Zobrazeno 1 - 10
of 46
pro vyhledávání: '"Robert B. van Huystee"'
Autor:
S. V. Muginova, Robert B. van Huystee, Irina G. Gazaryan, Nailya A. Bagirova, Tatyana N. Shekhovtsova
Publikováno v:
Analytical Letters. 39:521-541
Mercury(II) in the range of 0.1–1 µg L−1 concentrations was found to be a much more efficient inhibitor of native peanut peroxidase (PNP) than of horseradish peroxidase (HRP) in the reaction of o‐dianisidine oxidation with hydrogen peroxide. T
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::feda974fae2ffc9edb55773d32682c7f
https://doi.org/10.1080/00032710500536137
https://doi.org/10.1080/00032710500536137
Autor:
Evgeny G. Evtushenko, Alexei V. Caramyshev, Viktor F. Ivanov, Alfonso Ros Barceló, Ivan Yu. Sakharov, Manuel G. Roig, Robert B. van Huystee, and Andrey Kh. Vorobiev, Iliya N. Kurochkin, Shnyrov Vl
Publikováno v:
Biomacromolecules. 6:1360-1366
Comparison of the stability of five plant peroxidases (horseradish, royal palm tree leaf, soybean, and cationic and anionic peanut peroxidases) was carried out under acidic conditions favorable for synthesis of polyelectrolyte complexes of polyanilin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ea777522342dac71391659c13bc9e89f
https://doi.org/10.1021/bm049370w
https://doi.org/10.1021/bm049370w
Autor:
David G. Pina, Andrei P. Jadan, Ivan Yu. Sakharov, Francisco Gavilanes, Robert B. van Huystee, Enrique Villar, Laura S. Zamorano, Valery L. Shnyrov, Manuel G. Roig
Publikováno v:
Thermochimica Acta. 417:67-73
Detailed differential scanning calorimetry (DSC), steady-state tryptophan fluorescence and far-UV circular dichroism (CD) studies, together with enzymatic assays, were carried out to monitor the thermal stability of anionic peanut peroxidase (aPrx) a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::657ad7612981261e6659528497c0fb50
https://doi.org/10.1016/j.tca.2004.01.018
https://doi.org/10.1016/j.tca.2004.01.018
Publikováno v:
Phytochemistry. 65:1575-1588
Cationic peanut peroxidase (CP) was isolated from peanut (Arachis hypogaea) cell suspension culture medium. CP is a glycoprotein with three N-linked glycan sites at Asn60, Asn144, and Asn185. ESI-MS of the intact purified protein reveals the microhet
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::84bd445799860da3a585228ad390fd5e
https://doi.org/10.1016/j.phytochem.2004.03.031
https://doi.org/10.1016/j.phytochem.2004.03.031
Publikováno v:
Phytochemistry Reviews. 3:19-28
Peroxidases are known to be very stable enzymes. The reasons for such have not yet been fully investigated. Cationic peroxidase from cultured peanut peroxidase can be obtained in substantial amounts and can easily be purified. It is thus an ideal enz
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c165856c6a030025e052495619464574
https://doi.org/10.1023/b:phyt.0000047802.79211.32
https://doi.org/10.1023/b:phyt.0000047802.79211.32
Publikováno v:
Talanta. 55:1151-1164
The influence of phenol and its derivatives on the kinetics of oxidation of aryldiamines (indicator-substrates) catalyzed by novel plant peroxidase—cationic peanut peroxidase—was studied. The character of influence of phenols on the kinetics of e
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8fe08bae25bbb73f4e3bebb68180cf42
https://doi.org/10.1016/s0039-9140(01)00544-6
https://doi.org/10.1016/s0039-9140(01)00544-6
Publikováno v:
Archives of Biochemistry and Biophysics. 386:17-24
Peanut peroxidase has been diffracted. The location of its heme and calcium moieties have been shown and their role demonstrated. However, the structure and role of its glycans is only now being elucidated. The role of three N-linked complex glycans
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::18ffca3eb42baf8cf5e2847371bc0049
https://doi.org/10.1006/abbi.2000.2187
https://doi.org/10.1006/abbi.2000.2187
Publikováno v:
Plant Science. 136:159-168
Cationic peanut ( Arachis hypogaea ) peroxidase (CPRX) is the major isozyme of peanut peroxidases secreted into the culture medium from the cells growing in liquid suspension culture. In this report, CPRX was expressed in transgenic tobacco ( Nicotia
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::bda0d3f4ede4c7fd0de5ba32ad8bb1bb
https://doi.org/10.1016/s0168-9452(98)00087-9
https://doi.org/10.1016/s0168-9452(98)00087-9
Autor:
Trish A. Murray, Robert B. van Huystee, Ian N. Watson, Lyn M. Watson, Michael T. McManus, Bao Lige
Publikováno v:
Plant Physiology and Biochemistry. 36:591-599
Two cationic peroxidase isoenzymes have been identified, using ion-exchange and hydrophobic column chromatography, in the spent media of peanut cells maintained in suspension culture. One isoenzyme, designated CPz-I, has a molecular mass of 34 000 Da
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::83e97e07724ab26cb051526890749966
https://doi.org/10.1016/s0981-9428(98)80007-7
https://doi.org/10.1016/s0981-9428(98)80007-7
Publikováno v:
Plant Physiology and Biochemistry. 36:335-338
A cDNA sequence containing the entire cationic peanut (Arachis hypogaea) peroxidase (EC 1.11.1.7, CPRX) coding sequence, including a 22-amino acid signal peptide, was extended using a synthetic oligonucleotide with a six histidine-tag at the C-termin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::628f95506be8efd8c919beeb295db186
https://doi.org/10.1016/s0981-9428(98)80074-0
https://doi.org/10.1016/s0981-9428(98)80074-0