Isolation, purification and kinetic characterization of plasma membrane H(+)-ATPase of Candida albicans

Gupta, P. ; Mahanty, S. K. ; Ansari, S. ; Prasad, R. (1991) Isolation, purification and kinetic characterization of plasma membrane H(+)-ATPase of Candida albicans Biochemistry International, 24 (5). pp. 907-915. ISSN 0158-5231

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Abstract

The plasma membrane ATPase of Candida albicans was solubilized by Tween 40 and purified to homogeneity on glycerol step gradient. The purified protein appeared as a single band of 100 +/- 4 KDa, represented greater than 98% of the total pure protein on densitometer scan. The purified PM-ATPase which was very specific to MgATP, had Km of about 0.77 mM and a sharp pH optimum at 6.6. Orthovanadate was able to inhibit the enzyme in a non-competitive manner, however, at higher concentrations the nature of inhibition changed to uncompetitive type. Based on molecular size, immuno cross-reactivity and sensitivity to different inhibitors, PM-ATPase of C. albicans appears to be similar to other ion pumps.

Item Type:Article
Source:Copyright of this article belongs to International Union of Biochemistry.
ID Code:66278
Deposited On:24 Oct 2011 08:31
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