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Amino-acid sequence homology of a polymorphic cellular protein from human lymphocytes and the chaperonins from Escherichia coli (groEL) and chloroplasts (Rubisco-binding protein).

作者信息

Waldinger D, Eckerskorn C, Lottspeich F, Cleve H

机构信息

Institut für Anthropologie und Humangenetik der Universität München.

出版信息

Biol Chem Hoppe Seyler. 1988 Oct;369(10):1185-9. doi: 10.1515/bchm3.1988.369.2.1185.

Abstract

The human p60 (Mr 60,000) is an abundant protein in the two-dimensional electrophoresis pattern of the cellular proteins of human mitogen-stimulated lymphocytes. The p60 shows as remarkable characteristic a genetic polymorphism with two different alleles. Electrotransfer of this protein from two-dimensional gels onto siliconized glass fiber sheets and subsequent amino-acid sequence analysis has revealed a striking homology to the known bacteria and plant chaperonins, the groEL and the Rubisco-subunit-binding protein. From this sequence homology we conclude that we have identified the human chaperonin homologue.

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