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Proteinase inhibitors complexes

The inhibitory capacity of a serine protease inhibitor, o( -pI [ref. 58], was investigated by Feste and Gan [ref. 59] by use of a SEC separation of the inhibitor-proteinase complex. The protein-ases used in the investigation were trypsin and elastase. A column and an eluent utilized were TSKgel G2000SW and 0.1 M sodium phosphate buffer. In the SEC separation, the molar ratio of the inhibitor to elastase was varied, and the investigators measured the resulting increase in the peak of the complex and a concomitant reduction of the corresponding elastase peak. This increase in the peak was used to assay the inhibitory capacity of oobtained data were compared with those from a conventional spec-trophotometric assay and found to be consistent with them. [Pg.254]

Blundell TL, Cooper J, Foundling SI, Jones DM, Atrash B, Szelke M. On the rational design of renin inhibitors X-ray studies of aspartic proteinases complexed with transition state analogues. Biochemistry 1987 26 5585-5590. [Pg.338]

The structures of hepatitis A viral 3C proteinases complexed with tetrapeptidyl-based methyl ketone inhibitors were shown to have an episulfide cation embedded in them. The authors concluded that the mechanism of inactivation of 3G peptidases by methyl ketone inhibitors is different than those operating in serine proteinases or in papain-like cysteine peptidases <2006MI673>. [Pg.380]

Gustchina, A., Kervinen, J., Powell, D. J., Zdanov, A., Kay, J., and Wlodawer, A.(I996). Structure of equine infectious anemia virus proteinase complexed with an inhibitor. Protein Science (in press)... [Pg.653]

Foundling, S.I., Cooper, J., Watson, F.E.,, Cleasby, A., Pearl, L.H., et al. (1987) High resolution X-ray analyses of renin inhibitor-aspartic proteinase complexes. Nature 327 349-352. [Pg.458]

McPhalen, C. A., James, M. N. G. Structural comparison of two serine proteinase-protein inhibitor complexes Eglin-C-Subtilisin Carlsberg and CI-2-subtilisin novo. Biochemistry 27 (1988) 6582-6598... [Pg.147]

The mutation of the hydroxyl group positioned in R-configuration at the C(3) atom of the central statine (rSta) residue of the inhibitor gives rise to AAGbind of -0.51 kcal/mol, which is very close to the experimental value of -0.8 kcal/mol. It may be noted here that the starting configuration of the inhibitor in the enzyme-inhibitor complex is the same as that of pepstatin. The crystal structure of rhizopus pepsin or any other aspartic proteinase... [Pg.151]

BINAP-Ru is effective for the diastereoselective hydrogenation of some chiral yS-keto esters (Fig. 32.13). Reaction of N-Boc-protected (S)-y-amino / -keto esters 13A catalyzed by the (R)-BINAP-Ru complex results in the syn alcohols 13B exclusively [52]. The stereocenter at the / -position is controlled by the chirality of the catalyst therefore, use of the S catalyst affords the anti isomer, as predicted. Derivatives of statine, a key component of the aspartic proteinase inhibitor pep-... [Pg.1120]


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See also in sourсe #XX -- [ Pg.39 ]




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