Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Jan Derk G. Smit"'
Autor:
Klaus Piontek, Martina Struck-Donatz, Gerko Hester, Jan Derk G. Smit, Franco A. Rossi, Olga Brenner-Holzach, Kaspar H. Winterhalter
Publikováno v:
FEBS Letters. 292:237-242
The structure of fructose-1,6-bisphosphate aldolase from Drosophila melanogaster has been determined by X-ray diffraction at 2.5 A resolution. The insect enzyme crystallizes in space group P2(1)2(1)2(1) with lattice replacement with rabbit muscle ald
Autor:
Jan Derk G. Smit, Patricia J. Harvey, John M. Palmer, Gerhard Frank, Martin Goble, Sergio Molinari, Tuomo Glumoff, Matti Leisola
Publikováno v:
European Journal of Biochemistry. 187:515-520
Five isozymes of lignin peroxidase from Phanerochaete chrysosporium were purified and their physical, molecular and kinetic properties determined. The isozymes differ from each other in terms of their isoelectric point, molecular mass, sugar content,
Autor:
Krystyna M. Urbanska, Jan Derk G. Smit
Publikováno v:
Journal of Natural History. 20:1467-1476
Rhodanese (EC 2.8.1.1) is a sulphurtransferase which catalyses in vitro the formation of thiocyanate from cyanide and thiosulphate or some other sulphur donor. One proposed function of this multifunctional enzyme in vivo is detoxification of cyanide.
Autor:
Kevin M. Smith, Kevin C. Langry, Hiu-Kwong Leung, Juliette T. J. Lecomte, Jan Derk G. Smit, Kaspar H. Winterhalter, Gerd N. La Mar
Publikováno v:
Journal of Molecular Biology. 197:101-110
Reconstitution of liver fluke (Dicrocoelium dendriticum) apo-hemoglobin with hemins selectively deuterated at specific positions has permitted the assignment of several heme resonances in the proton nuclear magnetic resonance spectrum of the Met-aquo
Autor:
Jan Derk G. Smit, Gm Giacometti, Paolo Ascenzi, G.A. Gilbert, Kaspar H. Winterhalter, Maurizio Brunori
Publikováno v:
Journal of Molecular Biology. 168:181-191
The spectroscopic properties of Dicrocoelium dendriticum met-hemoglobin, investigated between pH 3·8 and 10·5, display two proton-induced transitions with apparent p K values of 8·1 and 4·7. The spectral changes, over the pH region 6·5 to 10·5,
Publikováno v:
Journal of Molecular Biology. 180:357-370
The 1H nuclear magnetic resonance characteristics of met-cyano and met-aquo hemoglobin from the sheep bile duct parasite Dicrocoelium dendriticum have been compared to those of other monomeric hemoglobins and myoglobins. By varying temperature and pH
Publikováno v:
European Journal of Biochemistry. 155:231-237
The dioxygen affinity of Dicrocoelium dendriticum haemoglobin was determined as a function of pH with a thin-layer diffusion technique. From the oxygen dissociation and association curves Hill coefficients h equal 1 were obtained throughout. Ultracen
Publikováno v:
Journal of Molecular Biology. 209:235-247
Structural features of the heme and the heme cavity of the monomeric hemoglobin (Hb) from the platyhelminth Dicrocoelium dendriticum were investigated by optical and proton nuclear magnetic resonance spectroscopy. Using nuclear Overhauser effects (NO
Publikováno v:
FEBS Letters. (1):59-62
The lignin peroxidase isozyme with an isoelectric point of 4.15 from Phanerochaete chrysosporium was crystallized and the crystal parameters were determined. The new crystals are monoclinic but they are related to the orthorhombic crystals previously
Autor:
Kaspar H. Winterhalter, Armin Fiechter, Jörg Kallen, Matti S. A. Leisola, Jakob Troller, Jan Derk G. Smit
Publikováno v:
Nature Biotechnology. 6:571-573
The major lignin peroxidase from carbon limited cultures of the white–rot fungus Phanerochaete chrysosporium was purified by isoelectric focusing and crystallized by the hanging drop method. The nature of the crystalline material as lignin peroxida