Cellular mixed disulphides between thiols and proteins, and their possible implication for radiation protection

Modig, Hans

doi:10.1016/0006-2952(68)90321-3

Cited by 88 publications

(28 citation statements)

References 28 publications

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“…Considering the possibility that the inactivation of tyrosine aminotransferase may have been due to mixed-disulphide formation, it is noteworthy that mixed disulphides of proteins with low-molecular-weight thiol compounds, including glutathione and cysteine, have been identi-fied in a variety of tissues (Modig, 1968;Harrap et al, 1973).…”

Section: Discussionmentioning

confidence: 99%

Participation of cysteine and cystine in inactivation of tyrosine aminotransferase in rat liver homogenates

Buckley¹,

Milligan²

1978

Biochemical Journal

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1. Inactivation of tyrosine aminotransferase was studied in rat liver homogenates. Under an 02 atmosphere with cysteine added, inactivation was rapid after a lag period of approx. 1 h, whereas a N2 atmosphere extended the lag period to approx. 3 h. 2. Replacement of cysteine with cystine resulted in rapid inactivation both aerobically and anaerobically. 3. Removal of the particulate fraction by centrifuging rat liver homogenates at 13 00Og for 9min resulted in an aerobic lag period of 0.5 h in the presence of cystine and approx. 3 h in the presence of cysteine. 4. It is proposed that the stimulatory effect of cysteine on tyrosine aminotransferase inactivation occurs largely as a result of oxidation to cystine, which appears to be a more directly effective agent.

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Section: Discussionmentioning

confidence: 99%

Participation of cysteine and cystine in inactivation of tyrosine aminotransferase in rat liver homogenates

Buckley¹,

Milligan²

1978

Biochemical Journal

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“…A standard method for measuring PrSSG is that described by Akerboom and Sies (1981) and by Modig (1968). Tissue proteins are isolated by precipitation with perchloric acid (PCA) and rinsed to remove endogenous GSH and GSSG.…”

Section: Experimental Studies: (Part II Methodology For Prssg)mentioning

confidence: 99%

Reversal of Mitochondrial Damage Caused by Environmental Neurotoxins

Cohen¹

1999

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“…6 mCi/mmole), purchased from Amersham, was dissolved in triple-distilled, deionized water before use . Binding of 35S-cysteamine to cellular proteins was measured by the procedure of Modig (1968) .…”

Section: Methodsmentioning

confidence: 99%

“…Some workers believe that radical scavenging and electrondonation reactions account for cysteamine's protective efplcacy ; others that the amino-thiol forms a mixed disulphide with protein-bound sulphydryl groups and that this confers protection (Eldjarn and Pihl 1960) . Modig and his coworkers proposed a variation on the latter theme, hypothesizing that formation of the mixed disulphide releases glutathione from binding sites on cellular proteins and that this glutathione is the protector (Revesz and Modig 1965, Modig 1968 .…”

Section: Introductionmentioning

confidence: 99%