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Evidence that the nature of amino acid residues in the P3 position directs substrates to distinct catalytic sites of the pituitary multicatalytic proteinase complex (proteasome).
Cardozo C, Vinitsky A, Michaud C, Orlowski M. Cardozo C, et al. Biochemistry. 1994 May 31;33(21):6483-9. doi: 10.1021/bi00187a014. Biochemistry. 1994. PMID: 8204582
Cleavage of bonds after neutral amino acids by the multicatalytic proteinase complex (MPC) has been recently shown to be catalyzed by at least three distinct components [Orlowski, M., Cardozo, C., & Michaud, C. (1993) Biochemistry 32, 1563-1572]. One comp …
Cleavage of bonds after neutral amino acids by the multicatalytic proteinase complex (MPC) has been recently shown to be catalyzed by at lea …
Evidence for the presence of five distinct proteolytic components in the pituitary multicatalytic proteinase complex. Properties of two components cleaving bonds on the carboxyl side of branched chain and small neutral amino acids.
Orlowski M, Cardozo C, Michaud C. Orlowski M, et al. Among authors: cardozo c. Biochemistry. 1993 Feb 16;32(6):1563-72. doi: 10.1021/bi00057a022. Biochemistry. 1993. PMID: 8431436
This component is apparently identical with the previously identified DCI-resistant component of the MPC that cleaves preferentially bonds on the carboxyl side of branched chain amino acids in natural peptides including neurotensin and proinsulin [Cardozo, C., Vinit …
This component is apparently identical with the previously identified DCI-resistant component of the MPC that cleaves preferentially bonds o …
297 results