Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Willard W. Hall"'
Autor:
Willard W. Hall, Thomas A. Krenitsky
Publikováno v:
Preparative biochemistry. 20(1)
Formycin B [9-deazainosine] was reacted with epoxy-activated Sepharose 6B to form an affinity resin for purine nucleoside phosphorylase (PNPase). This resin had a large capacity (7,600 units/ml) for the enzyme from Escherichia coli. Enzyme retention
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cb8b23da4520710ad8397efd97e3658c
https://pubmed.ncbi.nlm.nih.gov/2114620
https://pubmed.ncbi.nlm.nih.gov/2114620
Autor:
Willard W. Hall, Thomas A. Krenitsky
Publikováno v:
Archives of Biochemistry and Biophysics. 251:36-46
Aldehyde oxidase (EC 1.2.3.1) plays a role in the oxidation of aromatic heterocyclic compounds ingested by some higher vertebrates. To better understand this function, the specificity of the rabbit liver enzyme toward purines and their analogs was qu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::14e073327276909988a6589d17afc1a4
https://doi.org/10.1016/0003-9861(86)90048-2
https://doi.org/10.1016/0003-9861(86)90048-2
Publikováno v:
Journal of Medicinal Chemistry. 32:1471-1475
Azathioprine [Imuran; 6-[(1-methyl-4-nitro-1H-imidazol-5-yl)thio]-1H-purine] is a widely used immunosuppressive and antiarthritic drug. For the sake of comparison, the riboside, the 2'-deoxyriboside, and the arabinoside of azathioprine and its 2-amin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6624c0dc3c3465be5adcffe97b5ade57
https://doi.org/10.1021/jm00127a013
https://doi.org/10.1021/jm00127a013
Autor:
Donald J. Nelson, Catherine U. Lambe, David J.T. Porter, Willard W. Hall, Thomas A. Krenitsky, Thomas Spector
Publikováno v:
Biochemical Pharmacology. 38:4315-4320
Compound B103U, 4-hydroxy-6-mercaptopyrazolo[3,4-d]pyrimidine, was investigated as an inhibitor of human xanthine oxidase. Studies in vitro demonstrated that it was significantly more potent than oxypurinol, 4,6-dihydroxypyrazolo[3,4-d]pyrimidine. It
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2ef542f14a2d159255847b89fda4649a
https://doi.org/10.1016/0006-2952(89)90531-5
https://doi.org/10.1016/0006-2952(89)90531-5
Publikováno v:
Biochemical Pharmacology. 35:3109-3114
Oxipurinol inhibited human xanthine oxidase and bovine xanthine oxidases by very similar mechanisms. It bound to an electronically reduced form of human xanthine oxidase in a manner similar to that previously discerned from its interactions with the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8d1f9ca2809b744fe72bbdecf8f50b20
https://doi.org/10.1016/0006-2952(86)90394-1
https://doi.org/10.1016/0006-2952(86)90394-1
Publikováno v:
Archives of Biochemistry and Biophysics. 247:108-119
Xanthine oxidase [EC 1.2.3.2] was purified 2000-fold from human liver. The last step of the procedure involved affinity chromatography. The resulting preparation showed two closely migrating bands of enzyme activity after gel electrophoresis under no
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9e54fd6f3a9fefff6df3bac28db1b74d
https://doi.org/10.1016/0003-9861(86)90539-4
https://doi.org/10.1016/0003-9861(86)90539-4