[Preparation and properties of trypsin from the pyloric caeca of Pacific Ocean salmon].
Trypsin from pyloric caeca of Pacific salmon was purified by affinity chromatography of the water extract on hexamethylenediamine-glycidylmethacrylate-cellulose. A protein band with a molecular weight of 22.5 kDa was found on SDS-electrophoresis in PAG. The protein band was homogeneous according to isoelectrofocusing in PAG (pI 4.0). The amino acid composition of the enzyme is typical of trypsin anionic forms; the major difference from the cationic forms is the lower content of lysine. The differences in properties caused by change of the enzyme molecule charge are similar to those observed in cationic trypsin when the lysine epsilon-amino groups of the latter are modified (change of pI, shift of the pH-optimum towards basic values, increase of stability to autolysis). Some natural trypsin inhibitors of the different origin suppressed the enzyme activity of trypsin from Pacific salmon in typical stoichiometric ratios. An unusual interaction of the enzyme with the specific inhibitor N-L-tosyl-L-lysine chloromethyl ketone was observed.
Pivnenko
T N
TN
Epshteĭn
L M
LM
Kolodzeĭskaia
M V
MV
Kudinov
S A
SA
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D010179:Pancreas / Q000201:enzymology; D010447:Peptide Hydrolases / Q000302:isolation & purification; D012474:Salmon / Q000378:metabolism*; D014357:Trypsin / Q000302:isolation & purification* / Q000378:metabolism
D000596:Amino Acids; D010447:Peptide Hydrolases; D014357:Trypsin
Poluchenie i svoĭstva tripsina iz pilorichekikh pridatkov tikhookeanskikh lososeĭ.