François Pochon
French Institute of Health and Medical Research
6 Papers
76 Citations
François Pochon is an academic researcher from French Institute of Health and Medical Research. The author has contributed to research in topics: Chymotrypsin & Substrate (chemistry). The author has an hindex of 5, co-authored 6 publications.
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Papers
Ultrastructure of alpha 2-macroglobulins.
TL;DR: It is confirmed that alpha 2M is a twin trap capable of inactivating one or two proteinases by partial immobilization and the technical limitations reached with some techniques and some possible extensions of future research in the field are presented.
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Study of the Hansenula anomala yeast flavocytochrome‐b2–cytochrome‐c complex 1. Characterization of fluorescent Zn(II)‐substituted cytochrome c
TL;DR: H. anomala Zn-cytochrome c appears to be in the form of a stable though non-covalent dimer from molecular weight determinations performed using gel filtration, polyacrylamide gel electrophoresis under denaturing conditions, and ultracentrifugation methods.
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Localization of the proteinases in the human alpha 2-macroglobulin-chymotrypsin complex by image processing of electron micrographs.
Nicolas Boisset,Jean-Christophe Taveau,François Pochon,Martine Barray,Etienne Delain,Jean Lamy +5 more
TL;DR: The comparison of the alpha 2M molecules transformed either by immobilized chymotrypsin or methylamine shows that the proteolysis of the bait regions seems of minimal importance for the general shape of the molecule and provides a direct visualization of the actual role of the thiol esters in the conformational change.
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The reaction of human α2‐macroglobulin with α‐chymotrypsin
TL;DR: The kinetics of the conformational changes of human α2-macroglobulin (α2M) induced by reaction with pure α-chymotrypsin, have been analyzed using three fluorescent probes, namely protein tryptophan groups and the dye 6-(4-toluidino)-2-naphthalenesulfonate, to monitor alterations of the α2M structure.
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INTERACTION OF PROTEIN SUBSTRATE AND INHIBITORS WITH α2-MACROGLOBULIN-BOUND PROTEINASES
TL;DR: This work attempts to quantify the interaction between a,M-bound trypsin and chymotrypsinogen, a protein substrate for which the kinetic parameters k,,, and K, can be measured and whether or not the a, M-induced decrease in proteinase-inhibitor affinity depends upon the size of the inhibitor as is usually believed.
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