Histochemical Analysis of the Skeletal Muscle Fibers in Five Species of Japanese Reptiles (Mauremys japonica, Gekko japonicus, Elaphe quadrivirgata, Elaphe climacophora, Rhabdophis tigrinus). Noboru MANABE, Eimei SATO, Kazuko MARUYAMA* and Takehiko ISHIBASHI The fiber type profiles of the skeletal muscles (Musclus masseter, M. rectus capitis major, M. rectus capitis minor, M. complexus, M. trapezius, M, pectoralis major, M. triceps brachii, M. externus carpi radialis, M. rectus femoris, M. semimembranosus, M. gastrocnemius in Mauremys japonica, M. masseter, M. trapezius, M. latissimus dorsi, M. triceps brachii, M. extensor carpi radialis, M. obliquus extensor abdominis, M. obliquus internus abdominis, M. rectus femoris, M. semimembranosus, M. gastrocnemius in Gekko japonicus, and M. linguae, M. masseter, M. epaxialis, M. hypaxialis, in Elaphe quadrivirgata, Elaphe climacophora, Rhabdophis tigrinus) were examined histochemically. According to the enzymatic reactions, muscle fibers were divided into 3 main types; i. e., slow-twitch-oxidative (SO), fast-twitchoxidative-glycolytic(fog) and fast-twitch-glycolytic(fg) types. Moreover according to the intensities of various enzyme reactions, the 3 main types were subdivided into 11 subtypes in all, 3-5 types fibers were identified in the muscle of Mauremys japonioa, 4-6 types in Gekko japonicus, and 3 types in Elaphe quadrivirgata, Elaphe climacophora and Rhabdophis tigrinus. The ratio of the number of FG type fibers was higher than the other types fibers in Mauremys japonica and Gekko japonicus, but the ratio of FG type fibers was not higher in Elaphe quadrivirgata, Elaphe climacophora and Rhabdophis tigrinus. The diameter of muscle fibers was largest in FG type and smallest in SO type fibers. The ph stability of myosin adenosine triphosphatase (myosin ATPase) activity varied with the types of muscles, namely the range of ph stability at an acidic ph range in SO and FOG type fibers was more extensive than in FG type of fibers and at an alkaline ph range FG and FOG types fibers were more extensive than SO type fibers in the range of ph stability. Department of Animal Science, Faculty of Agriculture, Kyoto University, Kitashirakawa, Sakyoku, Kyoto 606. Department of Zoology, Faculty of Science, Kyoto University, Kitashirakawa, Sakyoku, Kyoto 606.
Vol. 9, No. 2, 1981 Table 1. Comparison of fiber type characteristics with histochemical reactions of skeletal muscles.
"F able 2. Percentage of number of histochemical fiber types in reptile skeletal muscles.
Vol. 9, No. 2, 1981 Table 3a. Fiber size and percentage of fiber size distributions of main histochemical fiber types in reptile skeletal muscles. (Values are means of percentage.)
Vol. 9, No. 2, 1981 39 Table 3b. Fiber size and percentage of fiber size distributions of main histochemical fiber types in reptile skeletal muscles. (Values are means of percentage.)
Fig. 1. The ph stability of myosin ATPase reaction in reptile skeletal muscle fibers. Intensity of histochemical reactions: white rectangle slight, dotted moderate, striped strong, dark very strong. The branches at both ends of the bars show the variations of intensity of reactions.
Photos 1-6. Serial transverse sections of M. hypaxialis in Elaphe quadrivirgata. Myosin ATPase activities preincubated at ph 10.2 (Photo 1), 10.4 (Photo 2), 10.6 (Photo 3), 10.8 (Photo 4), 11.0 (Photo 5) and 11.2 (Photo 6). It is shown that the ph stability of myosin ATPase activity varies according to muscular fibers. Photos 7 and 8. Serial transverse sections of M. linguae in Elaphe climacophora. Myosin ATPase activity preincubated at ph 10.4 (Photo 7) and glycogen phosphorylase activity (Photo 8). It is shown that the muscular fibers can he classified as SO type with FOG type.
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