Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Ariane Gase"'
Publikováno v:
Schriften zur öffentlichen Verwaltung und öffentlichen Wirtschaft
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::54a1fabb4d31fdee4b3c87c642107dcf
https://doi.org/10.35998/9783830543763-05
https://doi.org/10.35998/9783830543763-05
Autor:
Bernhard Schlott, Detlev Behnke, Ariane Gase, Karl-Heinz Gührs, Manfred Hartmann, Desire Collen, Anja Röcker
Publikováno v:
Thrombosis and Haemostasis. 76:755-760
SummaryStructure/function relationships in the activation of plasminogen with staphylokinase were studied using mutants of recombinant staphylokinase (Sak42D). Deletion of up to 10 NH2-terminal amino acids (Sak42DΔN10) did not affect plasminogen act
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bda6f954ff33ef8b9c599878c2f43ab2
https://doi.org/10.1055/s-0038-1650656
https://doi.org/10.1055/s-0038-1650656
Autor:
Gregor Damaschun, Stefan Vetterman, Karl-Heinz Gührs, Klaus Gast, Dietrich Zirwer, Rolf Misselwitz, Bernhard Schlott, Hilde Damaschun, Manfred Hartmann, Desire Collen, Ariane Gase, Eckhard Birch-Hirschfeld
Publikováno v:
European Journal of Biochemistry. 223:303-308
Three natural variants (wild-type staphylokinase, [R36G, R43H]staphylokinase, and [G34S, R36G, R43H]staphylokinase) of the bacterial plasminogen-activator staphylokinase, a 136-amino-acid protein secreted by certain Staphylococcus aureus strains, hav
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4dfe384ba735802717e572e9f6c3be46
https://doi.org/10.1111/j.1432-1033.1994.tb18995.x
https://doi.org/10.1111/j.1432-1033.1994.tb18995.x
Autor:
H.R. Lijnen, Bernard Schlott, Karl-Heinz Gührs, Desire Collen, Ariane Gase, Manfred Hartmann, Stephan Vettermann, Eckehart Birch-Hirschfeld
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1204:235-242
Variants of recombinant staphylokinase (Sak) were produced by site-specific mutagenesis of the unique Met-26 residue and purified to homogeneity from the cell extract of transformed E. coli. The desired mutations were confirmed by cDNA and amino-acid
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7d32c821d27718ee20cb023650995c71
https://doi.org/10.1016/0167-4838(94)90013-2
https://doi.org/10.1016/0167-4838(94)90013-2