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KMID : 0380919800090010059
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Journal of the Korean Society of Food Nutrition
1980 Volume.9 No. 1 p.59 ~ p.73
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Studies on Adenosine Triphosphate - Creatine Phosphotransferase from Muscle of the Snake Bungarus fasciatus
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박충웅/Park CU
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Abstract
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A detailed procedure was described for the isolation of cratine kinase (ATP-Creatine phosphotransferase, E. C. 2. 7. 3. 2.) from the muscle of the snake Bungarus fasciatus. The original isolation procedure of Kuby et al. for the rabbit muscle enzyme has been modified and extended to include a chromatographic step.
The properties of the enzyme have been investigated and kinetic constants for the reverse reactions determined as the followings:
1) A molecular weight of the enzyme was determined by gel filteration on Sephadex G-100 and by electrophoresis on SDS-polyacrylamide was 86,000.
2) Two reactive sulphydryl groups were detected with dithiobis nitrobenzoic acid (DTNB).
3) The nucleotide substrate specificity in the reverse reaction was determined as ADP*2’-dADP＞GDP＞XDP＞UDP with magnesium as the activating metal ion.
4) The order of the metal specificity in the reverse reaction Mg>Mn>Ca~Co was determined with ADP as substrate.
5) A detailed kinetic analysis was carried out in the reverse direction with MgADP￣ as the nucleotide substrate. Initial velocity and product inhibition studies(MgATP^(2-) competitive with respect to MgADP- and noncompetitive with respect to N-phosphorycreatine^(2-) ; Creatine competitive with respect to N-phosphorylcreatine^(2-) and noncompetitive with respect to Mg ADP￣) indicated that the reaction obeyed a sequential mechanism of the rapid equilibrium random type.
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KEYWORD
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