Literature DB >> 568001

Reduction and renaturation of hen egg lysozyme containing carboxymethylcysteine-6 and -127.

A S Acharya, H Taniuchi.   

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Year:  1978        PMID： 568001     DOI： 10.1021/bi00608a019

Source DB:  PubMed          Journal:  Biochemistry        ISSN： 0006-2960            Impact factor:   3.162


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  5 in total

1.  On the renaturation of reduced hen egg white lysozyme containing two blocked sulfhydryl groups.

Authors:  A S Acharya; H Taniuchi
Journal:  Biophys J       Date:  1980-10       Impact factor: 4.033

2.  Controlled release of functional proteins through designer self-assembling peptide nanofiber hydrogel scaffold.

Authors:  Sotirios Koutsopoulos; Larry D Unsworth; Yusuke Nagai; Shuguang Zhang
Journal:  Proc Natl Acad Sci U S A       Date:  2009-03-09       Impact factor: 11.205

Review 3.  Implication of the structure and stability of disulfide intermediates of lysozyme on the mechanism of renaturation.

Authors:  A S Acharya; H Taniuchi
Journal:  Mol Cell Biochem       Date:  1982-05-14       Impact factor: 3.396

4.  Spectroscopic, immunochemical, and thermodynamic properties of carboxymethyl(Cys6, Cys127)-hen egg white lysozyme.

Authors:  M E Denton; H A Scheraga
Journal:  J Protein Chem       Date:  1991-04

5.  Local interactions favor the native 8-residue disulfide loop in the oxidation of a fragment corresponding to the sequence Ser-50-Met-79 derived from bovine pancreatic ribonuclease A.

Authors:  P J Milburn; H A Scheraga
Journal:  J Protein Chem       Date:  1988-08
  5 in total

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