prepared by repeated precipitations as a pure, electrophoretically homogeneous protein. Some physicochemical measurements were carried out at low pH. The electrophoretic mobility was found to be 5·9·10 −5 cm 2 /V·sec in buffer pH 3·5, I 0.1. The apparent partial specific volume (φ p ) was 0·730 at 18°, using solutions of pH 3·55. The intrinsic viscosity [η] was 0.35 at 18° and pH 2.65. The increment of specific refraction corresponded to 173·10 −5 . Electron micrographs, obtained from an aqueous suspension of α n -crystallin, showed particles of spherical shape. The specific extinction coefficient in the ultraviolet spectrum of aqueous solutions (pH 2.65) is 9.354 at 277 mμ. The relatively high value of the intrinsic viscosity observed may be related to molecular expansion at low pH.

Details

ISSN :
00063002
Volume :
54
Database :
OpenAIRE
Journal :
Biochimica et biophysica acta
Accession number :
edsair.doi.dedup.....ac05c941897ea5ddb11445decd1e74c3