One female, five juveniles and four pairs of egg sacs of a Hynobiid salamander of the Hynobius lichenatus complex from Hakuba Village, Nagano Pref. were taxonomically examined in comparison with H. lichenatus and H. abei. The salamanders from Hakuba lacked evident longitudinal striae on the surface of egg sac envelopes and greatly differed from H. lichenatus and H. abei in this structure, suggesting a different taxonomic status from the latter two species. Features of some other taxonomically important characteristics, together with geographic distribution, are discussed for these thtee forms.

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The fiber type profiles of 12 muscles (M. masseter, M. trapezius, M. latissimus dorsi, M. triceps brachii, M. extensor carpi radialis, M. longissimus dorsi, M. obliquus externus abdominis, M. rectus femoris anterior, M. semitendinosus, M. semimembranosus, M. gastrocnemius and M. tibialis anterior) in eight species of amphibians (Cynops pyrrhogaster, Hyla japonica, Rana nigromaculata, Rana brevipoda, Rana rugosa, Rana limnocharis, Rhacophorus buergeri, Rhacophorus arboreus) were examined histochemically. According to the enzymatic reactions (succinate dehydrogenase, glycogen phosphorylase and myosin adenosine triphosphatase), muscle fibers were divided into three types; i. e., slow-twitch-oxidative (SO), fast-twitch-oxidative-glycolytic (FOG) and fast-twitch-glycolytic (FG) types. Moreover, according to the reactions of α-glycerophosphate dehydrogenase, aldolase and β-hydroxybutylate dehydrogenase, each of the three main types was subdivided into three types. The number of FG type fibers was higher than the other types of fibers in all species. The diameter of muscle fiber was largest in FG type fibers and smallest in SO type fibers. The fibers of muscles in the hindlimb were larger than those in the forelimb and the diameters of fibers in Cynops pyrrhogaster and Hyla japonica were smaller than those of the other six species.

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Effects of different pH on myosin adenosine triphosphatase (myosin ATPase) activity in M. gastrocnemius in eight species of amphibians (Cynops pyrrhogaster, Hyla japonica, Rana nigromaculata, Rana brevipoda, Rana rugosa, Rana limnocharis, Rhacophorus buergeri, Rhacophorus arboreus) were estimated histochemically. The pH stability of myosin ATPase activity varies with the types of muscular fibers; namely, the range of pH stability at an acidic pH range in SO fibers was more extensive than in the other types of fibers. PH stability of myosin ATPase actixity in the same fiber type varied with species, but the pattern of the stability after various pH treatments coincided in Rana nigromaculata and Rana brevipoda, and in Rana rugosa and Rana limnocharis.

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