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S A Bernhard

Showing results (11-20 of 44) with videos related to

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Biochemistry|June 22, 1971
Mechanism of alkylation of rabbit muscle glyceraldehyde 3-phosphate dehydrogenaseR A MacQuarrie, S A Bernhard
Biochemistry|November 23, 1971
Rapid kinetic evidence for adduct formation between the substrate analog p-nitroso-N,N-dimethylaniline and reduced nicotinamide-adenine dinucleotide during enzymic reductionM F Dunn, S A Bernhard
Journal of Molecular Biology|April 14, 1970
Are the structure and function of an enzyme the same in aqueous solution and in the wet crystal?G L Rossi, S A Bernhard
Annual Review of Biophysics and Bioengineering|January 1, 1973
Structure and symmetry of oligomeric enzymesB W Matthews, S A Bernhard
Annual Review of Biophysics and Bioengineering|January 1, 1973
Structure and symmetry of oligomeric enzymesB W Matthews, S A Bernhard
Biochemistry|October 26, 1971
Studies of catalysis by acetylcholinesterase. I. Fluorescent titration with a carbamoylating agentT L Rosenberry, S A Bernhard
Biochemistry|March 10, 1987
Mechanism of transfer of reduced nicotinamide adenine dinucleotide among dehydrogenases. Transfer rates and equilibria with enzyme-enzyme complexesD K Srivastava, S A Bernhard
Biochemical Society Transactions|October 1, 1987
Functional consequences of the direct transfer of metabolites in muscle glycolysisS A Bernhard, D K Srivastava
Science (New York, N.Y.)|November 28, 1986
Metabolite transfer via enzyme-enzyme complexesD K Srivastava, S A Bernhard
Biochemistry|January 29, 1985
Mechanism of transfer of reduced nicotinamide adenine dinucleotide among dehydrogenasesD K Srivastava, S A Bernhard
Pageof 5

Showing results (11-20 of 44) with videos related to

Sort By:
Pageof 5
Biochemistry|June 22, 1971
Mechanism of alkylation of rabbit muscle glyceraldehyde 3-phosphate dehydrogenaseR A MacQuarrie, S A Bernhard
Biochemistry|November 23, 1971
Rapid kinetic evidence for adduct formation between the substrate analog p-nitroso-N,N-dimethylaniline and reduced nicotinamide-adenine dinucleotide during enzymic reductionM F Dunn, S A Bernhard
Journal of Molecular Biology|April 14, 1970
Are the structure and function of an enzyme the same in aqueous solution and in the wet crystal?G L Rossi, S A Bernhard
Annual Review of Biophysics and Bioengineering|January 1, 1973
Structure and symmetry of oligomeric enzymesB W Matthews, S A Bernhard
Annual Review of Biophysics and Bioengineering|January 1, 1973
Structure and symmetry of oligomeric enzymesB W Matthews, S A Bernhard
Biochemistry|October 26, 1971
Studies of catalysis by acetylcholinesterase. I. Fluorescent titration with a carbamoylating agentT L Rosenberry, S A Bernhard
Biochemistry|March 10, 1987
Mechanism of transfer of reduced nicotinamide adenine dinucleotide among dehydrogenases. Transfer rates and equilibria with enzyme-enzyme complexesD K Srivastava, S A Bernhard
Biochemical Society Transactions|October 1, 1987
Functional consequences of the direct transfer of metabolites in muscle glycolysisS A Bernhard, D K Srivastava
Science (New York, N.Y.)|November 28, 1986
Metabolite transfer via enzyme-enzyme complexesD K Srivastava, S A Bernhard
Biochemistry|January 29, 1985
Mechanism of transfer of reduced nicotinamide adenine dinucleotide among dehydrogenasesD K Srivastava, S A Bernhard
Pageof 5