Abstract
The disulfide-sulfhydryl (SS/SH) ratios of subcellular fractions of rat hepatic tissues were found to vary diurnally with the ratio lowest in the early morning and highest in the early evening. These changes were found in the nuclear, microsomal and cytosol fractions. The primary reaction is the reversible formation of mixed disulfides of glutathione with proteins. This formation is controlled by the activity of thiol transferase and the level of oxidized glutathione (GSSG) as substrate. Several enzymes including mitochondrial and microsomal oxidases, glutathione reductase and peroxidase and glucose-6-phosphate dehydrogenase were found to control the levels of GSSG. An NADPH-dependent microsomal oxidase system, inhibited by GSSG, was found to produce activated oxygen which served as substrate for glutathione peroxidase. Evidence is presented for the concept that the formation of mixed disulfides of proteins with glutathione is a mechanism for maintenance of a disulfide-sulfhydryl ratio such that the integrity of particulate membranes is maintained during oxidative and reductive stresses on the hepatic cells.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 192-204 |
| Number of pages | 13 |
| Journal | Biochimica et Biophysica Acta - General Subjects |
| Volume | 497 |
| Issue number | 1 |
| DOIs | |
| State | Published - Mar 29 1977 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology
- Medicine(all)
Cite this
Glutathione dependent control of protein disulfide-sulfhydryl content by subcellular fractions of hepatic tissue. / Isaacs, John Tod; Binkley, Francis.
In: Biochimica et Biophysica Acta - General Subjects, Vol. 497, No. 1, 29.03.1977, p. 192-204.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Glutathione dependent control of protein disulfide-sulfhydryl content by subcellular fractions of hepatic tissue
AU - Isaacs, John Tod
AU - Binkley, Francis
PY - 1977/3/29
Y1 - 1977/3/29
N2 - The disulfide-sulfhydryl (SS/SH) ratios of subcellular fractions of rat hepatic tissues were found to vary diurnally with the ratio lowest in the early morning and highest in the early evening. These changes were found in the nuclear, microsomal and cytosol fractions. The primary reaction is the reversible formation of mixed disulfides of glutathione with proteins. This formation is controlled by the activity of thiol transferase and the level of oxidized glutathione (GSSG) as substrate. Several enzymes including mitochondrial and microsomal oxidases, glutathione reductase and peroxidase and glucose-6-phosphate dehydrogenase were found to control the levels of GSSG. An NADPH-dependent microsomal oxidase system, inhibited by GSSG, was found to produce activated oxygen which served as substrate for glutathione peroxidase. Evidence is presented for the concept that the formation of mixed disulfides of proteins with glutathione is a mechanism for maintenance of a disulfide-sulfhydryl ratio such that the integrity of particulate membranes is maintained during oxidative and reductive stresses on the hepatic cells.
AB - The disulfide-sulfhydryl (SS/SH) ratios of subcellular fractions of rat hepatic tissues were found to vary diurnally with the ratio lowest in the early morning and highest in the early evening. These changes were found in the nuclear, microsomal and cytosol fractions. The primary reaction is the reversible formation of mixed disulfides of glutathione with proteins. This formation is controlled by the activity of thiol transferase and the level of oxidized glutathione (GSSG) as substrate. Several enzymes including mitochondrial and microsomal oxidases, glutathione reductase and peroxidase and glucose-6-phosphate dehydrogenase were found to control the levels of GSSG. An NADPH-dependent microsomal oxidase system, inhibited by GSSG, was found to produce activated oxygen which served as substrate for glutathione peroxidase. Evidence is presented for the concept that the formation of mixed disulfides of proteins with glutathione is a mechanism for maintenance of a disulfide-sulfhydryl ratio such that the integrity of particulate membranes is maintained during oxidative and reductive stresses on the hepatic cells.
UR - http://www.scopus.com/inward/record.url?scp=0017339770&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0017339770&partnerID=8YFLogxK
U2 - 10.1016/0304-4165(77)90152-0
DO - 10.1016/0304-4165(77)90152-0
M3 - Article
C2 - 557349
AN - SCOPUS:0017339770
VL - 497
SP - 192
EP - 204
JO - Biochimica et Biophysica Acta - General Subjects
JF - Biochimica et Biophysica Acta - General Subjects
SN - 0304-4165
IS - 1
ER -