ATPase ACTIVITY IN THE MIDGUT OF THE MOSQUITO, ANOPHELES STEPHENSI: BIOCHEMICAL CHARACTERISATION OF OUABAIN-SENSITIVE AND OUABAIN-INSENSITIVE ACTIVITIES
作者： M. B. A. Djamgoz , P. F. Billingsley , J. A. K. Macvicker
关键词:
摘要: Na+/K(+)-ATPase activity was demonstrated in the midgut of Anopheles stephensi. More than 80% total ATPase sensitive to inhibition by ouabain with an IC50 4.5 x 10(-7) +/- 0.3 mol l-1 and maximal occurring at 10(-4) l-1. This ouabain-sensitive maximally activated a Mg2+:ATP ratio 1:1.3, Km mmol Vmax 2.4 mumol Pi mg-1 protein min-1 for ATP. Maximal activation reached 15 K+ 0.72 Activation Na+ showed increase up 120 6.47 l-1, optimal K+:Na+ 1:5.5. The enzyme inhibited Ca2+ 1.11 0.07 pH optima were 7.2 8.9 ouabain-insensitive fraction. minor fraction unaffected Na+, or Ca2+, but dependent some extent on Mg2+. demonstration being major mosquito is consistent hypothesis that this region actively involved post-feeding ion water regulation.
biologists.com
biologists.org
researchgate.net 参考文章(52)
R. M. Lebovitz, K. Takeyasu, D. M. Fambrough, Molecular characterization and expression of the (Na+ + K+)-ATPase alpha-subunit in Drosophila melanogaster. The EMBO Journal. ,vol. 8, pp. 193- 202 ,(1989) , 10.1002/J.1460-2075.1989.TB03364.X
Colin W. Taylor, Calcium Regulation in Insects Advances in Insect Physiology. ,vol. 19, pp. 155- 186 ,(1987) , 10.1016/S0065-2806(08)60101-0
Joseph D. Robinson, Kinetic Analyses and the Reaction Mechanism of the Na,K-ATPase Current Topics in Membranes and Transport. ,vol. 19, pp. 485- 512 ,(1983) , 10.1016/S0070-2161(08)60600-0
G E Shull, J B Lingrel, Molecular cloning of the rat stomach (H+ + K+)-ATPase. Journal of Biological Chemistry. ,vol. 261, pp. 16788- 16791 ,(1986) , 10.1016/S0021-9258(19)75957-2
P.A. Lucchesi, K.J. Sweadner, Postnatal changes in Na,K-ATPase isoform expression in rat cardiac ventricle. Conservation of biphasic ouabain affinity. Journal of Biological Chemistry. ,vol. 266, pp. 9327- 9331 ,(1991) , 10.1016/S0021-9258(18)31589-8
K J Sweadner, Two molecular forms of (Na+ + K+)-stimulated ATPase in brain. Separation, and difference in affinity for strophanthidin. Journal of Biological Chemistry. ,vol. 254, pp. 6060- 6067 ,(1979) , 10.1016/S0021-9258(18)50519-6
Brij L. Gupta, Betty J. Wall, T. A. Hall, James L. Oschman, Direct Microprobe Evidence of Local Concentration Gradients and Recycling of Electrolytes During Fluid Absorption in the Rectal Papillae of Calliphora The Journal of Experimental Biology. ,vol. 88, pp. 21- 48 ,(1980)
Elmer M. Price, Jerry B. Lingrel, Structure-function relationships in the sodium-potassium ATPase .alpha. subunit: site-directed mutagenesis of glutamine-111 to arginine and asparagine-122 to aspartic acid generates a ouabain-resistant enzyme Biochemistry. ,vol. 27, pp. 8400- 8408 ,(1988) , 10.1021/BI00422A016
R. E. Sinden, The biology of Plasmodium in the mosquito Cellular and Molecular Life Sciences. ,vol. 40, pp. 1330- 1343 ,(1984) , 10.1007/BF01951886
J.H. Tolman, J.E. Steele, A ouabain-sensitive, (Na+-K+)-activated ATPase in the rectal epithelium of the american cockroach, Periplaneta americana Insect Biochemistry. ,vol. 6, pp. 513- 517 ,(1976) , 10.1016/0020-1790(76)90077-9