Zobrazeno 1 - 10
of 91
pro vyhledávání: '"Barton Holmquist"'
Extracellular Fluid Proteins of Goldfish Brain: Evidence for the Presence of Proteases and Esterases
Autor:
Barton Holmquist, Victor E. Shashoua
Publikováno v:
Journal of Neurochemistry. 47:738-743
Preparations of enriched fractions of extracellular fluid (ECF) proteins from goldfish brain were found to contain protease(s) and esterase(s). The N-substituted furanacryloyl (FA) peptides FA-Phe-Gly-Gly and FA-Phe-OMe were used as model substrates
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2f168427860d3fec66ceb32016ddbabf
https://doi.org/10.1111/j.1471-4159.1986.tb00674.x
https://doi.org/10.1111/j.1471-4159.1986.tb00674.x
Publikováno v:
Alcoholism: Clinical and Experimental Research. 19:860-866
Electrophoresis of rabbit liver homogenate on starch gel followed by activity staining revealed multiple forms of alcohol dehydrogenase (ADH) which, based on their electrophoretic mobilities, had been tentatively labeled as class “I,” class “II
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4b1c77c76e8569742bbe15a2e4bf0670
https://doi.org/10.1111/j.1530-0277.1995.tb00959.x
https://doi.org/10.1111/j.1530-0277.1995.tb00959.x
Publikováno v:
Analytical Chemistry. 64:181-186
Both class I and class II alcohol dehydrogenase (ADH) activities are present in human serum. The contribution of each class can be measured using two class-specific, fluorogenic substrates, 4-methoxy-1-naphthaldehyde and 6-methoxy-2-naphthaldehyde. T
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::76e9590de900ec15e36b80fe4d9dc1ff
https://doi.org/10.1021/ac00026a017
https://doi.org/10.1021/ac00026a017
Publikováno v:
Biochemistry. 31:475-481
The glutathione-dependent formaldehyde dehydrogenase from Escherichia coli has been purified to homogeneity and characterized. It is a 83,000-kDa homodimer containing 4 g-atom of zinc per dimer with a specific activity of 60 units/mg toward S-(hydrox
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::227b247225ce056303466b06eaa21068
https://doi.org/10.1021/bi00117a025
https://doi.org/10.1021/bi00117a025
Autor:
Barton Holmquist, Bert L. Vallee
Publikováno v:
Biochemical and Biophysical Research Communications. 178:1371-1377
Human liver class III alcohol dehydrogenase (chi chi-ADH) and glutathione dependent formaldehyde dehydrogenase are the same enzyme. The enzyme, chi chi-ADH, exhibits a kcat of 200 min-1 and a km of 4 microM for the oxidation of formaldehyde, but only
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bfc9733b50c7d61f1ce5a6b09d138c36
https://doi.org/10.1016/0006-291x(91)91045-e
https://doi.org/10.1016/0006-291x(91)91045-e
Autor:
Bert L. Vallee, Jan-Olov Höög, Edward A. Fox, Hans Jörnvall, Christina Karlsson, Barton Holmquist, Mats Estonius, William S. Davidson
Publikováno v:
European Journal of Biochemistry. 194:593-602
The major ethanol-active form of chicken liver alcohol dehydrogenase was characterized. The primary structure was determined by peptide analysis and, to a large part, was also deduced by cDNA analysis of a near full-length cDNA clone. The latter was
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::97e6215ca13494035059a756b31ef971
https://doi.org/10.1111/j.1432-1033.1990.tb15657.x
https://doi.org/10.1111/j.1432-1033.1990.tb15657.x
Autor:
Mats ESTONIUS, Christina KARLSSON, Edward A. FOX, Jan-Olov HOOG, Barton HOLMQUIST, Bert L. VALLEE, William S. DAVIDSON, Hans JORNVALL
Publikováno v:
European Journal of Biochemistry. 194:598-602
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a42e3287c7255d33a33dede512d8e152
https://doi.org/10.1111/j.1432-1033.1990.tb15658.x
https://doi.org/10.1111/j.1432-1033.1990.tb15658.x
Autor:
Ulrika Waldenström, Bengt Persson, Tomas Bergman, Hans Jörnvall, Bert L. Vallee, Barton Holmquist, Wing Ming Keung
Publikováno v:
European journal of biochemistry. 216(1)
The enzymatic and structural properties of alligator liver alcohol dehydrogenase have been determined. Aliphatic and alicyclic alcohols serve as substrates for this first reptilian form of the enzyme characterized, with Km values decreasing rapidly f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c44a632277101410751c91cbe963cb11
https://pubmed.ncbi.nlm.nih.gov/8365416
https://pubmed.ncbi.nlm.nih.gov/8365416
Publikováno v:
Biochemistry. 32(19)
Modification of class III alcohol dehydrogenase (chi chi-ADH) with phenylglyoxal eliminates fatty acid activation by pentanoate and octanoate and concomitantly increases specific activity toward ethanol and 3-methylcrotyl alcohol 2-3-fold. In contras
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::882c2c6ff1622c8e863b075351a89802
https://pubmed.ncbi.nlm.nih.gov/8494891
https://pubmed.ncbi.nlm.nih.gov/8494891
The origin of the fatty acid activation and formaldehyde dehydrogenase activity that distinguishes human class III alcohol dehydrogenase (alcohol:NAD+ oxidoreductase, EC 1.1.1.1) from all other alcohol dehydrogenases has been examined by site-directe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5c9f8894bb61b3016231ec3decf2d208
https://europepmc.org/articles/PMC46113/
https://europepmc.org/articles/PMC46113/
