翼手類の飛翔適応からみた乳酸脱水素酵素アイソザイム

概要

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the enzyme lactate dehydrogenase (LDH) from skeletal muscles, cardiac muscle and liver of bats and mice was obtained by scrylamide gel electrophoresis. In the bats, the pectoralis muscles were selected as representative skeletal muscles; in the mice, the piceps femoris muscles were used. This choice was based upon the obvious similarity in function.Species examined were the japanese long-fingered bat (Miniopterus schreibersi fuliginosus), Japanese house bat (Pipistrellus abramus abramus), Japanese lesser horseshoe bat (Rhinolophus cornutus cornutus) and greater Japanese horseshoe bat (Rhinolophus ferrumequinum nippon). KDH_5 was absent from the pectoralis muscles of all specles examind, on the countrary, LHD_5 is a dominant isozyme in the biceps femoris muscles of the albino mice which represent the common mammalian type. Moreover, general LDH isozyme patterns in the pectoralis muscles exhibit differences among the four species, except for LDH_1 which takes the place of LDH_5 as the dominant isozyme in all species except for R. f. nippon. Differences of LDH percentage among the four species seem to indicate quantitatively the morphological and ecological differences. Thus the difference in the relative amount of each isozyme of LDH in the pectoralis muscles is considered to correspond to the degree of adaptation for flight in the bats investigated.
社団法人日本動物学会の論文
1974-03-25