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P F Cook

Showing results (101-110 of 130) with videos related to

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Biochemistry|May 21, 1996
Kinetic isotope effects as a probe of the beta-elimination reaction catalyzed by O-acetylserine sulfhydrylaseC C Hwang, E U Woehl, D E Minter, et al.
Archives of Biochemistry and Biophysics|May 15, 1987
Modification of an arginine residue essential for the activity of NAD-malic enzyme from Ascaris suumG S Rao, C T Kong, R C Benjamin, et al.
The Journal of Biological Chemistry|October 15, 1987
Reaction of Ascaris suum phosphofructokinase with diethylpyrocarbonate. Inactivation and desensitization to allosteric modulationG S Rao, B A Wariso, P F Cook, et al.
Biochemistry|August 11, 1999
Mapping the active site topography of the NAD-malic enzyme via alanine-scanning site-directed mutagenesisW E Karsten, L Chooback, D Liu, et al.
Biochemistry|September 26, 1995
Acid-base chemical mechanism of O-acetylserine sulfhydrylases-A and -B from pH studiesC H Tai, S R Nalabolu, J W Simmons, et al.
Biochemistry|March 22, 1988
Kinetics and mechanism of benzoylformate decarboxylase using 13C and solvent deuterium isotope effects on benzoylformate and benzoylformate analoguesP M Weiss, G A Garcia, G L Kenyon, et al.
Protein Expression and Purification|July 24, 1998
Cloning, expression, purification, and characterization of the 6-phosphogluconate dehydrogenase from sheep liverL Chooback, N E Price, W E Karsten, et al.
Biochemistry|May 3, 1988
Isotope exchange as a probe of the kinetic mechanism of pyrophosphate-dependent phosphofructokinaseY K Cho, T O Matsunaga, G L Kenyon, et al.
Biochemistry|November 6, 1984
Determination of dissociation constants for enzyme-reactant complexes for NAD-malic enzyme by modulation of the thiol inactivation rateD M Kiick, B L Allen, J G Rao, et al.
Biochemistry|August 12, 1986
Carbohydrate substrate specificity of bacterial and plant pyrophosphate-dependent phosphofructokinasesB L Bertagnolli, E S Younathan, R J Voll, et al.
Pageof 13

Showing results (101-110 of 130) with videos related to

Sort By:
Pageof 13
Biochemistry|May 21, 1996
Kinetic isotope effects as a probe of the beta-elimination reaction catalyzed by O-acetylserine sulfhydrylaseC C Hwang, E U Woehl, D E Minter, et al.
Archives of Biochemistry and Biophysics|May 15, 1987
Modification of an arginine residue essential for the activity of NAD-malic enzyme from Ascaris suumG S Rao, C T Kong, R C Benjamin, et al.
The Journal of Biological Chemistry|October 15, 1987
Reaction of Ascaris suum phosphofructokinase with diethylpyrocarbonate. Inactivation and desensitization to allosteric modulationG S Rao, B A Wariso, P F Cook, et al.
Biochemistry|August 11, 1999
Mapping the active site topography of the NAD-malic enzyme via alanine-scanning site-directed mutagenesisW E Karsten, L Chooback, D Liu, et al.
Biochemistry|September 26, 1995
Acid-base chemical mechanism of O-acetylserine sulfhydrylases-A and -B from pH studiesC H Tai, S R Nalabolu, J W Simmons, et al.
Biochemistry|March 22, 1988
Kinetics and mechanism of benzoylformate decarboxylase using 13C and solvent deuterium isotope effects on benzoylformate and benzoylformate analoguesP M Weiss, G A Garcia, G L Kenyon, et al.
Protein Expression and Purification|July 24, 1998
Cloning, expression, purification, and characterization of the 6-phosphogluconate dehydrogenase from sheep liverL Chooback, N E Price, W E Karsten, et al.
Biochemistry|May 3, 1988
Isotope exchange as a probe of the kinetic mechanism of pyrophosphate-dependent phosphofructokinaseY K Cho, T O Matsunaga, G L Kenyon, et al.
Biochemistry|November 6, 1984
Determination of dissociation constants for enzyme-reactant complexes for NAD-malic enzyme by modulation of the thiol inactivation rateD M Kiick, B L Allen, J G Rao, et al.
Biochemistry|August 12, 1986
Carbohydrate substrate specificity of bacterial and plant pyrophosphate-dependent phosphofructokinasesB L Bertagnolli, E S Younathan, R J Voll, et al.
Pageof 13