COMPARISON OF MUSCLE-FIBER TYPING BY QUANTITATIVE ENZYME ASSAYS AND BY MYOSIN ATPASE STAINING
COMPARISON OF MUSCLE-FIBER TYPING BY QUANTITATIVE ENZYME ASSAYS AND BY MYOSIN ATPASE STAINING
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DOI:
10.1177/32.6.6202737
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发表时间:
1984-01-01
影响因子:
3.2
通讯作者:
LOWRY, OH
中科院分区:
文献类型:
--
作者:
HINTZ, CS;COYLE, EF;LOWRY, OH
Fibers in cross sections of human and rat muscle were typed by using histochemical ATPase stains, and the results were compared with those of quantitative enzyme assays of fragments of the same fibers dissected from serial freeze-dried sections. Two enzymes previously used to assess the metabolic type were measured in each case: lactate dehydrogenase and either adenylokinase (human fibers) or malate dehydrogenase (rat fibers). With human fibers there was essentially complete agreement between ATPase staining and the metabolic enzyme assays in distinguishing types I and II fibers. The agreement was less consistent with regard to type IIA and IIB fibers. A number of ATPase type IIC fibers were identified in 1 human muscle, and were found to fall between ATPase types I and IIA on the basis of metabolic enzyme assay results. Rat-fiber ATPase types I, IIA and IIB from the plantaris muscle were rather well segregated on a 2-dimensional lactate dehydrogenase-malate dehydrogense grid. In the rat soleus muscle, ATPase types I and IIA fibers were shifted to lower lactate dehydrogenase levels, with IIC fibers interposed between them.