TRYPTIC ACTIVATION OF ACETYLATED CHYMOTRYPSINOGEN

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The lodination of Chymotrypsinogen

Katz, E. & Weissbach, H. (1963). J. biol. Chem. 238, 666. Kossel, A. & Edlbacher, S. (1915). Hoppe-Seyl. Z. 94, 264. Linko, P., Alfthan, M., Miettinen, J. K. & Virtanen, A. I. (1953). Acta chem. 8cand. 7, 1310. Lowry, 0. H., Rosebrough, N. J., Farr, A. L. & Randall, R. J. (1951). J. biol. Chem. 193, 265. Moore, S. & Stein, W. H. (1948). J. biol. Chem. 176, 367. Ratner, S., Nocito, V. & Green, D...

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Mechanism of Tryptic Activation of Clostridium Botulinum Type E Toxin.

Gerwing, Julia (University of British Columbia, Vancouver, B.C., Canada), Claude E. Dolman, and Arthur Ko. Mechanism of tryptic activation of Clostridium botulinum type E toxin. J. Bacteriol. 89:1176-1179. 1965.-The toxic peptide of trypsin activated Clostridium botulinum type E toxin was purified by chromatography through columns packed with Sephadex G-75 and G-50. The molecular weight of the ...

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The tryptic activation pathway of monomeric procarboxypeptidase A.

Procarboxypeptidases are the remaining major digestive zymogens the activation process of which remains unsolved. Here it is shown that in the tryptic activation of monomeric procarboxypeptidase A from porcine pancreas, the generation of carboxypeptidase A (CPA) activity parallels the limited proteolysis of the 94-residue activation segment. This degradation proceeds from the COOH-terminal end ...

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Doxycycline Indirectly Inhibits Proteolytic Activation of Tryptic Kallikrein-Related Peptidases and Activation of Cathelicidin

The increased abundance and activity of cathelicidin and kallikrein 5 (KLK5), a predominant trypsin-like serine protease (TLSP) in the stratum corneum, have been implicated in the pathogenesis of rosacea, a disorder treated by the use of low-dose doxycycline. Here we hypothesized that doxycycline can inhibit activation of tryptic KLKs through an indirect mechanism by inhibition of matrix metall...

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Amino terminal group in chymotrypsinogen.

Bovine chymotrypsinogen Q! was examined for N-terminal groups by Rovery et al. (l), using both the dinitrophenyl (DNP) and the phenyl isocyanate techniques (2, 3). Their failure to find evidence for any such group, together with the absence of a C-terminal residue reactive towards carboxypeptidase (4), suggested that this protein consists of one or more cyclic peptide chains. Evidence has now b...

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ژورنال

عنوان ژورنال: Proceedings of the National Academy of Sciences

سال: 1964

ISSN: 0027-8424,1091-6490

DOI: 10.1073/pnas.51.2.151