Zobrazeno 1 - 10
of 34
pro vyhledávání: '"C K, De Bruyne"'
Autor:
C. K. de Bruyne, O. van Opstal
Publikováno v:
Bulletin des Sociétés Chimiques Belges. 93:185-190
A general reaction scheme for glycosidase catalyzed hydrolyses, proceeding via a two-phase reaction, is presented. It explains, on the basis of some simple assumptions, transfer to nucleophiles other than water, selftransfer and substrateinhibition.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::21ee040a93cbf86451f4094239841f65
https://doi.org/10.1002/bscb.19840930304
https://doi.org/10.1002/bscb.19840930304
Publikováno v:
Bulletin des Sociétés Chimiques Belges. 94:123-125
A thermostated diafiltration apparatus (1–2 ml) is described. A more rigorous control of cell-volume and temperature during equilibrium binding experiments by forced-flow ultrafiltration is obtained. Because the apparatus induces two reservoirs wit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a04a20f09dad3258f2078a1e7923b0b5
https://doi.org/10.1002/bscb.19850940209
https://doi.org/10.1002/bscb.19850940209
Autor:
J. Vandekerckhove, R Cornelis, W Vangrysperre, J. Van Damme, C. K. de Bruyne, Hilda Kersters-Hilderson
Publikováno v:
Biochemical Journal. 265:699-705
D-Xylose isomerases from different bacterial strains were chemically modified with histidine and carboxylate-specific reagents. The active-site residues were identified by amino acid sequence analysis of peptides recognized by differential peptide ma
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7b60856dfd8681602046a39f063d67d6
https://doi.org/10.1042/bj2650699
https://doi.org/10.1042/bj2650699
Publikováno v:
Canadian Journal of Biochemistry. 58:5-8
The influence of the chain length in n-alkyl β-D-xylopyranosides and of the para substituents in aryl β-D-xylopyranosides on the kinetic parameters (Ka, V) for hydrolysis of these substrates by a β-D-xylosidase from Penicillium wortmanni, has been
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::64a373b884c1f08b2baab600d893f344
https://doi.org/10.1139/o80-002
https://doi.org/10.1139/o80-002
Publikováno v:
Biochemical Journal. 250:285-290
The binding of two activating cations, Co2+ and Mg2+, and of one inhibitory cation, Ca2+, to D-xylose isomerase from Streptomyces violaceoruber was investigated. Equilibrium-dialysis and spectrometric studies revealed that the enzyme binds 2 mol of C
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8fceba5a8554e4b917c3bf87ec401bfe
https://doi.org/10.1042/bj2500285
https://doi.org/10.1042/bj2500285
Publikováno v:
Biochemical Journal. 260:163-169
D-Xylose isomerases from Streptomyces violaceoruber, Streptomyces sp., Lactobacillus xylosus, Lactobacillus brevis and Bacillus coagulans were rapidly inactivated by Woodward's reagent K. Second-order rate constants in the absence of ligands, at pH 6
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b6f73ea87acd899d09232d12ba722030
https://doi.org/10.1042/bj2600163
https://doi.org/10.1042/bj2600163
Publikováno v:
Archives of Biochemistry and Biophysics. 234:61-72
The pH dependence of the kinetic parameters of beta-D-xylosidase (EC. 3.2.1.37) from Bacillus pumilus reveals that an acidic functional group with pK 8.0 is involved in the catalysis. The fast inactivation of the dimeric enzyme by near equivalent amo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fc3490a6d7891c55930eb60cdf4f8a36
https://doi.org/10.1016/0003-9861(84)90324-2
https://doi.org/10.1016/0003-9861(84)90324-2
Publikováno v:
Methods in enzymology. 83
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::f728de1369f93f6320182288ff234ef2
https://pubmed.ncbi.nlm.nih.gov/6808311
https://pubmed.ncbi.nlm.nih.gov/6808311
Publikováno v:
Archives internationales de physiologie et de biochimie. 83(1)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::334c4e57f1fc51734a2249a2eabf0893
https://pubmed.ncbi.nlm.nih.gov/50798
https://pubmed.ncbi.nlm.nih.gov/50798
Publikováno v:
Archives internationales de physiologie et de biochimie. 84(1)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::faaf8173ea061357d7da083e1dbfbb6c
https://pubmed.ncbi.nlm.nih.gov/60935
https://pubmed.ncbi.nlm.nih.gov/60935