Carica Candamarcensis Peptidase

SCOPUS: ch.binfo:eu-repo/semantics/publishe

Comparaison des structures conformationnelles de divers lysozymes(poule-cane-oie-homme)

Doctorat en Sciencesinfo:eu-repo/semantics/nonPublishe

Comparative effects of N bromosuccinimide on lysozymes of hen egg white and of human origin

SCOPUS: NotDefined.jinfo:eu-repo/semantics/publishe

Evidence that trimethylation of iso 1 cytochrome c from Saccharomyces cerevisiae does not alter its functional properties

SCOPUS: ar.jinfo:eu-repo/semantics/publishe

A comparative study of the thermal denaturation parameters of lysozyme in the dissolved and crystalline states

Differential scanning calorimetry was used for investigating the conformational changes of lysozyme resulting from the combined actions of temperature and of denaturants at various concentrations. The transition temperatures, for the protein in the dissolved and in the crystalline states (tetragonal crystals, crosslinked by glutaraldehyde), were thus investigated in a variety of environmental conditions. The effect of a wide range of alcohols demonstrates that lysozyme, whether in solution or crystalline, displays structural features which are on the whole strikingly similar. By contrast, in the case of urea this similarity becomes apparent only for concentrations higher than 4M. Molecular interpretation of the data, as discussed in the text, is entirely consistent with information from X-ray studies. © 1976.SCOPUS: ar.jinfo:eu-repo/semantics/publishe

Study of the biological significance of cytochrome methylation I. Thermal, acid and guanidinium hydrochloride denaturations of baker's yeast ferricytochromes c

The iso-cytochromes c from baker's yeast: iso-1 methylated and unmethylated forms and iso-2 have been purified and their stabilities towards denaturants compared to that of horse heart cytochrome c. Thermal, acid and guanidinium hydrochloride denaturations were followed using fluorescence emission of their tryptophan 59 and/or the absorbance in the Soret region as the physical parameters. Very few differences could be evidenced among the ferricytochromes investigated in this study insofar as the acid denaturations are concerned. This is to be contrasted with the conclusions of the thermal and guanidinium hydrochloride denaturations studies which clearly showed the ferricytochrome from horse heart to be much more stable than those from baker's yeast. No appreciable differences could be measured among the methylated and unmethylated forms of iso-1 cytochrome c nor among iso-1 and iso-2 cytochromes from baker's yeast. Our results suggest that a stabilizing effect of methylation on the tridimensional structure of ferricytochrome c must probably be discarded. Other possible physiological roles of methylation are suggested taking into account the relative instability of ascomycetes's cytochromes as compared to mammalian ones. © 1976.SCOPUS: ar.jinfo:eu-repo/semantics/publishe

Biological significance of methylation of cytochromes from ascomycetes and plants

The Km and Vmax values characterizing the reaction of baker's yeast iso-I-cytochrome c, whether tri-methylated or not at lysine residue 72, with crude preparations of cytochrome c peroxidase, cytochrome c oxidase and succinate cytochrome c oxidoreductase from Saccharomyces cerevisiae are similar. These results, as well as the redox potential values, the auto-oxidability parameters and the circular dichroism spectra, strongly suggest that the biological methylation of yeast cytochrome c does not alter its functional properties. The functional characteristics of baker's yeast iso-I-cytochrome c are similar to those of horse heart cytochrome c and yeast iso-2-cytochrome c. © 1977.SCOPUS: ar.jinfo:eu-repo/semantics/publishe

Comparative study of the binding to human serum albumin of biliscopine (a new cholangiographic contrast medium) and five other contrast media

SCOPUS: ar.jinfo:eu-repo/semantics/publishe

Protease B from Saccharomyces cerevisiae. Purification and characterization

SCOPUS: ar.jinfo:eu-repo/semantics/publishe

Reoxidation of reduced hen egg white lysozyme fragment 1-123

The reactivation of reduced lysozyme, whose 6 COOH-terminal amino acid including cysteine 127 were cut off, was studied. The results show that the disulfide bridge I-VIII as well as the COOH-terminal hexapeptide do not play a decisive role in the acquisition of the native 3-dimensional structure of the enzyme. © 1978 Birkhäuser Verlag.SCOPUS: ar.jinfo:eu-repo/semantics/publishe