Amino-Acid Sequence Homology of a Polymorphic Cellular Protein from Human Lymphocytes and the Chaperonins fromEscherichia coli (groEL)and Chloroplasts (Rubisco-Binding Protein)
- 1 January 1988
- journal article
- research article
- Published by Walter de Gruyter GmbH in Biological Chemistry Hoppe-Seyler
- Vol. 369 (2), 1185-1190
- https://doi.org/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 lyphocytes. 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.This publication has 16 references indexed in Scilit:
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