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Lyublinskaya, V. V.; Королева, И. В.; Stolyarova, E I

doi:10.1023/a:1015500617699

Cited by 1 publication

(1 citation statement)

References 13 publications

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“…most completely by the precipitated adduct of this peptide with phenylalanine methyl ester. Subsequent elution of thermolysin with 1 M NaCl led to nearly quantitative recovery of the active enzyme (13).…”

Section: Dependence Of' Synthesis Eficiencj On Pepsiii Coiiceiirrcitmentioning

confidence: 99%

Pepsin as a catalyst of peptide synthesis Enzyme co‐precipitation with emerging peptide products

Malak

Filippova

Lysogorskaya

et al. 1992

International Journal of Peptide and Protein Research

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Pepsin successfully catalyzed the synthesis of several peptide derivatives from N‐protected di‐ or tripeptides and amino acid or peptide esters or p‐nitroanilides in dimethylformamide‐water solutions at pH 4.6. An optimal substrates:pepsin ratio depended on the structure of starting peptides, especially their fit to the substrate binding sites of the enzyme. For hexapeptide Z‐Ala‐Ala‐Phe‐Leu‐Ala‐Ala‐OCH3 formation, an equilibrium yield was attained at 1:3. 105 enzyme‐substrates ratio that indicated high efficiency of pepsin in synthesis reactions. In the course of the equilibrium peptide synthesis, pepsin gradually disappeared from the liquid phase due to its entrapment within a gel, formed by the hexapeptide product, while retaining its activity. The inclusion into the precipitate was not specific for pepsin, so far as inert proteins, lysozyme, ribonuclease A and carbonic anhydrase, when added to the reaction mixture, became also co‐precipitated with the hexapeptide formed. It appears that co‐precipitation of pepsin, an important factor limiting the enzyme efficiency, might be operative as well for other proteinases used to catalyze peptide synthesis.

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Section: Dependence Of' Synthesis Eficiencj On Pepsiii Coiiceiirrcitmentioning

confidence: 99%