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B V Plapp

Showing results (21-30 of 77) with videos related to

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The Journal of Biological Chemistry|April 15, 1988
Carboxyl groups near the active site zinc contribute to catalysis in yeast alcohol dehydrogenaseA J Ganzhorn, B V Plapp
Biochemistry|June 14, 1977
pH, isotope, and substituent effects on the interconversion of aromatic substrates catalyzed by hydroxybutyrimidylated liver alcohol dehydrogenaseR T Dworschack, B V Plapp
Advances in Experimental Medicine and Biology|January 1, 1980
Kinetics and control of alcohol oxidation in ratsW S Chen, B V Plapp
Biochemistry|September 24, 1999
Control of coenzyme binding to horse liver alcohol dehydrogenaseL A LeBrun, B V Plapp
Biochemistry|September 4, 1979
Transition-state analysis of the facilitated alkylation of ribonuclease A by bromoacetateE P Lennette, B V Plapp
Biochemistry|January 17, 1984
Inactivation of horse liver alcohol dehydrogenase by modification of cysteine residue 174 with 3-bromopropionic acidV K Chadha, B V Plapp
Biochemistry|March 9, 1976
Inactivation of horse liver alcohol dehydrogenase by modification of cysteine residue 174 with diazonium-1H-tetrazoleD C Sogin, B V Plapp
The Journal of Biological Chemistry|January 10, 1975
Activation and inactivation of horse liver alcohol dehydrogenase with pyridoxal compoundsD C Sogin, B V Plapp
The Journal of Biological Chemistry|March 15, 1992
Interconversion of E and S isoenzymes of horse liver alcohol dehydrogenase. Several residues contribute indirectly to catalysisD H Park, B V Plapp
Journal of Molecular Evolution|June 1, 1992
Progressive sequence alignment and molecular evolution of the Zn-containing alcohol dehydrogenase familyH W Sun, B V Plapp
Pageof 8

Showing results (21-30 of 77) with videos related to

Sort By:
Pageof 8
The Journal of Biological Chemistry|April 15, 1988
Carboxyl groups near the active site zinc contribute to catalysis in yeast alcohol dehydrogenaseA J Ganzhorn, B V Plapp
Biochemistry|June 14, 1977
pH, isotope, and substituent effects on the interconversion of aromatic substrates catalyzed by hydroxybutyrimidylated liver alcohol dehydrogenaseR T Dworschack, B V Plapp
Advances in Experimental Medicine and Biology|January 1, 1980
Kinetics and control of alcohol oxidation in ratsW S Chen, B V Plapp
Biochemistry|September 24, 1999
Control of coenzyme binding to horse liver alcohol dehydrogenaseL A LeBrun, B V Plapp
Biochemistry|September 4, 1979
Transition-state analysis of the facilitated alkylation of ribonuclease A by bromoacetateE P Lennette, B V Plapp
Biochemistry|January 17, 1984
Inactivation of horse liver alcohol dehydrogenase by modification of cysteine residue 174 with 3-bromopropionic acidV K Chadha, B V Plapp
Biochemistry|March 9, 1976
Inactivation of horse liver alcohol dehydrogenase by modification of cysteine residue 174 with diazonium-1H-tetrazoleD C Sogin, B V Plapp
The Journal of Biological Chemistry|January 10, 1975
Activation and inactivation of horse liver alcohol dehydrogenase with pyridoxal compoundsD C Sogin, B V Plapp
The Journal of Biological Chemistry|March 15, 1992
Interconversion of E and S isoenzymes of horse liver alcohol dehydrogenase. Several residues contribute indirectly to catalysisD H Park, B V Plapp
Journal of Molecular Evolution|June 1, 1992
Progressive sequence alignment and molecular evolution of the Zn-containing alcohol dehydrogenase familyH W Sun, B V Plapp
Pageof 8