Instruments for Kinetic Studies HPLC and Fluorimetry make possible studies of enzymatic activity

Instruments for Protein Purification and Kinetic Studies
Chromatography and fluorimetry make possible studies of enzymatic activity of newly-synthesized enzyme variants.

A Perkin-Elmer LS55 spectrofluorometer enables static or slow kinetic processes to be monitored. Enzyme constructs can be evaluated if fluorometric substrates are available. This enables evaluation of Km and Vmax at very low substrate concentrations. These will be used by Dr. David Rodgers and Louis Hersh with proteolytic enzymes. The high sensitivity of this instrument is compatible with such concentrations. The instrument is also being used by Dr. Richard McCann for studying depolymerization of proteins involved in cell architecture, such as Talins, and Dr.Wally Whitehart for platelet aggregation studies. Fluorescence depolarization is available for measuring rotational motion of proteins.

HPLC (Waters Breeze) which uses a programmable gradient and UV- vis dual wavelengrth detector is used to monitor slow kinetics of enzyme-catalyzed hydrolysis of peptides. This methodology is an alternative to using fluorometric substrates.

Protein purification with automated fraction collector and computer generated data is available using the gradient CSB Akta Explorer FPLC.

Perkin Elmer LS-55 fluoromter is ultra sensitive, for enzyme kinetics and binding studies

Waters BREEZE HPLC (UV-vis) can be used for analytical resolution of mixtures of peptides