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Physicochemical investigation of bovine alpha n-crystallin at low pH
- 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