Zobrazeno 1 - 10
of 22
pro vyhledávání: '"Jan Kvassman"'
Autor:
Joseph D. Shore, Steven T. Olson, Ingrid M. Verhamme, Jan Kvassman, Richard Swanson, Duane E. Day
Publikováno v:
Biochemistry. 40:11742-11756
Michaelis complex, acylation, and conformational change steps were resolved in the reactions of the serpin, plasminogen activator inhibitor-1 (PAI-1), with tissue plasminogen activator (tPA) and trypsin by comparing the reactions of active and Ser 19
Autor:
Paul E. Bock, Jan Kvassman, Steven T. Olson, David Ginsburg, Joseph D. Shore, Ingemar Björk, Daniel A. Lawrence
Publikováno v:
Journal of Biological Chemistry. 270:30007-30017
The contribution of a covalent bond to the stability of complexes of serine proteinases with inhibitors of the serpin family was evaluated by comparing the affinities of β-trypsin and the catalytic serine-modified derivative, β-anhydrotrypsin, for
Autor:
Jan Kvassman, Ingrid M. Verhamme, David Ginsburg, Duane E. Day, Ann Marie Francis-Chmura, Joseph D. Shore, Daniel A. Lawrence
Publikováno v:
Journal of Biological Chemistry. 270:5395-5398
A mutant recombinant plasminogen activator inhibitor 1 (PAI-1) was created (Ser-338 → Cys) in which cysteine was placed at the P9 position of the reactive center loop. Labeling this mutant with N,N′-dimethyl-N(acetyl)-N′-(7-nitrobenz-2-oxa-1,3-
Publikováno v:
Bioorganic Chemistry. 19:53-65
Desacetamidocolchicine (3) and desacetamidoisocolchicine (4) have been chromatographically resolved into enantiomers. Thermal racemization gives inversion barriers of 22.1 and 23.4 kcal mol−1, respectively, for rotation around the bond joining the
Autor:
Rob Horsefield, Richard Neutze, Maria Fellert, Kristina Nordén, Jan Kvassman, Per Kjellbom, Anke C. Terwisscha van Scheltinga, Susanna Törnroth-Horsefield, Anna Backmark, Urban Johanson
Publikováno v:
Proceedings of the National Academy of Sciences, 105(36). NATL ACAD SCIENCES
Human aquaporin 5 (HsAQP5) facilitates the transport of water across plasma membranes and has been identified within cells of the stomach, duodenum, pancreas, airways, lungs, salivary glands, sweat glands, eyes, lacrimal glands, and the inner ear. AQ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::10f55adb6a924e293940a1fbb7501a74
https://research.rug.nl/en/publications/73801ed4-a396-46e0-9d55-db50eb09e305
https://research.rug.nl/en/publications/73801ed4-a396-46e0-9d55-db50eb09e305
Autor:
Jason P. Beech, Jonas O. Tegenfeldt, Seyed R. Tabaei, Urban Johanson, Fredrik Höök, Jan Kvassman, Per Kjellbom, Gabriel Ohlsson
Publikováno v:
Lab on a Chip. 12:4635
Screening assays designed to probe ligand and drug-candidate regulation of membrane proteins responsible for ion-translocation across the cell membrane are wide spread, while efficient means to screen membrane-protein facilitated transport of uncharg
Autor:
Gösta Pettersson, Jan Kvassman
Publikováno v:
European Journal of Biochemistry. 186:265-272
1. The kinetics of 1,3-bisphosphoglycerate binding to glyceraldehyde-3-phosphate dehydrogenase have been examined by stopped-flow techniques in the absence and presence of phosphoglycerate kinase, using enzyme concentrations in the range 0.5-40 micro
Publikováno v:
European Journal of Biochemistry. 118:119-123
1. The interaction of decanoate and benzoate with the substrate-binding site in liver alcohol dehydrogenase has been characterized by fluorimetric equilibrium binding studies, using auramine O as a receptor ligand. 2. The affinity of the enzyme for t
Publikováno v:
European Journal of Biochemistry. 133:651-655
Aldehyde binding to liver alcohol dehydrogenase in the absence and presence of coenzymes has been characterized by spectrometric equilibrium methods, using auramine O and bipyridine as reporter ligands. Free enzyme shows a significant affinity for al
Publikováno v:
European Journal of Biochemistry. 139:519-527
The interaction of liver alcohol dehydrogenase with NADH and aldehyde substrates has been characterized with respect to ternary-complex formation by the apparently non-preferred pathway which involves intermediate formation of binary enzyme X aldehyd