Journal of immunology (Baltimore, Md. : 1950), 136(2), 452-458 (1986-01-01)
A limited intralysosomal proteolytic degradation is probably a key event in the accessory cell processing of large protein antigens before their presentation to T cells. With the aid of highly specific inhibitors of proteinases, we have examined the role of
Biochimica et biophysica acta, 1388(1), 84-92 (1998-10-17)
The kinetic theory of the substrate reaction during modification of enzyme activity has been applied to study the inactivation kinetics of enzymes by denaturant. However, an important problem related to the determination of the inactivation rate constants has not been
The Journal of biological chemistry, 258(8), 4676-4678 (1983-04-25)
The formation of the bovine beta-trypsin-bovine basic pancreatic trypsin inhibitor (Kunitz) (BPTI) complex was monitored, making use of three different signals: proflavine displacement, optical density changes in the ultraviolet region, and the loss of the catalytic activity. The rates of
Biochimica et biophysica acta, 915(3), 421-425 (1987-10-15)
A titration method for determination of trypsin-like serine proteinase concentration has been developed by using ZArgONp and ZLysONp, two specific chromogenic amino-acid derivatives which show the characteristics of optimal active-site titrants. Active proteinase concentration has been estimated from the effect
The Biochemical journal, 215(3), 555-563 (1983-12-01)
A detailed study of the kinetics of the trypsin (EC 3.4.21.4)-catalysed hydrolysis of N-alpha-benzyloxycarbonyl-L-lysine p-nitrophenyl ester in cryosolvents at 0 degrees C and below was undertaken. The pH-dependences of kcat, Km, k+2, k+3 and Ks were determined under cryoenzymological conditions
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