Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Rune I. Lindstad"'
Publikováno v:
Biochemical and Biophysical Research Communications. 435:202-208
Sorbitol dehydrogenase inhibitors have been found to prevent, or alleviate, various secondary complications of diabetes mellitus. In the present study, the effects of nucleosides and nucleotides on the rate of sorbitol oxidation catalyzed by the shee
Autor:
Svein-Ole Mikalsen, Eli Berg, Ingebrigt Sylte, Rune I. Lindstad, Jan-Olof Winberg, Per Ottar Seglen
Publikováno v:
Journal of Molecular Biology. 350:682-698
In contrast to the prevalent view in the literature hitherto, the present study shows that pancreatic trypsin can activate human promatrix metalloproteinase-2 (proMMP-2). It is shown that trypsin's ability to activate proMMP-2 is dependent on various
Autor:
Rune I. Lindstad, Berit Mathisen, Jan-Olof Winberg, Thrina Loennechen, Eivind Hovig, Janne Hansen, Øystein Fodstad, Gunhild Mari Mælandsmo, Sara Ann El-Gewely
Publikováno v:
Clinical & Experimental Metastasis. 20:701-711
To study the role of the metastasis associated protein S100A4, an osteosarcoma cell line (OHS) with a high level of this protein was transfected with a vector containing a ribozyme that degrades S100A4 mRNA and, as controls, OHS cells were transfecte
Publikováno v:
FEBS Letters. 408:57-61
The mechanism of the inhibition of sheep liver sorbitol dehydrogenase by the novel antidiabetogenic drug 2-hydroxymethyl-4-(4-N,N-dimethylaminosulfonyl-1-piperazino)pyrimidine has been investigated by steady-state kinetics over the range pH 5–10. T
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1293:267-271
The role of configuration for the affinity labelling of sheep liver sorbitol dehydrogenase by chloro-substituted analogues of 2-bromo-3-(5-imidazolyl)propionate (BrImPpOH) has been studied. A saturation kinetics mechanism applies which includes forma
Publikováno v:
European Journal of Biochemistry. 233:891-898
The variation with pH of the kinetic parameters for sorbitol oxidation and fructose reduction by sheep liver sorbitol dehydrogenase has been studied over the pH 5–10 range. The reaction is compulsory ordered in both directions with the coenzyme as
Publikováno v:
European Journal of Biochemistry. 221:847-854
Reversible inhibition and activation, as well as protection against affinity labelling with DL-2-bromo-3-(5-imidazolyl)propionic acid, of sheep liver sorbitol dehydrogenase have been studied. The results presented are discussed in terms of enzyme act
Autor:
Kristin Andersen, Berit Mathisen, Jan-Olof Winberg, Gunhild Mari Mælandsmo, Rune I. Lindstad, Thrina Loennechen, Janne Hansen, Sara Ann El-Gewely
Publikováno v:
Biochemical pharmacology. 66(12)
Like the metastasis-associated protein S100A4, matrix metalloproteinases (MMPs) and their tissue inhibitors (TIMPs) are important in physiological and pathological conditions. Previously, we showed that S100A4 is involved in the regulation of MMPs an
Autor:
Jan-Olof Winberg, Ingebrigt Sylte, John S. McKinley-McKee, Michelle Kaaber Brendskag, Rune I. Lindstad
Publikováno v:
Journal of molecular biology. 294(2)
Drosophila alcohol dehydrogenase belongs to the short chain dehydrogenase/reductase (SDR) family which lack metal ions in their active site. In this family, it appears that the three amino acid residues, Ser138, Tyr151 and Lys155 have a similar funct
Publikováno v:
European journal of biochemistry. 241(1)
Reversible inhibition of sheep liver sorbitol dehydrogenase by various thiol compounds has been studied. Most species inhibit the enzyme-catalyzed reaction competitively with respect to sorbitol, due to the formation of ternary enzyme-NAD-thiol compl