Characterization of refolded hen lysozyme variant lacking two outside disulfide bonds

Takatoshi Ohkuri; Taiji Imoto; Tadashi Ueda

doi:10.1271/bbb.69.1206

Characterization of refolded hen lysozyme variant lacking two outside disulfide bonds

Takatoshi Ohkuri, Taiji Imoto, Tadashi Ueda

Pharmaceutical Health Care and Sciences

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

Abstract

We characterized a refolded hen lysozyme variant containing only two SS-bonds, C64-C80 and C76-C94 (4CAHEL). From CD spectra and its activity, it was found that the refolded 4CAHEL has a structural topology analogous to wild-type lysozyme (WTHEL). Moreover, the refolded 4CAHEL showed no thermal transition, indicating that it had a character like a molten globule.

Original language	English
Pages (from-to)	1206-1208
Number of pages	3
Journal	Bioscience, Biotechnology and Biochemistry
Volume	69
Issue number	6
DOIs	https://doi.org/10.1271/bbb.69.1206
Publication status	Published - Jun 2005

All Science Journal Classification (ASJC) codes

Biotechnology
Analytical Chemistry
Biochemistry
Applied Microbiology and Biotechnology
Molecular Biology
Organic Chemistry

Access to Document

10.1271/bbb.69.1206

Cite this

@article{f64001a9639144e8bab20722fb74d291,

title = "Characterization of refolded hen lysozyme variant lacking two outside disulfide bonds",

abstract = "We characterized a refolded hen lysozyme variant containing only two SS-bonds, C64-C80 and C76-C94 (4CAHEL). From CD spectra and its activity, it was found that the refolded 4CAHEL has a structural topology analogous to wild-type lysozyme (WTHEL). Moreover, the refolded 4CAHEL showed no thermal transition, indicating that it had a character like a molten globule.",

author = "Takatoshi Ohkuri and Taiji Imoto and Tadashi Ueda",

year = "2005",

month = jun,

doi = "10.1271/bbb.69.1206",

language = "English",

volume = "69",

pages = "1206--1208",

journal = "Bioscience, Biotechnology and Biochemistry",

issn = "0916-8451",

publisher = "Japan Society for Bioscience Biotechnology and Agrochemistry",

number = "6",

}

TY - JOUR

T1 - Characterization of refolded hen lysozyme variant lacking two outside disulfide bonds

AU - Ohkuri, Takatoshi

AU - Imoto, Taiji

AU - Ueda, Tadashi

PY - 2005/6

Y1 - 2005/6

N2 - We characterized a refolded hen lysozyme variant containing only two SS-bonds, C64-C80 and C76-C94 (4CAHEL). From CD spectra and its activity, it was found that the refolded 4CAHEL has a structural topology analogous to wild-type lysozyme (WTHEL). Moreover, the refolded 4CAHEL showed no thermal transition, indicating that it had a character like a molten globule.

AB - We characterized a refolded hen lysozyme variant containing only two SS-bonds, C64-C80 and C76-C94 (4CAHEL). From CD spectra and its activity, it was found that the refolded 4CAHEL has a structural topology analogous to wild-type lysozyme (WTHEL). Moreover, the refolded 4CAHEL showed no thermal transition, indicating that it had a character like a molten globule.

UR - http://www.scopus.com/inward/record.url?scp=22444443364&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=22444443364&partnerID=8YFLogxK

U2 - 10.1271/bbb.69.1206

DO - 10.1271/bbb.69.1206

M3 - Article

C2 - 15973056

AN - SCOPUS:22444443364

SN - 0916-8451

VL - 69

SP - 1206

EP - 1208

JO - Bioscience, Biotechnology and Biochemistry

JF - Bioscience, Biotechnology and Biochemistry

IS - 6

ER -

Characterization of refolded hen lysozyme variant lacking two outside disulfide bonds

Abstract

All Science Journal Classification (ASJC) codes

Access to Document

Other files and links

Fingerprint

Cite this