Literature DB >> 2907406

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 Waldinger1, C Eckerskorn, F Lottspeich, H Cleve.   

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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Year:  1988        PMID: 2907406     DOI: 10.1515/bchm3.1988.369.2.1185

Source DB:  PubMed          Journal:  Biol Chem Hoppe Seyler        ISSN: 0177-3593


  10 in total

1.  An interaction between p21ras and heat shock protein hsp60, a chaperonin.

Authors:  S Ikawa; R A Weinberg
Journal:  Proc Natl Acad Sci U S A       Date:  1992-03-15       Impact factor: 11.205

2.  Highly resolving two-dimensional gels for protein sequencing.

Authors:  S M Hanash; J R Strahler; J V Neel; N Hailat; R Melhem; D Keim; X X Zhu; D Wagner; D A Gage; J T Watson
Journal:  Proc Natl Acad Sci U S A       Date:  1991-07-01       Impact factor: 11.205

3.  cDNA and deduced amino acid sequence of rat liver prehsp60 (chaperonin-60).

Authors:  D Peralta; D J Hartman; A M McIntosh; N J Hoogenraad; P B Høj
Journal:  Nucleic Acids Res       Date:  1990-12-11       Impact factor: 16.971

4.  A common evolutionary origin for mitochondria and hydrogenosomes.

Authors:  E T Bui; P J Bradley; P J Johnson
Journal:  Proc Natl Acad Sci U S A       Date:  1996-09-03       Impact factor: 11.205

5.  Primary structure of a human mitochondrial protein homologous to the bacterial and plant chaperonins and to the 65-kilodalton mycobacterial antigen.

Authors:  S Jindal; A K Dudani; B Singh; C B Harley; R S Gupta
Journal:  Mol Cell Biol       Date:  1989-05       Impact factor: 4.272

6.  Protein kinase A-catalyzed phosphorylation of heat shock protein 60 chaperone regulates its attachment to histone 2B in the T lymphocyte plasma membrane.

Authors:  I U Khan; R Wallin; R S Gupta; G M Kammer
Journal:  Proc Natl Acad Sci U S A       Date:  1998-09-01       Impact factor: 11.205

7.  Identification of two related markers for common acute lymphoblastic leukemia as heat shock proteins.

Authors:  J R Strahler; R Kuick; C Eckerskorn; F Lottspeich; B C Richardson; D A Fox; L M Stoolman; C A Hanson; D Nichols; H J Tueche
Journal:  J Clin Invest       Date:  1990-01       Impact factor: 14.808

8.  Cloning and sequence of the gene for heat shock protein 60 from Chlamydia trachomatis and immunological reactivity of the protein.

Authors:  M C Cerrone; J J Ma; R S Stephens
Journal:  Infect Immun       Date:  1991-01       Impact factor: 3.441

9.  Enhancement in amount of P1 (hsp60) in mutants of Chinese hamster ovary (CHO-K1) cells exhibiting increases in the A system of amino acid transport.

Authors:  M Jones; R S Gupta; E Englesberg
Journal:  Proc Natl Acad Sci U S A       Date:  1994-02-01       Impact factor: 11.205

10.  Immunoblot studies in the differential diagnosis of porcine brucellosis: an immunodominant 62 kDa protein is related to the mycobacterial 65 kDa heat shock protein (HSP-65).

Authors:  S A Spencer; E S Broughton; S Hamid; D B Young
Journal:  Vet Microbiol       Date:  1994-03       Impact factor: 3.293

  10 in total

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