Zobrazeno 1 - 10
of 374
pro vyhledávání: '"S, Ghisla"'
Autor:
S. Ghisla, Alfons Penzkofer, Peyman Zirak, Peter Hegemann, Tilo Mathes, Amit Tyagi, Matthias Mack
Publikováno v:
Chemical Physics. 364:19-30
The flavin dye 8-amino-8-demethyl- d -riboflavin (AF) in the solvents water, DMSO, methanol, and chloroform/DMSO was studied by absorption and fluorescence spectroscopy. The first absorption band is red-shifted compared to riboflavin, and blue-shifte
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d200223f8c02a08525f1f775f46730d6
https://doi.org/10.1016/j.chemphys.2009.08.005
https://doi.org/10.1016/j.chemphys.2009.08.005
Publikováno v:
European journal of biochemistry. 268(21)
The effects of pH, solvent isotope, and primary isotope replacement on substrate dehydrogenation by Rhodotorula gracilis d-amino acid oxidase were investigated. The rate constant for enzyme-FAD reduction by d-alanine increases approximately fourfold
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::9248f4dd9119042658fef403a82b754b
https://pubmed.ncbi.nlm.nih.gov/11683874
https://pubmed.ncbi.nlm.nih.gov/11683874
Publikováno v:
European journal of biochemistry. 268(6)
Here we report the cDNA-deduced amino-acid sequence of L-amino-acid oxidase (LAAO) from the Malayan pit viper Calloselasma rhodostoma, which shows 83% identity to LAAOs from the Eastern and Western diamondback rattlesnake (Crotalus adamanteus and Cro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::241e02b2502b9306a576876687302739
https://pubmed.ncbi.nlm.nih.gov/11248687
https://pubmed.ncbi.nlm.nih.gov/11248687
Brevibacterium sterolicum possesses two forms of cholesterol oxidase, one containing noncovalently bound FAD, the second containing a FAD covalently linked to His(69) of the protein backbone. The functional role of the histidyl-FAD bond in the latter
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::b01eb9583b9493b020e4735f46478ec6
http://hdl.handle.net/11383/1488708
http://hdl.handle.net/11383/1488708
Autor:
D, Edmondson, S, Ghisla
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 131
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::4a32f809f8ffdbbcb509abf32253f369
https://pubmed.ncbi.nlm.nih.gov/10494549
https://pubmed.ncbi.nlm.nih.gov/10494549
Publikováno v:
Biotechnology and applied biochemistry. 30(1)
We have studied systematically the effect of the non-ionic surfactants Thesit and Triton X-100, and of propan-2-ol (used as a substrate solubilizer) on the activity of the cholesterol oxidases from Streptomyces hygroscopicus (SCO) and Brevibacterium
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::5e3b6180a1e919f1103fe8557cd00f5e
https://pubmed.ncbi.nlm.nih.gov/10467115
https://pubmed.ncbi.nlm.nih.gov/10467115
Publikováno v:
The Journal of biological chemistry. 272(8)
The kinetic mechanism of the reaction of D-amino acid oxidase (EC 1.4.3.3) from Trigonopsis variabilis with [alpha-1H]- and [alpha-2H]phenylglycine has been determined. The pH dependence of Vmax is compatible with pKa values of approximately 8.1 and9
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::d7252bfa2be0a59b12e4c91a9931e373
https://pubmed.ncbi.nlm.nih.gov/9030552
https://pubmed.ncbi.nlm.nih.gov/9030552
Publikováno v:
Biochemistry and molecular biology international. 31(4)
D-amino acid oxidase from Trigonopsis variabilis was purified to homogeneity as a well resolved flavoprotein. Specific activity of pure enzyme was 86.6 U/mg at 30 degrees C and pH 8.5. Optimum pH for enzyme activity was 7.5 and optimum temperature wa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::e8e7f4dccf362950ddbab768d749edfe
https://pubmed.ncbi.nlm.nih.gov/7905327
https://pubmed.ncbi.nlm.nih.gov/7905327
Autor:
A, Schieber, S, Ghisla
Publikováno v:
Eicosanoids.
Prostaglandin 9-ketoreductase has been purified to apparent homogeneity from pig and human kidney with an overall yield of 6%. The enzyme has a molecular mass of 34 kDa, it is present as an active monomer in diluted solution and contains approx. 2 eq
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::2bffbb4ad2af0607debfd4b2c8a32917
https://pubmed.ncbi.nlm.nih.gov/1449827
https://pubmed.ncbi.nlm.nih.gov/1449827