Kinetic studies on the lactate dehydrogenase isozymes of the brown trout, Salmo trutta L

Informative crosses have verified the genetic basis of a polymorphism at the Ldh-1 locus in brown trout and enzyme activity measurements indicate that the previously described polymorphism at this locus is best explained by a null allele. The LDH-1, LDH-2, LDH-3 and LDH-4 homotetrameric isozymes were purified and subjected to enzyme kinetic analysis. While LDH-1 and LDH-2 displayed catalytic equivalence, important kinetic differences were found between the LDH-3 and LDH-4 isozymes.     

Synthesis by Enzymatic Catalysis VI—An Investigation of Chemical Modification of HRP by Fourier Transform Infra-Red Vibrational Spectroscopy

Horseradish peroxidase was chemically conjugated on its carbohydrate moieties with short aliphatic chains (C₈ and C₁₆). An analytical method using FT.IR spectroscopy was developed to analyze this alteration in enzyme structure. This method is non-destructive, and can be applied directly to samples of the reaction mixture. More general applications of this technique are described and discussed.     

Development and virtual screening of target libraries.

The concomitant development of in silico screening technologies and of three-dimensional information on therapeutically relevant macromolecular targets makes it possible to navigate in the structural proteome and to identify targets fulfilling user-defined queries. This review illustrates some in-house recent advances in the development of target libraries and how they can be browsed to unravel chemogenomic information.