REGULATING FUNCTION OF COENZYMIZATION AND DECOENZYMIZATION OF THE LACTATE DEHYDROGENASE ISOZYMES IN

来源 :中国医学科学杂志 | 被引量 : 0次 | 上传用户:liu0686
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Objective. To study the characteristics of changes of LDH enzyme patterns of mice under slight hypoxia.Methods. Mice treated with artificial hypoxia, various tissues were made for the test of LDH enzy-matic activity by the specific staining technique. LDH (1-5) relative percentage enzymatic activity(RPEA) were measured with CS-910 dual-wavelength thin layer chromatography scanner.Results. The RPEA of LDH isozymes of various tissues after slight hypoxia shifted to the isozymesLDH1 and LDH2, whose principal subunits are H subunits, and the RPEA of LDH1(H4), LDH2(H3M)increased, while RPEA of LDH5(M4) in vahous tissues decreased prominently except the cardiac muscle,and that of LDH4(HM3) decreased as well. After polyacrylamide gel electrophoresis (PAGE) of the hypox-ia treated cardiac muscle specimen was made, activity subbands originated regularly in the isozyme pat-terns of LDH, with the regularity of LDH1 (0 subband), LDH2 (0-1 subbands), LDH3 (0-2 subbands),LDH4 (1-3 subbands), LDHs (2-4 subbands). After adding appropriate amount of NAD+ to the hypoxiatreated cardiac muscle specimen, PAGE showed the subbands of four isozymes (LDH2-LDH5) reduced oreven totally disappeared in the isozyme patterns.Conclusions. The negative feedback regulation of coenzymization and decoenzymization of LDHisozymes is one of the mouse stress responses to slight hypoxia.
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