Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Bernard Schwendimann"'
Publikováno v:
Biochimie. 81:765-770
Allomyces arbuscula, an aquatic fungus, contains two Ca2+-dependent neutral cysteine proteases (CDP I and CDP II), eluting respectively, at 0.07 and 0.2 M NaCl from DEAE cellulose columns. The purified CDP I has a Mr of 39 kDa whereas CDP II appears
Publikováno v:
Journal of Molecular Biology. 108:123-138
Glyceraldehyde 3-phosphate dehydrogenase extracted from sturgeon muscle, exhibits half-site reactivity in its reaction with the pseudo-substrate β -(2-furyl) acryloyl phosphate ( Malhotra & Bernhard, 1968 ). The product is the difurylacryloyl thiol
Publikováno v:
European journal of biochemistry. 143(2)
Peptides containing the C-terminus of the alpha-chain of the nicotinic acetylcholine receptor (nAChR), as deduced from cDNA data, were synthesised and shown to bind to antibodies to denatured nAChR. Conversely, peptide-specific antibodies bound both
Publikováno v:
The Journal of protozoology. 27(4)
Under aerobic conditions, we have determined glycerol uptake in the long slender (LS) bloodstream form of Trypanosoma (Trypanozoon) brucei brucei by studying glycerophosphate accumulation in the parasites. The coupled enzyme theory applies to the per
Publikováno v:
Hoppe-Seyler's Zeitschrift fur physiologische Chemie. 361(10)
The iodination of alpha-bungarotoxin and the reactivity of iodinated derivatives towards nicotinic acetylcholine receptor are described. 125I2- and 125I-alpha-bungarotoxin can be resolved, but the latter was not separated from unreacted alpha-bungaro
Publikováno v:
Pyridine Nucleotide-Dependent Dehydrogenases
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::aedfb1130ab27bc59274a6f8407f8e93
https://doi.org/10.1515/9783110853704-010
https://doi.org/10.1515/9783110853704-010
Autor:
S.J. Remington, Bernard Schwendimann, Gail E. Christie, Brian W. Matthews, Margaret A. Holmes
Publikováno v:
Journal of molecular biology. 112(4)
Crystals of sturgeon holo- D -glyceraldehyde-3-phosphate dehydrogenase have space group P 6 1 22 with cell dimensions a = b = 82.2 A and c = 458 A, implying that this tetrameric enzyme has an exact 2-fold axis of symmetry. The results obtained here a