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 (α and β) isolated fromM. lysodeikticus F1-ATPase form A, which was the most stable form of the enzyme. Anti-(α-subunit) serum strongly inhibited the ATPase activity of membrane-bound ATPase but showed little inhibition of the purified, soluble F1-ATPase. The anti-(β-subunit) serum inhibited the soluble F1-ATPase, but to a lesser extent than the membrane-bound enzyme. In any event, the effect of anti-β antibodies on the membrane-bound ATPase was smaller than that of anti-α antibodies. It was postulated that the α 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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Larraga, V., Mollinedo, F. & Muñoz, E. Immunochemistry of membrane F1-Adenosine triphosphatase fromMicrococcus lysodeikticus. Role of the alpha subunit. Current Microbiology 5, 363–366 (1981). https://doi.org/10.1007/BF01566750
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DOI: https://doi.org/10.1007/BF01566750