Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Jerome Souppe"'
Publikováno v:
Biocatalysis. 7:289-295
In an attempt to alter the catalytic properties of horseradish peroxidase (HRP, EC 1.11.1.7), aspartic, glutamic and arginine residues were modified using ethanedithiol and diacetyl. Modification of Asp and Glu led to a marked increase in Vmax along
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4ce151d322839cdcfb0c85da17fcc796
https://doi.org/10.3109/10242429308992101
https://doi.org/10.3109/10242429308992101
Publikováno v:
Bioorganic Chemistry. 19:133-142
The oxidation of polyethylene glycol monomethyl ethers (MW 350, 1990, and 5000) by the Moffatt-Swern method to the corresponding aldehyde is described. These aldehydes are used to modify horseradish peroxidase (HRP) by a reductive amination. The modi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5b1ff4c78f64ef0b9786a88da5bcbecd
https://doi.org/10.1016/0045-2068(91)90029-o
https://doi.org/10.1016/0045-2068(91)90029-o
Publikováno v:
Enzyme and Microbial Technology. 12:46-51
This paper deals with enzymatic activities present in dialyzed crude extracts of methanol-grown Pichia pastoris : oxidation of NADH by O 2 , degradation of NADH, secondary alcohol dehydrogenase and formate dehydrogenase activities. The use of crude e
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0708a36515c375b0a9ff1b1b8fd5399a
https://doi.org/10.1016/0141-0229(90)90179-t
https://doi.org/10.1016/0141-0229(90)90179-t
Publikováno v:
Journal of chromatography. 613(1)
A simple and rapid method for measuring phenylethanolamine N-methyltransferase (PNMT) activity by high-performance liquid chromatography (HPLC) with ultraviolet (UV) detection is described. This assay requires a partially purified PNMT preparation de
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a4992b7db78bdad2b1297fcbf6d37935
https://pubmed.ncbi.nlm.nih.gov/8458902
https://pubmed.ncbi.nlm.nih.gov/8458902
Publikováno v:
Biochimica et biophysica acta. 1079(2)
Histidine residues in horseradish peroxidase (HRP) were modified chemically with diethyl pyrocarbonate, 4,omega-dibromoacetophenone or diallylpyrocarbonate. Histidines were chosen as His-170, the fifth ligand of the heme iron atom, forms part of the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ca236041fb264b98d7c2efbe86246b57
https://pubmed.ncbi.nlm.nih.gov/1911843
https://pubmed.ncbi.nlm.nih.gov/1911843
Publikováno v:
Analytica Chimica Acta. 208:295-300
An electrochemical sensor with two soluble enzymes allows assay of 0.1–10 mM, l- carnitine with an accuracy of 2%. The assay takes about 2 min. The first enzyme, carnitine dehydrogenase, catalyzes the oxidation of l-carnitine by NAD+. The NADH form
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::69fc4e28c1653c99af676913e3bb2f37
https://doi.org/10.1016/s0003-2670(00)80759-x
https://doi.org/10.1016/s0003-2670(00)80759-x
Autor:
Martine Urrutigoïty, Jerome Souppe
Publikováno v:
Biocatalysis. 2:145-149
This paper describes the preparation of polyethyleneglycol-bound horseradish peroxidase. Coupling with the polymer occurs via the glycolic moiety of the protein after an optimised oxidation process with periodate. Analysis of the modified enzyme show
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::cd01ba2309532f02add89a9ce835c7b6
https://doi.org/10.3109/10242428909003655
https://doi.org/10.3109/10242428909003655