The Journal of biological chemistry, 257(6), 3014-3017 (1982-03-25)
p-Aminobenzamidine is weakly fluorescent in neutral aqueous buffer, with excitation and emission maxima at 293 and 376 nm, respectively. Binding to trypsin results in a blue shift of the emission peak to 362 nm, and 50-fold fluorescence enhancement, while binding
Comparative studies on the inhibition of trypsin, plasmin, and thrombin by derivatives of benzylamine and benzamidine.
F Markwardt et al.
European journal of biochemistry, 6(4), 502-506 (1968-12-05)
STUDIES ON THE ACTIVE CENTER OF TRYPSIN. THE BINDING OF AMIDINES AND GUANIDINES AS MODELS OF THE SUBSTRATE SIDE CHAIN.
M MARES-GUIA et al.
The Journal of biological chemistry, 240, 1579-1585 (1965-04-01)
Biochemical and biophysical research communications, 457(3), 358-362 (2015-01-13)
The potent fibrinolytic enzyme, plasmin has numerous clinical applications for recannulizing vessels obstructed by thrombus. Despite its diminutive size, 91 kDa, success in the recombinant expression of this serine protease has been limited. For this reason, a truncated non-glycosylated plasmin
Questions
Reviews
★★★★★ No rating value
Active Filters
Nuestro equipo de científicos tiene experiencia en todas las áreas de investigación: Ciencias de la vida, Ciencia de los materiales, Síntesis química, Cromatografía, Analítica y muchas otras.