Open AccessInteraction between the soluble F 1 ATPase and its naturally occurring inhibitor protein
Author(s) -
HARRIS David A.,
HUSAIN Iqbal,
JACKSON Philip J.,
LÖNSDORF Heinrich,
SCHÄFER Günter,
TIEDGE Henri
Publication year - 1986
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1986.tb09654.x
Subject(s) - gel permeation chromatography , immunoelectron microscopy , size exclusion chromatography , chemistry , inhibitor protein , atpase , binding site , antibody , biochemistry , biology , enzyme , organic chemistry , immunology , polymer
Binding of the isolated ATPase (F 1 ) to its naturally occurring inhibitor protein was studied by two novel, independent techniques. High‐pressure gel permeation chromatography revealed one tight binding site ( K d = 0.46 μM) for the inhibitor on F 1 , and a number of weak, non‐specific sites. Use of an antibody directed against a non‐binding region of the inhibitor protein demonstrated the formation of inhibitor/F 1 /immunoglobulin G complexes of 1:1:1 and 2:2:1 stoichiometry, but not of the putatively more stable cyclic 4:2:2 complexes. It was concluded that, despite the presence of three β‐subunits, only one site per F 1 molecule is available for binding its inhibitor protein.