Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Erna Steffen"'
Publikováno v:
European Journal of Biochemistry. 86:353-360
Modified trypsin kallikrein inhibitor (I*), with the reactive-site peptide bond Lys-15--Ala-16 split, reacts with alpha-chymotrypsin (E) via an intermediate X to the stable tetrahedral complex C:E + I in equilibrium X leads to C. Formation X constitu
Publikováno v:
Biochemistry. 13:2512-2520
Publikováno v:
European Journal of Biochemistry. 52:511-514
Spectroscopic measurements of virgin bovine trypsin-kallikrein inhibitor and its modified species (in which the reactive-site peptide bond Lys-15--Ala-16 is split) indicate a conformational difference between both proteins. The inhibitor contains fou
Publikováno v:
Biophysical Chemistry. 9:57-64
The dimerization reactions of complete Bence-Jones protein Au (VC-Au) and of its variable fragment (V-Au) were compared in 0.2 M (ionic strength) sodium phosphate buffer, pH 6.8 at 20° C. The dimerization constant for VC-Au (6.6 × 10 4 M −1 ) was
Publikováno v:
Biochemistry. 17(9)
Publikováno v:
European journal of biochemistry. 52(3)
Equilibrium measurements of the binding of reactive-site-cleaved (modified) bovine trypsin-kallikrein inhibitor (Kunitz) to alpha-chymotrypsin and beta-trypsin show a stoichiometric 1:1 association with high binding constants. At least in the case of
Publikováno v:
Bayer-Symposium ISBN: 9783642879685
Recently Luthy et al [1] investigated the mechanism of the interaction between soybean trypsin inhibitor (STI)1 and trypsin by kinetic methods. These authors found that only at very low reactant concentration the reaction is second order with rate co
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8457881d0bed07a7593f0d124fe246e3
https://doi.org/10.1007/978-3-642-87966-1_46
https://doi.org/10.1007/978-3-642-87966-1_46