Font, Bernard published the artcileInteraction of creatine kinase and hexokinase with the mitochondrial membranes, and self-association of creatine kinase: crosslinking studies, Related Products of alcohols-buliding-blocks, the publication is Molecular and Cellular Biochemistry (1987), 78(2), 131-40, database is CAplus and MEDLINE.
Covalent coupling of protein by crosslinking reagents has been used to study the interaction of mitochondrial creatine kinase (CKm) and hexokinase (HK) with the mitochondrial membranes. The effects of crosslinkers were studied either by following the inhibition of solubilization of enzymic activities or by modification of the electrophoretic patterns of proteins solubilized from mitochondria after treatment with different crosslinkers. Dimethylsuberimidate (DMS) efficiently reduced the amount of HK activity solubilized by various agents but it did not modify solubilization of CKm from mitochondria. The effect of DMS on HK solubilization did not result from nonspecific crosslinking since it did not impede the solubilization of adenylate kinase. The bissuccinimidyl class of crosslinkers was also tested. Ethyleneglycolbis(succinimidylsuccinate) (EGS) efficiently reduced HK solubilization, but it addnl. induced osmotic stabilization of mitochondria and thus impeded release of soluble or solubilized proteins from the intermembrane space. Furthermore, this agent drastically inhibited CKm activity and thus, in a second set of experiments the effect of crosslinkers were studied by the disappearance of protein bands in the electrophoretic pattern of soluble fractions obtained from mitochondria, the outer membranes of which have been ruptured to allow free release of soluble proteins. Results of these experiments showed that succinimidyl reagents and Cu2+-phenanthroline substantially reduced the amount of CKm released from mitochondria and confirmed that bisimidates were ineffective in inhibiting CKm solubilization. In addition, crosslinking reagents were used to study subunit interactions in purified CKm. The results showed, in contrast with control experiments with a monomeric protein (ovalbumin) which did not give rise to polymers, that under the same conditions, electrophoresis of crosslinked CKm resolved a set of species with mol. weights roughly equal to integral multiples of the protomer. These results prove that the polymeric form of CKm is an octamer.
Molecular and Cellular Biochemistry published new progress about 70539-42-3. 70539-42-3 belongs to alcohols-buliding-blocks, auxiliary class pyrrolidine,Ester,Amide,Inhibitor,Inhibitor, name is Bis(2,5-dioxopyrrolidin-1-yl) O,O’-ethane-1,2-diyl disuccinate, and the molecular formula is C18H20N2O12, Related Products of alcohols-buliding-blocks.
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