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KMID : 0364219740170020093
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Korean Journal of Zoology
1974 Volume.17 No. 2 p.93 ~ p.102
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Studies on the ATPases of Fragmented Sarcoplasmic Reticulum of Rabbit Skeletal Muscle
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Ha Doo-Bong
Song Eun-Sook
Park Hee-Soon
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Abstract
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Fragmente dsarcoplasmic reticulum of rabbit skeletal muscle was prepared and biochemical properties of its ATPase activity were studied. The ATPase of the fragments could be distinguished as $Mg^++ - ATPase and (Mg^++ - Ca^++)$-ATPase. The activity of $(Mg^++ - Ca^++)$-ATPase was predominant over that of $Mg^++$-ATPase in the temperature range of $0 \\sim 40^\\circ C$ and in the pH 6.4$\\sim$7.6. At higher temperatures the predominance of $(Mg^++ - Ca^++)$-ATpase was far greater. The apparent energies of activation were 14 kcal/mole for $Mg^++$-ATPase, 21kcal/mole for $(Mg^++ - Ca^++)$-ATPase, and 18kcal/mole for total ATPase. Changes in pH and Mg concentration did not alter the energies of activation of these ATPases. The Km values of these ATPases were found to be 0.36 mM for $Mg^++$-ATPase, 2.20 mM for $(Mg^++ - Ca^++)$-ATpase, and 0.86 mM for total ATPase.
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