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Sodium dodecyl sulfate-stable complexes between serpins and active or inactive proteinases contain the region COOH-terminal to the reactive site loop.
Christensen S, Valnickova Z, Thøgersen IB, Pizzo SV, Nielsen HR, Roepstorff P, Enghild JJ. Christensen S, et al. Among authors: valnickova z. J Biol Chem. 1995 Jun 23;270(25):14859-62. doi: 10.1074/jbc.270.25.14859. J Biol Chem. 1995. PMID: 7797463 Free article.
Recently inhibitors of the serpin family were shown to form complexes with dichloroisocoumarine (DCI)-inactivated proteinases under native conditions (Enghild, J. J., Valnickova, Z., Thogersen I., and Pizzo, S. V. (1994) J. Biol. Chem. 269, 20159-20166). This study …
Recently inhibitors of the serpin family were shown to form complexes with dichloroisocoumarine (DCI)-inactivated proteinases under native c …
The heparin-binding domain of extracellular superoxide dismutase is proteolytically processed intracellularly during biosynthesis.
Enghild JJ, Thogersen IB, Oury TD, Valnickova Z, Hojrup P, Crapo JD. Enghild JJ, et al. Among authors: valnickova z. J Biol Chem. 1999 May 21;274(21):14818-22. doi: 10.1074/jbc.274.21.14818. J Biol Chem. 1999. PMID: 10329680 Free article.
During the purification of human EC-SOD, the intact/cleaved ratio remains constant, suggesting that proteolytic removal of the heparin-binding domain does not occur during purification (Oury, T. D., Crapo, J. D., Valnickova, Z., and Enghild, J. J. (1996) Biochem. J. …
During the purification of human EC-SOD, the intact/cleaved ratio remains constant, suggesting that proteolytic removal of the heparin-bindi …
51 results