Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Filters

S G Waley

Showing results (11-20 of 83) with videos related to

Pageof 9
Sort By:
The Biochemical Journal|October 1, 1991
The kinetics of substrate-induced inactivationS G Waley
The Biochemical Journal|September 1, 1982
A quick method for the determination of inhibition constantsS G Waley
Science Progress|January 1, 1988
Beta-lactamases: a major cause of antibiotic resistanceS G Waley
The Biochemical Journal|August 15, 1993
The kinetics of slow-binding and slow, tight-binding inhibition: the effects of substrate depletionS G Waley
Microbiological Sciences|May 1, 1987
An explicit model for bacterial resistance: application to beta-lactam antibioticsS G Waley
The Biochemical Journal|January 1, 1972
The pK of the carboxyl group at the active centre of triose phosphate isomeraseS G Waley
The Biochemical Journal|July 15, 1988
Imipenem as substrate and inhibitor of beta-lactamasesJ Monks, S G Waley
Biochemistry|November 19, 1985
Cryoenzymology of Bacillus cereus beta-lactamase IIR Bicknell, S G Waley
The Biochemical Journal|October 1, 1985
Single-turnover and steady-state kinetics of hydrolysis of cephalosporins by beta-lactamase I from Bacillus cereusR Bicknell, S G Waley
The Biochemical Journal|September 15, 1988
Kinetic characterization of the acyl-enzyme mechanism for beta-lactamase IM T Martin, S G Waley
Pageof 9

Showing results (11-20 of 83) with videos related to

Sort By:
Pageof 9
The Biochemical Journal|October 1, 1991
The kinetics of substrate-induced inactivationS G Waley
The Biochemical Journal|September 1, 1982
A quick method for the determination of inhibition constantsS G Waley
Science Progress|January 1, 1988
Beta-lactamases: a major cause of antibiotic resistanceS G Waley
The Biochemical Journal|August 15, 1993
The kinetics of slow-binding and slow, tight-binding inhibition: the effects of substrate depletionS G Waley
Microbiological Sciences|May 1, 1987
An explicit model for bacterial resistance: application to beta-lactam antibioticsS G Waley
The Biochemical Journal|January 1, 1972
The pK of the carboxyl group at the active centre of triose phosphate isomeraseS G Waley
The Biochemical Journal|July 15, 1988
Imipenem as substrate and inhibitor of beta-lactamasesJ Monks, S G Waley
Biochemistry|November 19, 1985
Cryoenzymology of Bacillus cereus beta-lactamase IIR Bicknell, S G Waley
The Biochemical Journal|October 1, 1985
Single-turnover and steady-state kinetics of hydrolysis of cephalosporins by beta-lactamase I from Bacillus cereusR Bicknell, S G Waley
The Biochemical Journal|September 15, 1988
Kinetic characterization of the acyl-enzyme mechanism for beta-lactamase IM T Martin, S G Waley
Pageof 9