Literature DB >> 6383975

Denatured proteins are degraded more rapidly than abnormal proteins in cell-free extracts of Saccharomyces cerevisiae.

A K Chopra, J Chaloupka.   

Abstract

Abnormal proteins synthesized in the presence of ethionine were degraded more rapidly than the normal ones in cell-free extracts of ethanol-grown yeast. The denatured proteins, however, were degraded in preference to their native counterparts which were either normal or abnormal.

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Year:  1984        PMID： 6383975     DOI： 10.1007/bf02875968

Source DB:  PubMed          Journal:  Folia Microbiol (Praha)        ISSN： 0015-5632            Impact factor:   2.099


  5 in total

Review 1.  Intracellular proteinases in microorganisms.

Authors:  H Holzer; H Betz; E Ebner
Journal:  Curr Top Cell Regul       Date:  1975

2.  Degradation of abnormal proteins in Escherichia coli: relative susceptibility of canavanyl proteins and puromycin peptides to proteolysis in vitro.

Authors:  J T Kemshead; A R Hipkiss
Journal:  Eur J Biochem       Date:  1974-06-15

Review 3.  Intracellular protein degradation in mammalian and bacterial cells: Part 2.

Authors:  A L Goldberg; A C St John
Journal:  Annu Rev Biochem       Date:  1976       Impact factor: 23.643

4.  Intracellular proteolytic activity during sporulation of Bacillus megaterium.

Authors:  J Chaloupka; M Strnadová; V Zalabák
Journal:  Folia Microbiol (Praha)       Date:  1977       Impact factor: 2.099

5.  Properties of abnormal proteins degraded rapidly in reticulocytes. Intracellular aggregation of the globin molecules prior to hydrolysis.

Authors:  Y Klemes; J D Etlinger; A L Goldberg
Journal:  J Biol Chem       Date:  1981-08-25       Impact factor: 5.157
  5 in total

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