PMID: 71Nov 20, 1975

Calcium-stimulated adenosine triphosphatase in the microsomal fraction of tooth germ from porcine fetus

Biochimica Et Biophysica Acta
F Yoshimura, T Suzuki

Abstract

The characterization and localization of a Ca(2+)-ATPase (ATP phosphohydrolase, EC 3.6.1.3) in the tooth germ of the porcine fetus are reported. This enzyme, a microsome fraction, is preferentially activated by Ca(2+). In the presence of 0.5 mM ATP, maximal enzyme activity is obtained at 0.5--1.0 mM CaCl2. The maximal rate of ATP hydrolysis is approx. 20 mumol per h per mg of protein as the enzyme preparation is used here. At optimal Ca(2+) concentration, the Mg(2+) has an inhibitory effect. The enzyme does not require Na+ or/and K+ for activation by Ca(2+). Other nucleotide triphosphates may serve as the substrate, but V for ATP is the highest. The Km for ATP is 8.85 - 10(-5) M. The optimal pH for Ca(2+) activation of the enzyme lies around 9.2. Well known inhibitors of (Na+ + K+)-ATPase, mitochondria ATPase and Ca(2+)-ATPase in the erthrocyte do not inhibit the enzyme. In the subcellular order the enzyme may be assumed to be localized in the smooth endoplasmic reticulum fraction containing cell and Golgi body membrane fragments and in the tissue order in the enamel organ containing an ameloblast layer, stratum intermedium and stellate reticulum.

References

Dec 1, 1964·Proceedings of the National Academy of Sciences of the United States of America·T W CONWAY, F LIPMANN

Citations

Jan 1, 1983·The International Journal of Biochemistry·M HayakawaH Takiguchi
Aug 1, 1978·Archives of Biochemistry and Biophysics·F Yoshimura
Jan 27, 2010·International Reviews of Immunology·Fang Zhou
Jan 1, 1978·Scandinavian Journal of Dental Research·H Mörnstad
Dec 1, 1987·Advances in Dental Research·T SasakiP R Garant

Related Concepts

DNA-dependent ATPase
Metazoa
Calcium
Cations, Divalent
Edetic Acid, Calcium, Sodium Salt
Enzyme Activation
Fetal Structures
Hydrogen-Ion Concentration
Magnesium
Microsomes

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