G. Patel

A new fluorogenic substrate for chymotrypsin.

E. Yurewicz, M. Zimmerman, G. Patel, 1976, Analytical biochemistry.

Consequences of molecular recognition in the S1-S2 intersubsite region of papain for catalytic-site chemistry. Change in pH-dependence characteristics and generation of an inverse solvent kinetic isotope effect by introduction of a P1-P2 amide bond into a two-protonic-state reactivity probe.

C. Wharton, K. Brocklehurst, E. Thomas, 1988, The Biochemical journal.

SLOW METAL TRANSFER IN HYDROLYSES PROMOTED BY GOLD(III) IONS

G. Patel, D. Satchell, R. S. Satchell, 1981 .

A marked gradation in active-centre properties in the cysteine proteinases revealed by neutral and anionic reactivity probes. Reactivity characteristics of the thiol groups of actinidin, ficin, papain and papaya peptidase A towards 4,4'-dipyridyl disulphide and 5,5'-dithiobis-(2-nitrobenzoate) diani

K. Brocklehurst, F. Willenbrock, S. Mushiri, 1983, The Biochemical journal.

Evidence for a close similarity in the catalytic sites of papain and ficin in near-neutral media despite differences in acidic and alkaline media. Kinetics of the reactions of papain and ficin with chloroacetate.

K. Brocklehurst, F. Willenbrock, S. Mushiri, 1982, The Biochemical journal.

Sensitive assays for trypsin, elastase, and chymotrypsin using new fluorogenic substrates.

E. Yurewicz, M. Zimmerman, B. Ashe, 1977, Analytical biochemistry.

Supracrystallographic resolution of interactions contributing to enzyme catalysis by use of natural structural variants and reactivity-probe kinetics.

C. Topham, K. Brocklehurst, E. Thomas, 1988, The Biochemical journal.