[Coenzyme specificity and isoenzyme spectrum of lactate dehydrogenase from different regions of the brain].
The coenzyme affinity of lactate dehydrogenase of various parts of rat brain is different to deamino-NAD and NAD as well as to their reduced forms. In direct reactions NAD exhibits a higher activity than deamino-NAD. In the reverse reaction an opposite pattern is observed. The effect of deamino-NADH is much higher than that of NADH. Our studies have shown that the isoenzymes of LDH which are richer in H subunits have a higher affinity for deamino-NAD and deamino-NADH than for NAD and NADH. The isoenzymes of LDH that contain more M forms have opposite properties. LDH-3 does not show a pronounced selective affinity. The data obtained indicate that the activity of LDH and of its 5 isoenzymes varies greatly in different brain parts; crucial changes being observed in the relative percentage of molecular forms of LDH.
D000818:Animals; D001921:Brain / Q000201:enzymology*; D002531:Cerebellum / Q000201:enzymology; D003067:Coenzymes / Q000378:metabolism; D007031:Hypothalamus / Q000201:enzymology; D007527:Isoenzymes; D007770:L-Lactate Dehydrogenase / Q000302:isolation & purification / Q000378:metabolism*; D008526:Medulla Oblongata / Q000201:enzymology; D008722:Methods; D009243:NAD / Q000031:analogs & derivatives; D010870:Pineal Gland / Q000201:enzymology; D010902:Pituitary Gland / Q000201:enzymology; D051381:Rats; D013116:Spinal Cord / Q000201:enzymology
D003067:Coenzymes; D007527:Isoenzymes; D009243:NAD; D007770:L-Lactate Dehydrogenase
Kofermentnaia spetsifichnost' i izofermentnyĭ nabor laktatdegidrogenazy razlichnykh otdelov mozga