Zobrazeno 1 - 10
of 81
pro vyhledávání: '"C.L. Borders"'
Publikováno v:
Archives of biochemistry and biophysics. 279(1)
The Escherichia coli, Bacillus stearothermophilus, and human manganese-containing superoxide dismutases (MnSODs) and the E. coli iron-containing superoxide dismutase (FeSOD) are extensively inactivated by treatment with phenylglyoxal, an arginine-spe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d09fcdf6087c227fa38d93ac4fc484bf
https://pubmed.ncbi.nlm.nih.gov/2186704
https://pubmed.ncbi.nlm.nih.gov/2186704
Akademický článek
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Autor:
Irwin Fridovich, C.L. Borders
Publikováno v:
Archives of Biochemistry and Biophysics. 241:472-476
The Cu,Zn superoxide dismutases from bovine liver, yeast, Caulobacter crescentus, and Photobacter leiognathi were compared for their susceptibilities to inhibition by cyanide and to inactivation by hydrogen peroxide and phenylglyoxal. All of these en
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::893b18795953dfbd1feeddf2356268f8
https://doi.org/10.1016/0003-9861(85)90572-7
https://doi.org/10.1016/0003-9861(85)90572-7
Autor:
C.L. Borders, Dianne M. Blech
Publikováno v:
Archives of Biochemistry and Biophysics. 224:579-586
Yeast Cu,Zn superoxide dismutase is inactivated by H 2 O 2 at alkaline pH, and complete inactivation correlates with the modification of 1.0 histidine per subunit. At elevated concentrations of H 2 O 2 , a saturation process is evident and is charact
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::192a2c8b6522ca992d4e8e6d380a7cf1
https://doi.org/10.1016/0003-9861(83)90245-x
https://doi.org/10.1016/0003-9861(83)90245-x
Autor:
C.L. Borders, Dianne M. Perez, Mary B. Fenderson, Alexander J. Kondow, Jesper Brahm, Gregg L. Brelsford, Mark W. Lafferty, Virginia B. Pett
Publikováno v:
Bioorganic Chemistry. 17:96-107
4-Hydroxy-3,5-dinitroacetophenone anion inhibits erythrocyte anion transport with a K 50 of 220 μ m in 165 m m KCl, pH 7.3, at 0°C. Substitution of bromine atoms on the α-carbon greatly enhances the inhibitory potency of this class of compounds. T
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::807e7f75e839ce6a6b912e1f20e77698
https://doi.org/10.1016/0045-2068(89)90011-4
https://doi.org/10.1016/0045-2068(89)90011-4
Autor:
Olivia Bermingham-McDonogh, Andrew Kumamoto, Joan Selverstone Valentine, Duarte Mota de Freitas, C.L. Borders, Dianne M. Blech, Jan E. Saunders
Publikováno v:
Biochemical and Biophysical Research Communications. 108:1376-1382
We have studied the spectroscopic and anion-binding properties of bovine and yeast Cu,Zn superoxide dismutases which have been chemically modified at one arginine per subunit by phenylglyoxal. This modification is known to inactivate these proteins a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8e788a976cbdceedfd520e5dfa2330af
https://doi.org/10.1016/s0006-291x(82)80058-2
https://doi.org/10.1016/s0006-291x(82)80058-2
Autor:
Brett A. Wilson, C.L. Borders
Publikováno v:
Biochemical and Biophysical Research Communications. 73:978-984
Phosphoglycerate mutase is inactivated by butanedione in borate buffer. Inactivation by 0.13 mM reagent correlates with the modification of one arginyl residue per subunit, and is prevented by either 2, 3-diphosphoglycerate or 3-phosphoglycerate. Wit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::afd5ab9af68572a5e709db467e336668
https://doi.org/10.1016/0006-291x(76)90218-7
https://doi.org/10.1016/0006-291x(76)90218-7
Publikováno v:
Biochemical and Biophysical Research Communications. 82:901-906
Yeast enolase is rapidly inactivated by butanedione in borate buffer, complete inactivation correlating with the modification of 1. 8 arginyl residues per subunit. Protection against inactivation is provided by either an equilibrium mixture of substr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4c297b8dea6004d02f2b69dbc75ac5f1
https://doi.org/10.1016/0006-291x(78)90868-9
https://doi.org/10.1016/0006-291x(78)90868-9
Publikováno v:
Biochemical and Biophysical Research Communications. 109:242-249
β-Lactamase (EC 3.5.2.6: penicillin amido-β-lactam hydrolase) I from B. cereus 569 H is inactivated by treatment with phenylglyoxal. Inactivation depends on the pH and the presence of bicarbonate in a manner which suggests that it is due to the mod
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b58765a0aaf0b9887d844c5235230e46
https://doi.org/10.1016/0006-291x(82)91591-1
https://doi.org/10.1016/0006-291x(82)91591-1
Publikováno v:
Biochemical and Biophysical Research Communications. 49:246-251
We wish to report that tryptophan modified with dimethyl (2-hydroxy-5-nitrobenzyl)-sulfonium bromide is stable to conditions of acid hydrolysis with 3 N p-toluenesulfonic acid. This technique of hydrolysis can thus be applied to quantitatively determ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ff058c7d53b5a584e887c55fb140d2f8
https://doi.org/10.1016/0006-291x(72)90036-8
https://doi.org/10.1016/0006-291x(72)90036-8