We will continue studies of the role of ferroactivator in controlling gluconeogenesis and initiate studies aimed at controlling the function of this protein. We will continue to investigate (a) the mechanism by which glucagon and epinephrine enhance gluconeogenesis, and (b) the biochemical defects that cause diabetes. Having established that the metabolic defect responsible for malignant hyperpyrexia is located in the muscle itself, we will isolate phosphofructokinase and hexosediphosphatase from normal pig muscle and from muscle of animals genetically susceptible to this disease. The control of these two enzymes from each type of muscle will be examined. A prime goal in the area of oxidative phosphorylation is to define its chemical mechanism. While this may not be achieved in any one laboratory, we hope to contribute to the ultimate solution of this problem. We will continue to study the mechanism by which caffeine activates sperm motility and will investigate the mechanism by which a seminal protein blocks calcium transport in bovine spermatozoa and hope to establish the role of this phenomenon in decapacitation and fertilization. BIBLIOGRAPHIC REFERENCES: "Ionophore A23187: The Effect of H ion Concentration on Complex Formation with Divalent and Monovalent Cations and the Demonstration of K ion Transport in Mitochondria Mediated by A23187." by Douglas R. Pfeiffer and Henry A. Lardy, Biochemistry, 15, 935-943 (1976). "Essential Arginyl Residues in Mitochondrial Adenosine Triphosphatase." by Frank Marcus, Sheldon M. Schuster, and Henry A. Lardy, J. Biol. Chem., 251, 1775-1780 (1976).