
FOLLOWUS
1. College of Life Sciences
2. College of Chemistry & Molecular Engineering
3. Peking University
4. ,China
纸质出版日期:2003
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[1]袁明秀,蒋晖,邓爱萍,周晴中.REGULATING FUNCTION OF COENZYMIZATION AND DECOENZYMIZATION OF THE LACTATE DEHYDROGENASE ISOZYMES IN THE MOUSE TISSUES DURING HYPOXIA[J].Chinese Medical Sciences Journal,2003(02):128-131.
REGULATING FUNCTION OF COENZYMIZATION AND DECOENZYMIZATION OF THE LACTATE DEHYDROGENASE ISOZYMES IN THE MOUSE TISSUES DURING HYPOXIA[J]. Chinese medical sciences journal, 2003, (2): 128-131.
[1]袁明秀,蒋晖,邓爱萍,周晴中.REGULATING FUNCTION OF COENZYMIZATION AND DECOENZYMIZATION OF THE LACTATE DEHYDROGENASE ISOZYMES IN THE MOUSE TISSUES DURING HYPOXIA[J].Chinese Medical Sciences Journal,2003(02):128-131. DOI:
REGULATING FUNCTION OF COENZYMIZATION AND DECOENZYMIZATION OF THE LACTATE DEHYDROGENASE ISOZYMES IN THE MOUSE TISSUES DURING HYPOXIA[J]. Chinese medical sciences journal, 2003, (2): 128-131. DOI:
<正> 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 enzymatic 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 isozymes LDH1 and LDH2
whose principal subunits are H subunits
and the RPEA of LDH
(H4)
LDH2(H3M) increased
while RPEA of LDH5(M4) in various tissues decreased prominently except the cardiac muscle
and that of LDH4(HM3) decreased as well. After polyacrylamide gel electrophoresis (PAGE) of the hypoxia treated cardiac muscle specimen was made
activity subbands originated regularly in the isozyme patterns of LDH
with the regularity of LDH1 (0 subband)
LDH2 (0-1 subbands)
LDH3 (0-2 subbands)
LDH4 (1-3 subbands)
LDH5 (2-4 subbands).
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 enzymatic 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 isozymes LDH1 and LDH2
whose principal subunits are H subunits
and the RPEA of LDH
(H4)
LDH2(H3M) increased
while RPEA of LDH5(M4) in various tissues decreased prominently except the cardiac muscle
and that of LDH4(HM3) decreased as well. After polyacrylamide gel electrophoresis (PAGE) of the hypoxia treated cardiac muscle specimen was made
activity subbands originated regularly in the isozyme patterns of LDH
with the regularity of LDH1 (0 subband)
LDH2 (0-1 subbands)
LDH3 (0-2 subbands)
LDH4 (1-3 subbands)
LDH5 (2-4 subbands). After adding appropriate amount of NAD+ to the hypoxia treated cardiac muscle specimen
PAGE showed the subbands of four isozymes (LDH2-LDH5) reduced or even totally disappeared in the isozyme patterns.Conclusions. The negative feedback regulation of coenzymization and decoenzymization of LDH isozymes is one of the mouse stress responses to slight hypoxia.
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