Summary
The HCO −3 -stimulated Mg2+-ATPase activity in red cell ghost fragments was investigated. Increasing the HCO −3 concentration in the incubation medium resulted in increased ATPase activity. NaHCO3 appeared to be more effective than KHCO3 in this regard. The ATPase activities were slightly stimulated by increases in ionic strength and utilized ITP almost as readily as ATP. A Mg/ATP ratio of 1.0 and a pH of 7.6 yielded maximum activity. These properties are of interest since the present enzyme is the only unquestionable instance where a HCO −3 -ATPase is located in the surface membrane of a cell.
Similar content being viewed by others
References
Blum, A. L., Shah, G., St. Pierre, T., Helander, H. F., Sung, C. P., Wiebelhaus, V. D., Sachs, G.: Properties of soluble ATPase of gastric mucosa. II. Effect of HCO −3 . Biochim. biophys. Acta (Amst.)249, 101–113 (1971)
Davson, H.: In: A textbook of general physiology, p. 550. Baltimore: The Williams and Wilkins Co. 1970
de Pont, J. J. H. H. M., Hansen, T., Bonting, S. L.: An anionsensitive ATPase in lizard gastric mucosa. Biochim. biophys. Acta (Amst.)274, 189–200 (1972)
Duncan, C. J.: ATPases in rabbit erythrocytes: Stimulation by HCO −3 and Na+-plus-K+. Life Sci.16, 955–966 (1975)
Hegner, D., Anika, S.: The occurrence and some properties of HCO −3 -stimulated ATPase and aminopeptidases in the rumen forestomach epithelium of BOS Prinigenius Taurus. Comp. Biochem. Physiol.50B, 339–343 (1975)
Izutsu, K. T., Siegel, I. A.: A microsomal HCO −3 -stimulated ATPase from the dog submandibular gland. Biochim. biophys. Acta (Amst.)284, 478–484 (1972)
Izutsu, K. T., Siegel, I. A.: Bicarbonate ion-ATPase in rat liver cell fractions. Biochim. biophys. Acta (Amst.)382, 193–203 (1975)
Izutsu, K. T., Siegel, I. A., Brisson, D. L.: The effect of ionic strength on a Mg2+-ATPase and its relevance to the determination of (Na++K+)-ATPase. Biochim. biophys. Acta (Amst.)373, 361–368 (1974)
Kasbekar, D. K., Durbin, R. P.: An adenosine triphosphatase from frog gastric mucosa. Biochim. biophys. Acta (Amst.)105, 472–482 (1965)
Katz, A. I., Epstein, F. H.: Effect of anions on adenosine triphosphatase of kidney tissue. Enzyme12, 499–507 (1971)
Kinne-Saffran, E., Kinne, R.: Presence of bicarbonate-stimulated ATPase in the brush border microvillus membranes of the proximal tubules. Proc. Soc. exp. Biol. (N. Y.)146, 751–753 (1974)
Quist, E. E., Roufagalis, B. D.: Determination of the stoichiometry of the calcium pump in human erythrocytes using lanthanum as a selective inhibitor. FEBS Letters50, 135–139 (1975)
Sachs, G., Mitch, W. E., Hirschowitz, B. I.: Frog gastric mucosal ATPase. Proc. Soc. exp. Biol. (N. Y.)119, 1023–1027 (1965)
Sigma Price List, p. 216. St. Louis: The Sigma Chemical Co. 1974
Simon, B., Kinne, R., Sachs, G.: The presence of a HCO −3 -ATPase in pancreatic tissue. Biochim. biophys. Acta (Amst.)282, 293–300 (1972)
Simon, B., Thomas, L.: HCO −3 -stimulated ATPase from mammalian pancreas. Properties and its arrangements with other enzyme activities. Biochim. biophys. Acta (Amst.)288, 434–442 (1972)
Wiebelhaus, V. D., Sung, C. P., Helander, H. F., Shah, G., Blum, A. L., Sachs, G.: Solubilization of anion ATPase from necturus oxyntic cells. Biochim. biophys. Acta (Amst.)241 49–56 (1971)
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Izutsu, K.T., Madden, P.R., Watson, E.L. et al. Properties of the HCO −3 -stimulated Mg2+-ATPase activity in red cell membranes. Pflügers Arch. 369, 119–124 (1977). https://doi.org/10.1007/BF00591567
Received:
Issue Date:
DOI: https://doi.org/10.1007/BF00591567