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

A. Seetharama Acharya; Hiroshi Taniuchi

doi:10.1007/BF00238502

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

A. Seetharama Acharya, Hiroshi Taniuchi

Medicine

Research output: Contribution to journal › Article › peer-review

33 Scopus citations

Abstract

The conformational properties and stability of reduced hen egg lysozyme and those of the disulfide intermediates species formed during renaturation of reduced lysozyme have been reviewed. This information and that related with RNase A and other proteins are interpreted to outline a possible mechanism of renaturation of the reduced protein.

Original language	English (US)
Pages (from-to)	129-148
Number of pages	20
Journal	Molecular and Cellular Biochemistry
Volume	44
Issue number	3
DOIs	https://doi.org/10.1007/BF00238502
State	Published - May 1982

ASJC Scopus subject areas

Molecular Biology
Clinical Biochemistry
Cell Biology

Access to Document

10.1007/BF00238502

Cite this

@article{dd25450c69bf4d63af7fa8afd3902c30,

title = "Implication of the structure and stability of disulfide intermediates of lysozyme on the mechanism of renaturation",

abstract = "The conformational properties and stability of reduced hen egg lysozyme and those of the disulfide intermediates species formed during renaturation of reduced lysozyme have been reviewed. This information and that related with RNase A and other proteins are interpreted to outline a possible mechanism of renaturation of the reduced protein.",

author = "Acharya, {A. Seetharama} and Hiroshi Taniuchi",

year = "1982",

month = may,

doi = "10.1007/BF00238502",

language = "English (US)",

volume = "44",

pages = "129--148",

journal = "Molecular and Cellular Biochemistry",

issn = "0300-8177",

publisher = "Springer Netherlands",

number = "3",

}

TY - JOUR

T1 - Implication of the structure and stability of disulfide intermediates of lysozyme on the mechanism of renaturation

AU - Acharya, A. Seetharama

AU - Taniuchi, Hiroshi

PY - 1982/5

Y1 - 1982/5

N2 - The conformational properties and stability of reduced hen egg lysozyme and those of the disulfide intermediates species formed during renaturation of reduced lysozyme have been reviewed. This information and that related with RNase A and other proteins are interpreted to outline a possible mechanism of renaturation of the reduced protein.

AB - The conformational properties and stability of reduced hen egg lysozyme and those of the disulfide intermediates species formed during renaturation of reduced lysozyme have been reviewed. This information and that related with RNase A and other proteins are interpreted to outline a possible mechanism of renaturation of the reduced protein.

UR - http://www.scopus.com/inward/record.url?scp=0020482089&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0020482089&partnerID=8YFLogxK

U2 - 10.1007/BF00238502

DO - 10.1007/BF00238502

M3 - Article

C2 - 7050652

AN - SCOPUS:0020482089

SN - 0300-8177

VL - 44

SP - 129

EP - 148

JO - Molecular and Cellular Biochemistry

JF - Molecular and Cellular Biochemistry

IS - 3

ER -

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

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this