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Autor:
Gerhardus Venema, V.G.H. Eijsink, F Hardy, Bw Dijkstra, O.R Veltman, B Vandervinne, B Vandenburg, Gerrit Vriend, [No Value] Vanderzee
The neutral protease of B. stearothermophilus (NP-ste) is 13 degrees less thermostable than thermolysin, the neutral protease of B. thermoproteolyticus. The sequences of these two proteins differ at 45 positions. By introducing site-directed mutation
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7a07cae3492019af45b0612ea57431e5
https://doi.org/10.1016/b978-0-444-89372-7.50016-6
https://doi.org/10.1016/b978-0-444-89372-7.50016-6
Publikováno v:
Proteins-Structure Function and Bioinformatics, 14(2), 224-236. Wiley
Variants of the thermolabile neutral protease (Npr) of B. subtilis (Npr-sub) and the thermostable neutral protease of B. stearothermophilus (Npr-ste) were produced by means of site-directed mutagenesis and the effects of the mutations on thermostabil