Literature DB >> 1270441

Formation of three-dimensional structure in protein fragments. Reactivation of reduced hen egg lysozyme fragment 1-127.

E R Johnson, K J Oh, D B Wetlaufer.   

Abstract

Regeneration of enzymic activity from reduced hen egg lysozyme peptide 1-127 was effected with a glutathione oxidation-reduction buffer. The rate of regeneration was nearly as great for peptide 1-127 as for reduced lysozyme itself, and the yields were the same (greater than 80%). The regenerated fragment 1-127 was shown to be indistinguishable from fragment 1-127 before reduction by ion exchange chromatography, amino acid analysis, polyacrylamide gel electrophoresis, and disulfide analysis. These results show that the COOH-terminal dipeptide Arg-Leu is not essential for the acquisition of the native three-dimensional structure of lysozyme.

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Year:  1976        PMID: 1270441

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


  3 in total

1.  Formation of the four isomers of hen egg white lysozyme containing three negative disulfide bonds and one open disulfide bond.

Authors:  A S Acharya; H Taniuchi
Journal:  Proc Natl Acad Sci U S A       Date:  1977-06       Impact factor: 11.205

Review 2.  The problem of the stability globular proteins.

Authors:  W Pfeil
Journal:  Mol Cell Biochem       Date:  1981-10-09       Impact factor: 3.396

3.  Reoxidation of reduced hen egg white lysozyme fragment 1-123.

Authors:  Y Looze; A Vizet; J P Perraudin; J Depreter; M Deconinck; A G Schnek; J Léonis
Journal:  Experientia       Date:  1978-08-15
  3 in total

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