PMID: 6409145Jul 29, 1983Paper

Cross-linking of mitochondrial matrix proteins in situ

Biochimica Et Biophysica Acta
S F D'Souza, P A Srere

Abstract

Different cross-linkers (10 mM) of varying specificity and arm length were found to cross-link mitochondria matrix proteins in situ in 2 min at pH 7.4. As seen by SDS-polyacrylamide electrophoresis, the disappearance of individual protein bands was accompanied by concomitant appearance of polymeric aggregates that failed to enter the 4% spacer gel. The disorganization of the mitochondrial matrix infrastructure either by swelling or sonication of the mitochondria resulted in a decrease in the rate of cross-linking. Leakage of citrate synthase, malate dehydrogenase and fumarase was found to be reduced when cross-linked mitochondria were made permeable with toluene. On lysing the cross-linked mitochondria, a major part of the matrix protein (75%) was found to sediment with the membrane fraction. The activities of citrate synthase malate dehydrogenase and fumarase in rat liver mitochondria were also found to increase in the percipitates with concomitant decrease in their activities in the soluble matrix fraction. These results indicate that the cross-linkers enters the mitochondria and cross-links matrix proteins including Krebs cycle enzymes either to the mitochondrial membranes, or to themselves resulting in very large molecular ...Continue Reading

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Citations

Jan 1, 1984·The International Journal of Biochemistry·S Beeckmans
Jan 1, 1989·Bio Systems·A E Lyubarev, B I Kurganov
May 17, 2017·Nature Communications·Youjun ZhangToshihiro Obata
Oct 13, 2006·American Journal of Physiology. Cell Physiology·Giorgio Lenaz, Maria Luisa Genova
Jan 5, 2011·Chemical Communications : Chem Comm·Georgianna L MartinMichael Cooney
Jun 1, 2018·Nature Communications·Lee J Sweetlove, Alisdair R Fernie
Sep 25, 2019·Research : a Science Partner Journal·Alisdair R FernieLee J Sweetlove

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