Pepsin behavior as a catalyst in equilibrium-controlled peptide synthesis.
It has been shown that in the course of 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.
Filippova IYu
Chemistry Department of Moscow State University, USSR.
Lysogorskaya
E N
EN
Anisimova
V V
VV
Abdel Malak
C A
CA
Lavrenova
G I
GI
Stepanov
V M
VM
D000595:Amino Acid Sequence; D002384:Catalysis; D007700:Kinetics; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000138:chemical synthesis / Q000737:chemistry; D010434:Pepsin A / Q000737:chemistry*; D010455:Peptides / Q000138:chemical synthesis* / Q000737:chemistry
D009842:Oligopeptides; D010455:Peptides; D010434:Pepsin A