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Comparative Study
. 1988 Oct;369(10):1185-9.
doi: 10.1515/bchm3.1988.369.2.1185.

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

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Comparative Study

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

D Waldinger et al. Biol Chem Hoppe Seyler. 1988 Oct.

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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