[Conformational aspects of peptide interaction with proteolytic enzymes. Pepsin-catalyzed hydrolysis of cyclic peptides, containing leucyl-tyrosine fragments].
Pepsin was found capable of splitting cycloota- and cyclodecapeptides cyclo (-L-leucyl-L-tyrosyl-glycln-), n=6 or 8. The 18-membered peptides cyclo(-L-leucyl-L-tyrosyl-glycyl4-) and cyclo(-L-leucyl-L-tyrosy-delta-aminovaleroyl2-) were found stable to the effect of pepsin. To study the kinectics of hydrolysis for tyrosine-containing substrates of pepsin, a method of isolation of the unsplit substrate using ion-exchange resins and quantitative spectrophotometric estimation by absortion of tyysis of cycoocta and cyclodecapeptides was characterized by Km and kcat values.
D006868:Hydrolysis; D007700:Kinetics; D007930:Leucine / Q000378:metabolism*; D010434:Pepsin A / Q000378:metabolism*; D010446:Peptide Fragments / Q000032:analysis; D010456:Peptides, Cyclic / Q000378:metabolism*; D013056:Spectrophotometry, Ultraviolet; D014443:Tyrosine / Q000378:metabolism*
D010446:Peptide Fragments; D010456:Peptides, Cyclic; D014443:Tyrosine; D010434:Pepsin A; D007930:Leucine
Konformatsionnye aspekty vzaimodeĭstviia peptidov s proteoliticheskimi fermentami. Kataliairuemĭ pepsinom gidroliz tsiklicheskikh peptidov, soderzhashchikh leĭtsil-tirozinovye fragmenty