Evidence for identity between the hexokinase-binding protein and the mitochondrial porin in the outer membrane of rat liver mitochondria.
Hexokinase-binding protein and mitochondrial porin were isolated from rat liver mitochondria by different procedures. It was found that the hexokinase-binding protein made lipid vesicles permeable to ADP and formed asymmetric pores in lipid bilayer membranes identical to those obtained from the mitochondrial porin. On the other hand, the mitochondrial porin confers the ability to bind hexokinase. In addition, evidence is presented that both hexokinase-binding protein and mitochondrial porin bind glycerol kinase.
D000818:Animals; D006593:Hexokinase / Q000378:metabolism; D007425:Intracellular Membranes / Q000378:metabolism*; D007473:Ion Channels / Q000378:metabolism*; D008051:Lipid Bilayers; D008565:Membrane Proteins / Q000302:isolation & purification* / Q000378:metabolism; D008930:Mitochondria, Liver / Q000378:metabolism*; D008970:Molecular Weight; D010539:Permeability; D018272:Porins; D051381:Rats
D007473:Ion Channels; D008051:Lipid Bilayers; D008565:Membrane Proteins; D018272:Porins; D006593:Hexokinase