Effect of thiol modification on the thermal stability of erythrocyte membranes

Z. Jóźwiak; M. Gaczynska; M. Soszynski

doi:10.1016/0306-4565(94)90062-0

Effect of thiol modification on the thermal stability of erythrocyte membranes

Z. Jóźwiak, M. Gaczynska, M. Soszynski

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

Abstract

1. 1.|The effect of chemical modification of membrane proteins on the heat response of erythrocytes has been studied. 2. 2.|Erythrocytes preincubated with N-ethylmaleimide (NEM) or p-chloromercuribenzoic acid (pCMB), followed by heating at temperatures above 44°C, indicated a decreased thermal stability. 3. 3.|The action of pCMB is much more toxic to erythrocytes than the effect of NEM. 4. 4.|These results suggest that modification of proteins by SH reagents could be responsible for changes in the structural integrity of pig erythrocyte plasma membrane leading to their reduced thermal stability.

Original language	English (US)
Pages (from-to)	141-147
Number of pages	7
Journal	Journal of Thermal Biology
Volume	19
Issue number	2
DOIs	https://doi.org/10.1016/0306-4565(94)90062-0
State	Published - Apr 1994
Externally published	Yes

Keywords

Erythrocytes
SH reagents
heat
membrane proteins
thermal stability

ASJC Scopus subject areas

Biochemistry
Physiology
Agricultural and Biological Sciences(all)
Developmental Biology

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10.1016/0306-4565(94)90062-0

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title = "Effect of thiol modification on the thermal stability of erythrocyte membranes",

abstract = "1. 1.|The effect of chemical modification of membrane proteins on the heat response of erythrocytes has been studied. 2. 2.|Erythrocytes preincubated with N-ethylmaleimide (NEM) or p-chloromercuribenzoic acid (pCMB), followed by heating at temperatures above 44°C, indicated a decreased thermal stability. 3. 3.|The action of pCMB is much more toxic to erythrocytes than the effect of NEM. 4. 4.|These results suggest that modification of proteins by SH reagents could be responsible for changes in the structural integrity of pig erythrocyte plasma membrane leading to their reduced thermal stability.",

keywords = "Erythrocytes, SH reagents, heat, membrane proteins, thermal stability",

author = "Z. J{\'o}{\'z}wiak and M. Gaczynska and M. Soszynski",

year = "1994",

month = apr,

doi = "10.1016/0306-4565(94)90062-0",

language = "English (US)",

volume = "19",

pages = "141--147",

journal = "Journal of Thermal Biology",

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TY - JOUR

T1 - Effect of thiol modification on the thermal stability of erythrocyte membranes

AU - Jóźwiak, Z.

AU - Gaczynska, M.

AU - Soszynski, M.

PY - 1994/4

Y1 - 1994/4

N2 - 1. 1.|The effect of chemical modification of membrane proteins on the heat response of erythrocytes has been studied. 2. 2.|Erythrocytes preincubated with N-ethylmaleimide (NEM) or p-chloromercuribenzoic acid (pCMB), followed by heating at temperatures above 44°C, indicated a decreased thermal stability. 3. 3.|The action of pCMB is much more toxic to erythrocytes than the effect of NEM. 4. 4.|These results suggest that modification of proteins by SH reagents could be responsible for changes in the structural integrity of pig erythrocyte plasma membrane leading to their reduced thermal stability.

AB - 1. 1.|The effect of chemical modification of membrane proteins on the heat response of erythrocytes has been studied. 2. 2.|Erythrocytes preincubated with N-ethylmaleimide (NEM) or p-chloromercuribenzoic acid (pCMB), followed by heating at temperatures above 44°C, indicated a decreased thermal stability. 3. 3.|The action of pCMB is much more toxic to erythrocytes than the effect of NEM. 4. 4.|These results suggest that modification of proteins by SH reagents could be responsible for changes in the structural integrity of pig erythrocyte plasma membrane leading to their reduced thermal stability.

KW - Erythrocytes

KW - SH reagents

KW - heat

KW - membrane proteins

KW - thermal stability

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DO - 10.1016/0306-4565(94)90062-0

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JO - Journal of Thermal Biology

JF - Journal of Thermal Biology

SN - 0306-4565

IS - 2

ER -

Effect of thiol modification on the thermal stability of erythrocyte membranes

Abstract

Keywords

ASJC Scopus subject areas

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