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A M Kayastha

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Indian Journal of Biochemistry & Biophysics|April 1, 1993
Effect of substrate and phosphate ions on the quaternary structure symmetry of glyceraldehyde-3-phosphate dehydrogenases of mung beans and rabbit muscleO P Malhotra, K Tikoo, Srinivasan, et al.
Indian Journal of Biochemistry & Biophysics|October 1, 1991
Circular dichroism studies of the coenzyme environment in the active sites of mutant forms of the beta-subunit in the tryptophan synthase alpha 2 beta 2 complexA M Kayastha, Y Sawa, S Nagata, et al.
The Journal of Biological Chemistry|November 15, 1991
Mechanism of mutual activation of the tryptophan synthase alpha and beta subunits. Analysis of the reaction specificity and substrate-induced inactivation of active site and tunnel mutants of the beta subunitS A Ahmed, S B Ruvinov, A M Kayastha, 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.
World Journal of Microbiology & Biotechnology|January 29, 2024
Optimizing light regimes for neutral lipid accumulation in Dunaliella salina MCC 43: a study on physiological status and carbon allocationAbhishek Mohanta, Nitesh Prasad, Sk Riyazat Khadim, et al.
Pageof 3

Showing results (21-30 of 25) with videos related to

Sort By:
Pageof 3
You have reached the last page of results.This site can display upto 25 results.
Indian Journal of Biochemistry & Biophysics|April 1, 1993
Effect of substrate and phosphate ions on the quaternary structure symmetry of glyceraldehyde-3-phosphate dehydrogenases of mung beans and rabbit muscleO P Malhotra, K Tikoo, Srinivasan, et al.
Indian Journal of Biochemistry & Biophysics|October 1, 1991
Circular dichroism studies of the coenzyme environment in the active sites of mutant forms of the beta-subunit in the tryptophan synthase alpha 2 beta 2 complexA M Kayastha, Y Sawa, S Nagata, et al.
The Journal of Biological Chemistry|November 15, 1991
Mechanism of mutual activation of the tryptophan synthase alpha and beta subunits. Analysis of the reaction specificity and substrate-induced inactivation of active site and tunnel mutants of the beta subunitS A Ahmed, S B Ruvinov, A M Kayastha, 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.
World Journal of Microbiology & Biotechnology|January 29, 2024
Optimizing light regimes for neutral lipid accumulation in Dunaliella salina MCC 43: a study on physiological status and carbon allocationAbhishek Mohanta, Nitesh Prasad, Sk Riyazat Khadim, et al.
Pageof 3