Literature DB >> 592421

On the cysteine and cystine content of proteins. Differences between intracellular and extracellular proteins.

R C Fahey, J S Hunt, G C Windham.   

Abstract

Analysis of published data on the cysteine and half-cystine content of proteins indicates that most intracellular proteins may be classified as sulfhydryl proteins (those containing cysteine but little or no half-cystine) and that such sulfhydryl proteins have a low cysteine content. The mean systeine content found for 32 intracellular mammalian proteins was 1.6% and intracellular proteins of many bacteria have similar or lower values. Extracellular mammalian proteins are primarily disulfide proteins (those containing half-cystine but little or no cysteine) have a high half-cystine content, the mean value found for some 34 extracellular mammalian proteins being 4.1%. This is contrasted with many of the extracellular proteins from facultative bacteria which are cyst(e)ine-free proteins, being lacking in both cysteine and half-cystine. These and related observations are interpreted in terms of the evolution of life in a reducing atmosphere and the subsequent transition to an oxidizing environment. It is suggested that disulfide proteins evolved primarily after the accumulation of oxygen in the atmosphere.

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Year:  1977        PMID: 592421     DOI: 10.1007/bf01751808

Source DB:  PubMed          Journal:  J Mol Evol        ISSN: 0022-2844            Impact factor:   2.395


  20 in total

1.  Low cyst(e)ine content of bacterial extracellular proteins: its possible physiological significance.

Authors:  M R POLLOCK; M H RICHMOND
Journal:  Nature       Date:  1962-05-05       Impact factor: 49.962

2.  Conservation of Shannon's redundancy for proteins.

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3.  Purification and properties of clostridiopeptidase B (Clostripain).

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4.  Amino acid composition of proteins as a product of molecular evolution.

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5.  Genetic variability maintained in a finite population due to mutational production of neutral and nearly neutral isoalleles.

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6.  Primary structure of alpha-lytic protease: a bacterial homologue of the pancreatic serine proteases.

Authors:  M O Olson; N Nagabhushan; M Dzwiniel; L B Smillie; D R Whitaker
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7.  Amino acid sequence of Streptomyces griseus trypsin. Cyanogen bromide fragments and complete sequence.

Authors:  R W Olafson; L Jurásek; M R Carpenter; L B Smillie
Journal:  Biochemistry       Date:  1975-03-25       Impact factor: 3.162

8.  The elastase-like enzymes from Streptomyces griseus (pronase). Isolation and partial characterization.

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9.  Primary structural analysis of sulfhydryl protease inhibitors from pineapple stem.

Authors:  M N Reddy; P S Keim; R L Heinrikson; F J Kezdy
Journal:  J Biol Chem       Date:  1975-03-10       Impact factor: 5.157

10.  [Purification and characterization of an extracellular protease from Staphylococcus aureus inhibited by EDTA].

Authors:  S A Saheb
Journal:  Biochimie       Date:  1976       Impact factor: 4.079

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  31 in total

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6.  Organocatalysts of oxidative protein folding inspired by protein disulfide isomerase.

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Review 7.  The purification of eukaryotic polypeptides synthesized in Escherichia coli.

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Review 8.  Strategies for achieving high-level expression of genes in Escherichia coli.

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Journal:  Microbiol Rev       Date:  1996-09

9.  cDNAs for the postsynaptic 43-kDa protein of Torpedo electric organ encode two proteins with different carboxyl termini.

Authors:  D E Frail; J Mudd; V Shah; C Carr; J B Cohen; J P Merlie
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10.  Protein disulfide-isomerase interacts with soluble guanylyl cyclase via a redox-based mechanism and modulates its activity.

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