Immunological properties of antibodies against Mg(2+)-ATPase from Acholeplasma laidlawii membranes.
In the present study, antibodies were raised against the Mg(2+)-ATPase and the immunological relationships between the enzyme and other ATPase from a variety of biological membranes were determined. The anti Mg(2+)-ATPase antiserum inhibited 85% of the enzyme activity from A. laidlawii membranes. We demonstrate a specific selectivity of Mg(2+)-ATPase antiserum for antigenic determinants of the A. laidlawii membranes. Immunoblot studies of A. laidlawii membrane peptides indicated labeling of five bands, 66KD, 49KD, 34KD, 26KD and 13KD, corresponding to five subunits of the ATPase in A. laidlawii membranes.
Chen
J W
JW
Department of Biomembranes, Institute of Biophysics, Academia Sinica, Beijing, China.
Zhang
L P
LP
Hwang
F
F
D000128:Acholeplasma laidlawii / Q000201:enzymology* / Q000276:immunology; D000907:Antibodies, Bacterial / Q000276:immunology*; D000918:Antibody Specificity; D017301:Ca(2+) Mg(2+)-ATPase / Q000737:chemistry / Q000276:immunology* / Q000378:metabolism; D003429:Cross Reactions; D004797:Enzyme-Linked Immunosorbent Assay; D000939:Epitopes; D015151:Immunoblotting; D046911:Macromolecular Substances; D012680:Sensitivity and Specificity
D000907:Antibodies, Bacterial; D000939:Epitopes; D046911:Macromolecular Substances; D017301:Ca(2+) Mg(2+)-ATPase