Effect of ultrasound on activation of serine proteases precursors.
The effect of ultrasound (US) (26.4 kHz, 26 W/cm2) on the activation process of a mixture of chymotrypsinogen and trypsinogen was studied. US led to a significant decrease in proteolytic activity, as well as inhibition of the activation process in general. It was shown that inhibition of proteinase activity under US influence was a consequence of inhibition of chymotrypsinogen-chymotrypsin transformation and the complete proteolytic trypsin degradation in the proenzymes mixture.
Ovsianko
S L
SL
Research Institute for Physical and Chemical Problems, Belarusian State University, Leningradskaya St., 14, Lab 602, Minsk 220050, Belarus. biopharm@bsu.by
Chernyavsky
E A
EA
Minchenya
V T
VT
Adzerikho
I E
IE
Shkumatov
V M
VM
D000596:Amino Acids / Q000737:chemistry; D002851:Chromatography, High Pressure Liquid; D002919:Chymotrypsinogen / Q000737:chemistry / Q000528:radiation effects; D004789:Enzyme Activation / Q000528:radiation effects; D007700:Kinetics; D012697:Serine Endopeptidases / Q000737:chemistry* / Q000528:radiation effects*; D014362:Trypsinogen / Q000737:chemistry / Q000528:radiation effects; D014465:Ultrasonics
D000596:Amino Acids; D014362:Trypsinogen; D002919:Chymotrypsinogen; D012697:Serine Endopeptidases