Literature DB >> 99936

Intracellular protein catabolism. IX. Hydrophobicity of substrate proteins is a molecular basis of selectivity.

P Bohley, S Riemann.   

Abstract

Double-labeled cytosol proteins from rat liver (3H in short-lived, 14C in long-lived proteins) were fractionated by using siliconized glass-beads, phenylsepharose and octylsepharose. Always the short-lived proteins are more tightly bound to the hydrophobic matrix. The same distribution was found with monkey liver substrate proteins. Therefore it is concluded that the different degrees of exposure of superficial hydrophobic areas on substrate protein molecules are a molecular basis of selectivity of the intracellular protein catabolism.

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Year:  1977        PMID: 99936

Source DB:  PubMed          Journal:  Acta Biol Med Ger        ISSN: 0001-5318


  3 in total

Review 1.  The fates of proteins in cells.

Authors:  P Bohley
Journal:  Naturwissenschaften       Date:  1995-12

2.  Adsorptive pinocytosis of 125I-labelled lactate dehydrogenase isoenzymes H4 and M4 by rat yolk sacs incubated in vitro.

Authors:  T Kooistra; K E Williams
Journal:  Biochem J       Date:  1981-09-15       Impact factor: 3.857

3.  Endocytosis and breakdown of 125I-labelled lactate dehydrogenase isoenzyme M4 by rat liver and spleen in vivo.

Authors:  J Sinke; J M Bouma; T Kooistra; M Gruber
Journal:  Biochem J       Date:  1979-04-15       Impact factor: 3.857

  3 in total

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