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D Boyer

Showing results (51-60 of 390) with videos related to

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Seminars in Liver Disease|January 1, 1997
Hepatic hydrothoraxR M Strauss, T D Boyer
Biochemistry|January 28, 1975
The rapid labeling of adenosine triphosphate by 32P-labeled inorganic phosphate and the exchange of phosphate oxygens as related to conformational coupling in oxidative phosphorylationR L Cross, P D Boyer
Biochimica Et Biophysica Acta|October 24, 1990
The ADP that binds tightly to nucleotide-depleted mitochondrial F1-ATPase and inhibits catalysis is bound at a catalytic siteY M Milgrom, P D Boyer
The Journal of Biological Chemistry|October 25, 1985
The role of tightly bound ADP on chloroplast ATPaseR I Feldman, P D Boyer
Biochemistry|December 12, 1978
Effect of actin concentration on the intermediate oxygen exchange of myosin; relation to the refractory state and the mechanism of exchangeJ A Sleep, P D Boyer
Biochemical Genetics|October 1, 1982
Soluble starch synthases and starch branching enzymes from cotyledons of smooth- and wrinkled-seeded lines of Pisum sativum LG L Matters, C D Boyer
The Journal of Biological Chemistry|September 25, 1983
Probes of catalytic site cooperativity during catalysis by the chloroplast adenosine triphosphate and the adenosine triphosphate synthaseW E Kohlbrenner, P D Boyer
The Journal of Biological Chemistry|June 3, 1994
Interaction of mitochondrial F1-ATPase with trinitrophenyl derivatives of ATP and ADP. Participation of third catalytic site and role of Mg2+ in enzyme inactivationM B Murataliev, P D Boyer
Biochemistry|March 10, 1987
Catalytic and regulatory effects of light intensity on chloroplast ATP synthaseS D Stroop, P D Boyer
Proceedings of the National Academy of Sciences of the United States of America|November 1, 1989
Vacuolar ATPases, like F1,F0-ATPases, show a strong dependence of the reaction velocity on the binding of more than one ATP per enzymeV N Kasho, P D Boyer
Pageof 39

Showing results (51-60 of 390) with videos related to

Sort By:
Pageof 39
Seminars in Liver Disease|January 1, 1997
Hepatic hydrothoraxR M Strauss, T D Boyer
Biochemistry|January 28, 1975
The rapid labeling of adenosine triphosphate by 32P-labeled inorganic phosphate and the exchange of phosphate oxygens as related to conformational coupling in oxidative phosphorylationR L Cross, P D Boyer
Biochimica Et Biophysica Acta|October 24, 1990
The ADP that binds tightly to nucleotide-depleted mitochondrial F1-ATPase and inhibits catalysis is bound at a catalytic siteY M Milgrom, P D Boyer
The Journal of Biological Chemistry|October 25, 1985
The role of tightly bound ADP on chloroplast ATPaseR I Feldman, P D Boyer
Biochemistry|December 12, 1978
Effect of actin concentration on the intermediate oxygen exchange of myosin; relation to the refractory state and the mechanism of exchangeJ A Sleep, P D Boyer
Biochemical Genetics|October 1, 1982
Soluble starch synthases and starch branching enzymes from cotyledons of smooth- and wrinkled-seeded lines of Pisum sativum LG L Matters, C D Boyer
The Journal of Biological Chemistry|September 25, 1983
Probes of catalytic site cooperativity during catalysis by the chloroplast adenosine triphosphate and the adenosine triphosphate synthaseW E Kohlbrenner, P D Boyer
The Journal of Biological Chemistry|June 3, 1994
Interaction of mitochondrial F1-ATPase with trinitrophenyl derivatives of ATP and ADP. Participation of third catalytic site and role of Mg2+ in enzyme inactivationM B Murataliev, P D Boyer
Biochemistry|March 10, 1987
Catalytic and regulatory effects of light intensity on chloroplast ATP synthaseS D Stroop, P D Boyer
Proceedings of the National Academy of Sciences of the United States of America|November 1, 1989
Vacuolar ATPases, like F1,F0-ATPases, show a strong dependence of the reaction velocity on the binding of more than one ATP per enzymeV N Kasho, P D Boyer
Pageof 39