Formation and cleavage of mixed disulfide hemoglobin glutathione in intact erythrocytes

Satish Srivastava, E. Beutler

Research output: Contribution to journalArticle

Abstract

A marked decrease in the level of GSH was observed in human erythrocytes incubated with glucose in the presence of acetyl phenylhydrazine. All the GSH lost could not be accounted for as GSSG. After washing and reincubation of the erythrocytes with phosphate saline containing glucose, almost 80% of the GSH could be recovered. The rate of appearance of GSH was much faster when inosine and adenine were also incorporated in the incubation medium. The results of these studies, taken together with previous studies of GSH Hb mixed disulfide, suggest that in the presence of acetyl phenylhydrazine, a portion of GSH oxidized becomes bound to haemoglobin or other proteins in the form of mixed disulfide. GSH from the mixed disulfide is released in the presence of NADPH and glutathione reductase.

Original languageEnglish
Pages (from-to)121-125
Number of pages5
JournalHaematologia
Volume8
Issue number1-4
StatePublished - 1974
Externally publishedYes

Fingerprint

Glutathione Disulfide
Disulfides
Hemoglobins
Erythrocytes
Glucose
Inosine
Glutathione Reductase
Adenine
NADP
Phosphates
Proteins
phenylhydrazine

ASJC Scopus subject areas

  • Hematology

Cite this

Formation and cleavage of mixed disulfide hemoglobin glutathione in intact erythrocytes. / Srivastava, Satish; Beutler, E.

In: Haematologia, Vol. 8, No. 1-4, 1974, p. 121-125.

Research output: Contribution to journalArticle

Srivastava, S & Beutler, E 1974, 'Formation and cleavage of mixed disulfide hemoglobin glutathione in intact erythrocytes', Haematologia, vol. 8, no. 1-4, pp. 121-125.
Srivastava, Satish ; Beutler, E. / Formation and cleavage of mixed disulfide hemoglobin glutathione in intact erythrocytes. In: Haematologia. 1974 ; Vol. 8, No. 1-4. pp. 121-125.
@article{6a0db5f70e1243ab89f1c7190bad2621,
title = "Formation and cleavage of mixed disulfide hemoglobin glutathione in intact erythrocytes",
abstract = "A marked decrease in the level of GSH was observed in human erythrocytes incubated with glucose in the presence of acetyl phenylhydrazine. All the GSH lost could not be accounted for as GSSG. After washing and reincubation of the erythrocytes with phosphate saline containing glucose, almost 80{\%} of the GSH could be recovered. The rate of appearance of GSH was much faster when inosine and adenine were also incorporated in the incubation medium. The results of these studies, taken together with previous studies of GSH Hb mixed disulfide, suggest that in the presence of acetyl phenylhydrazine, a portion of GSH oxidized becomes bound to haemoglobin or other proteins in the form of mixed disulfide. GSH from the mixed disulfide is released in the presence of NADPH and glutathione reductase.",
author = "Satish Srivastava and E. Beutler",
year = "1974",
language = "English",
volume = "8",
pages = "121--125",
journal = "Haematologia",
issn = "0017-6559",
publisher = "VSP BV",
number = "1-4",

}

TY - JOUR

T1 - Formation and cleavage of mixed disulfide hemoglobin glutathione in intact erythrocytes

AU - Srivastava, Satish

AU - Beutler, E.

PY - 1974

Y1 - 1974

N2 - A marked decrease in the level of GSH was observed in human erythrocytes incubated with glucose in the presence of acetyl phenylhydrazine. All the GSH lost could not be accounted for as GSSG. After washing and reincubation of the erythrocytes with phosphate saline containing glucose, almost 80% of the GSH could be recovered. The rate of appearance of GSH was much faster when inosine and adenine were also incorporated in the incubation medium. The results of these studies, taken together with previous studies of GSH Hb mixed disulfide, suggest that in the presence of acetyl phenylhydrazine, a portion of GSH oxidized becomes bound to haemoglobin or other proteins in the form of mixed disulfide. GSH from the mixed disulfide is released in the presence of NADPH and glutathione reductase.

AB - A marked decrease in the level of GSH was observed in human erythrocytes incubated with glucose in the presence of acetyl phenylhydrazine. All the GSH lost could not be accounted for as GSSG. After washing and reincubation of the erythrocytes with phosphate saline containing glucose, almost 80% of the GSH could be recovered. The rate of appearance of GSH was much faster when inosine and adenine were also incorporated in the incubation medium. The results of these studies, taken together with previous studies of GSH Hb mixed disulfide, suggest that in the presence of acetyl phenylhydrazine, a portion of GSH oxidized becomes bound to haemoglobin or other proteins in the form of mixed disulfide. GSH from the mixed disulfide is released in the presence of NADPH and glutathione reductase.

UR - http://www.scopus.com/inward/record.url?scp=0016306311&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0016306311&partnerID=8YFLogxK

M3 - Article

C2 - 4461419

AN - SCOPUS:0016306311

VL - 8

SP - 121

EP - 125

JO - Haematologia

JF - Haematologia

SN - 0017-6559

IS - 1-4

ER -