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B V Plapp

Showing results (1-10 of 77) with videos related to

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Methods in Enzymology|January 1, 1995
Site-directed mutagenesis: a tool for studying enzyme catalysisB V Plapp
Advances in Experimental Medicine and Biology|January 1, 1975
Rate-limiting steps in ethanol metabolism and approaches to changing these rates biochemicallyB V Plapp
The Journal of Biological Chemistry|July 25, 1973
Mechanisms of carboxymethylation of bovine pancreatic nucleases by haloacetates and tosylglycolateB V Plapp
EXS|January 1, 1994
Control of alcohol metabolismB V Plapp
The Journal of Biological Chemistry|April 10, 1970
Enhancement of the activity of horse liver alcohol dehydrogenase by modification of amino groups at the active sitesB V Plapp
Archives of Biochemistry and Biophysics|May 1, 1973
On calculation of rate and dissociation constants from kinetic constants for the Ordered Bi Bi mechanism of liver alcohol dehydrogenaseB V Plapp
Methods in Enzymology|January 1, 1982
Application of affinity labeling for studying structure and function of enzymesB V Plapp
Biochemistry|April 29, 1998
Specificity of alcohol dehydrogenases for sulfoxidesH Cho, B V Plapp
Biochemistry|April 11, 1995
Substitutions of isoleucine residues at the adenine binding site activate horse liver alcohol dehydrogenaseF Fan, B V Plapp
Biochemistry|August 2, 1983
Involvement of histidine residues in the activity of horse liver alcohol dehydrogenaseM Hennecke, B V Plapp
Pageof 8

Showing results (1-10 of 77) with videos related to

Sort By:
Pageof 8
Methods in Enzymology|January 1, 1995
Site-directed mutagenesis: a tool for studying enzyme catalysisB V Plapp
Advances in Experimental Medicine and Biology|January 1, 1975
Rate-limiting steps in ethanol metabolism and approaches to changing these rates biochemicallyB V Plapp
The Journal of Biological Chemistry|July 25, 1973
Mechanisms of carboxymethylation of bovine pancreatic nucleases by haloacetates and tosylglycolateB V Plapp
EXS|January 1, 1994
Control of alcohol metabolismB V Plapp
The Journal of Biological Chemistry|April 10, 1970
Enhancement of the activity of horse liver alcohol dehydrogenase by modification of amino groups at the active sitesB V Plapp
Archives of Biochemistry and Biophysics|May 1, 1973
On calculation of rate and dissociation constants from kinetic constants for the Ordered Bi Bi mechanism of liver alcohol dehydrogenaseB V Plapp
Methods in Enzymology|January 1, 1982
Application of affinity labeling for studying structure and function of enzymesB V Plapp
Biochemistry|April 29, 1998
Specificity of alcohol dehydrogenases for sulfoxidesH Cho, B V Plapp
Biochemistry|April 11, 1995
Substitutions of isoleucine residues at the adenine binding site activate horse liver alcohol dehydrogenaseF Fan, B V Plapp
Biochemistry|August 2, 1983
Involvement of histidine residues in the activity of horse liver alcohol dehydrogenaseM Hennecke, B V Plapp
Pageof 8