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Guy Hervé

Researcher at Centre national de la recherche scientifique

Publications -  28
Citations -  579

Guy Hervé is an academic researcher from Centre national de la recherche scientifique. The author has contributed to research in topics: Aspartate carbamoyltransferase & Allosteric enzyme. The author has an hindex of 15, co-authored 28 publications receiving 571 citations.

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Hydrolysis of β-lactoglobulin by thermolysin and pepsin under high hydrostatic pressure

TL;DR: Hydrolysis of β‐lactoglobulin with thermolysin and pepsin at pressures ranging between 0.1 and 350 MPa showed a significant increase of cleavage rates, indicating combined influence of pressure‐induced thermoly sin activation and partial unfolding of β-lactogobulin by compression at neutral pHs.
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The stimulation of Escherichia coli aspartate transcarbamylase activity by adenosine triphosphate. Relation with the other regulatory conformational changes; a model.

TL;DR: The pH dependence of the stimulation by ATP and adenylyl methylenediphosphonate indicates that the binding of these nucleotides requires the ionization of their last phosphate acidic group, providing additional evidence that homotropic and heterotropic interactions correspond to different molecular mechanisms.
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Coupling of homotropic and heterotropic interactions in Escherichia coli aspartate transcarbamylase

TL;DR: 2-ThioU-aspartate transcarbamylase, a modified form of the enzyme in which the homotropic cooperative interactions between the catalytic sites are selectively abolished, shows the same heterogeneity in CTP binding sites as normal aspartates transcarb amylase.
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The primary structure of the aspartate transcarbamylase region of the URA2 gene product in Saccharomyces cerevisiae. Features involved in activity and nuclear localization.

TL;DR: A sequence in the central region of the protein and two short sequences in the C-terminal region are good candidates for the nuclear location signal involved in the targeting of the URA2 product.
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A reactor permitting injection and sampling for steady state studies of enzymatic reactions at high pressure: tests with aspartate transcarbamylase.

TL;DR: A high pressure reactor for steady state studies of enzymes is described, which can be used for any enzymatic reaction; unlike previously described high pressure apparatus, it is not limited to the study of enzymes whose activity can be directly followed by spectrophotometry.