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H Gutfreund

Showing results (41-50 of 49) with videos related to

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Proceedings of the National Academy of Sciences of the United States of America|January 15, 1991
Substrate channeling in glycolysis: a phantom phenomenonX M Wu, H Gutfreund, S Lakatos, et al.
Biochemistry|April 6, 1976
31P nuclear magnetic resonance study of alkaline phosphatase: the role of inorganic phosphate in limiting the enzyme turnover rate at alkaline pHW E Hull, S E Halford, H Gutfreund, et al.
FEBS Letters|December 1, 1977
Pressure relaxation studies of isomerisations of horse liver alcohol dehydrogenase linked to NAD+ bindingJ H Coates, M J Hardman, J D Shore, et al.
Biochemistry|September 24, 1974
Proton equilibria and kinetics in the liver alcohol dehydrogenase reaction mechanismJ D Shore, H Gutfreund, R L Brooks, et al.
The Biochemical Journal|December 15, 1989
A transient-kinetic study of the nitrogenase of Klebsiella pneumoniae by stopped-flow calorimetry. Comparison with the myosin ATPaseR N Thorneley, G Ashby, J V Howarth, et al.
FEBS Letters|January 1, 1977
The putative isomerization of the lactate dehydrogenase--NADH complexJ J Holbrook, M J Hardman, D M Parker, et al.
The Biochemical Journal|June 1, 1974
The identification of intermediates in the reaction of pig heart lactate dehydrogenase with its substratesJ R Whitaker, D W Yates, N G Bennett, et al.
Cellular and Molecular Life Sciences : CMLS|September 5, 2006
The identification of chemical intermediates in enzyme catalysis by the rapid quench-flow techniqueT E Barman, S R W Bellamy, H Gutfreund, et al.
The Biochemical Journal|August 1, 1974
The magnesium ion-dependent adenosine triphosphatase of myosin. Two-step processes of adenosine triphosphate association and adenosine diphosphate dissociationC R Bagshaw, J F Eccleston, F Eckstein, et al.
Pageof 5

Showing results (41-50 of 49) with videos related to

Sort By:
Pageof 5
You have reached the last page of results.This site can display upto 49 results.
Proceedings of the National Academy of Sciences of the United States of America|January 15, 1991
Substrate channeling in glycolysis: a phantom phenomenonX M Wu, H Gutfreund, S Lakatos, et al.
Biochemistry|April 6, 1976
31P nuclear magnetic resonance study of alkaline phosphatase: the role of inorganic phosphate in limiting the enzyme turnover rate at alkaline pHW E Hull, S E Halford, H Gutfreund, et al.
FEBS Letters|December 1, 1977
Pressure relaxation studies of isomerisations of horse liver alcohol dehydrogenase linked to NAD+ bindingJ H Coates, M J Hardman, J D Shore, et al.
Biochemistry|September 24, 1974
Proton equilibria and kinetics in the liver alcohol dehydrogenase reaction mechanismJ D Shore, H Gutfreund, R L Brooks, et al.
The Biochemical Journal|December 15, 1989
A transient-kinetic study of the nitrogenase of Klebsiella pneumoniae by stopped-flow calorimetry. Comparison with the myosin ATPaseR N Thorneley, G Ashby, J V Howarth, et al.
FEBS Letters|January 1, 1977
The putative isomerization of the lactate dehydrogenase--NADH complexJ J Holbrook, M J Hardman, D M Parker, et al.
The Biochemical Journal|June 1, 1974
The identification of intermediates in the reaction of pig heart lactate dehydrogenase with its substratesJ R Whitaker, D W Yates, N G Bennett, et al.
Cellular and Molecular Life Sciences : CMLS|September 5, 2006
The identification of chemical intermediates in enzyme catalysis by the rapid quench-flow techniqueT E Barman, S R W Bellamy, H Gutfreund, et al.
The Biochemical Journal|August 1, 1974
The magnesium ion-dependent adenosine triphosphatase of myosin. Two-step processes of adenosine triphosphate association and adenosine diphosphate dissociationC R Bagshaw, J F Eccleston, F Eckstein, et al.
Pageof 5