The 23 kDa Polypeptide from Common Frog Lens: Isolation, Properties, and Cellular Localization

The 23 kDa Polypeptide from Common Frog Lens: Isolation, Properties, and Cellular Localization The major water-soluble polypeptide with molecular weight of approximately 23 kDa (the 23 kDa polypeptide) was identified in the lens of common frog Rana temporaria L. According to the gel filtration data, the peptide is a part of an oligomeric protein with molecular weight over than 300 kDa (α-crystallin fraction). A highly pure fraction of the 23 kDa polypeptide was isolated by two-step ion-exchange chromatography and SDS electrophoresis and the specific antibodies were obtained. Immunohistochemistry showed the presence of the 23 kDa polypeptide in the cytoplasm of lens epithelial cells (including its central region) and in the zones neighboring the plasma membranes in the cortical fibers. The 23 kDa polypeptide was not found in the lens central zone (nucleus). It was also present in the retina (in the cells of inner nuclear layers), but not in the other tissues and organs of adult frog. Immunochemical analysis showed that the 23 kDa polypeptide was different from all known crystallins of frogs and other animals (bull, mouse, rat, and chicken). The nature of the 23 kDa polypeptide and the relation of its expression with the lens cell differentiation are discussed. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Russian Journal of Developmental Biology Springer Journals

The 23 kDa Polypeptide from Common Frog Lens: Isolation, Properties, and Cellular Localization

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Publisher
Kluwer Academic Publishers-Plenum Publishers
Copyright
Copyright © 2002 by MAIK “Nauka/Interperiodica”
Subject
Life Sciences; Animal Anatomy / Morphology / Histology
ISSN
1062-3604
eISSN
1608-3326
D.O.I.
10.1023/A:1016897732447
Publisher site
See Article on Publisher Site

Abstract

The major water-soluble polypeptide with molecular weight of approximately 23 kDa (the 23 kDa polypeptide) was identified in the lens of common frog Rana temporaria L. According to the gel filtration data, the peptide is a part of an oligomeric protein with molecular weight over than 300 kDa (α-crystallin fraction). A highly pure fraction of the 23 kDa polypeptide was isolated by two-step ion-exchange chromatography and SDS electrophoresis and the specific antibodies were obtained. Immunohistochemistry showed the presence of the 23 kDa polypeptide in the cytoplasm of lens epithelial cells (including its central region) and in the zones neighboring the plasma membranes in the cortical fibers. The 23 kDa polypeptide was not found in the lens central zone (nucleus). It was also present in the retina (in the cells of inner nuclear layers), but not in the other tissues and organs of adult frog. Immunochemical analysis showed that the 23 kDa polypeptide was different from all known crystallins of frogs and other animals (bull, mouse, rat, and chicken). The nature of the 23 kDa polypeptide and the relation of its expression with the lens cell differentiation are discussed.

Journal

Russian Journal of Developmental BiologySpringer Journals

Published: Oct 13, 2004

References

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