Immunochemistry of membrane F1-Adenosine triphosphatase fromMicrococcus lysodeikticus. Role of the alpha subunit |
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Authors: | Vicente Larraga Faustino Mollinedo Emilio Muñoz |
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Institution: | (1) Unidad de Biomembranas, Instituto de Inmunología y Biología Microbiana, C.S.I.C., Velazquez, 144 Madrid-6, Spain |
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Abstract: | The membrane-bound ATPase activity from two substrains ofMicrococcus lysodeikticus, designated as A and B, was inhibited by antibodies raised against the two forms of purified F1-ATPase. Form B of the enzyme, which behaved as a poorer immunogen than form A, also showed less reactivity as an antigen, independent of the physical state of the F1-ATPase form. Antibodies were raised against the two major subunits ( and ) isolated fromM. lysodeikticus F1-ATPase form A, which was the most stable form of the enzyme. Anti-( -subunit) serum strongly inhibited the ATPase activity of membrane-bound ATPase but showed little inhibition of the purified, soluble F1-ATPase. The anti-( -subunit) serum inhibited the soluble F1-ATPase, but to a lesser extent than the membrane-bound enzyme. In any event, the effect of anti- antibodies on the membrane-bound ATPase was smaller than that of anti- antibodies. It was postulated that the subunit ofM. lysodeikticus F1-ATPase plays an essential and regulatory role in the expression of the immunochemical properties of the protein. |
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