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M F Dunn

Showing results (61-70 of 106) with videos related to

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Biochemistry|February 19, 1980
Comparison of the zinc binding domains in the 7S nerve growth factor and the zinc-insulin hexamerM F Dunn, S E Pattison, M C Storm, et al.
The Journal of Biological Chemistry|May 25, 1977
Liver alcohol dehydrogenase-coenzyme reaction ratesM C DeTraglia, J Schmidt, M F Dunn, et al.
Biochemistry|January 6, 1970
Mechanistic studies on equine liver alcohol dehydrogenase. I. The stoichiometry relationship of the coenzyme binding sites to the catalytic sites active in the reduction of aromatic aldehydes in the transient stateS A Bernhard, M F Dunn, P L Luisi, et al.
Biochemistry|January 16, 1990
Reaction mechanism of Escherichia coli cystathionine gamma-synthase: direct evidence for a pyridoxamine derivative of vinylglyoxylate as a key intermediate in pyridoxal phosphate dependent gamma-elimination and gamma-replacement reactionsP Brzović, E L Holbrook, R C Greene, et al.
Biochemistry|June 20, 2001
Beta D305A mutant of tryptophan synthase shows strongly perturbed allosteric regulation and substrate specificityD Ferrari, L H Yang, E W Miles, et al.
Biochemistry|June 2, 1987
Characterization of a transient intermediate formed in the liver alcohol dehydrogenase catalyzed reduction of 3-hydroxy-4-nitrobenzaldehydeA K MacGibbon, S C Koerber, K Pease, et al.
Biochemistry|February 19, 1980
Investigation of a novel liver alcohol dehydrogenase catalyzed redox-elimination reaction involving arylnitroso substrate analoguesS C Koerber, P Schack, A M Au, et al.
Biochemistry|June 28, 1977
Lewis acid complexes wchich show spectroscopic similarities to an alcohol dehydrogenase ternary complexC T Angelis, M F Dunn, D C Muchmore, et al.
Biochemistry|October 5, 1993
Characterization of the functional role of a flexible loop in the alpha-subunit of tryptophan synthase from Salmonella typhimurium by rapid-scanning, stopped-flow spectroscopy and site-directed mutagenesisP S Brzović, C C Hyde, E W Miles, et al.
Biochemistry|February 4, 1992
Substitution of glutamic acid 109 by aspartic acid alters the substrate specificity and catalytic activity of the beta-subunit in the tryptophan synthase bienzyme complex from Salmonella typhimuriumP S Brzović, A M Kayastha, E W Miles, et al.
Pageof 11

Showing results (61-70 of 106) with videos related to

Sort By:
Pageof 11
Biochemistry|February 19, 1980
Comparison of the zinc binding domains in the 7S nerve growth factor and the zinc-insulin hexamerM F Dunn, S E Pattison, M C Storm, et al.
The Journal of Biological Chemistry|May 25, 1977
Liver alcohol dehydrogenase-coenzyme reaction ratesM C DeTraglia, J Schmidt, M F Dunn, et al.
Biochemistry|January 6, 1970
Mechanistic studies on equine liver alcohol dehydrogenase. I. The stoichiometry relationship of the coenzyme binding sites to the catalytic sites active in the reduction of aromatic aldehydes in the transient stateS A Bernhard, M F Dunn, P L Luisi, et al.
Biochemistry|January 16, 1990
Reaction mechanism of Escherichia coli cystathionine gamma-synthase: direct evidence for a pyridoxamine derivative of vinylglyoxylate as a key intermediate in pyridoxal phosphate dependent gamma-elimination and gamma-replacement reactionsP Brzović, E L Holbrook, R C Greene, et al.
Biochemistry|June 20, 2001
Beta D305A mutant of tryptophan synthase shows strongly perturbed allosteric regulation and substrate specificityD Ferrari, L H Yang, E W Miles, et al.
Biochemistry|June 2, 1987
Characterization of a transient intermediate formed in the liver alcohol dehydrogenase catalyzed reduction of 3-hydroxy-4-nitrobenzaldehydeA K MacGibbon, S C Koerber, K Pease, et al.
Biochemistry|February 19, 1980
Investigation of a novel liver alcohol dehydrogenase catalyzed redox-elimination reaction involving arylnitroso substrate analoguesS C Koerber, P Schack, A M Au, et al.
Biochemistry|June 28, 1977
Lewis acid complexes wchich show spectroscopic similarities to an alcohol dehydrogenase ternary complexC T Angelis, M F Dunn, D C Muchmore, et al.
Biochemistry|October 5, 1993
Characterization of the functional role of a flexible loop in the alpha-subunit of tryptophan synthase from Salmonella typhimurium by rapid-scanning, stopped-flow spectroscopy and site-directed mutagenesisP S Brzović, C C Hyde, E W Miles, et al.
Biochemistry|February 4, 1992
Substitution of glutamic acid 109 by aspartic acid alters the substrate specificity and catalytic activity of the beta-subunit in the tryptophan synthase bienzyme complex from Salmonella typhimuriumP S Brzović, A M Kayastha, E W Miles, et al.
Pageof 11