Purification and some properties of two anionic trypsins from the eel (Anguilla japonica).
Two anionic enzymes, designated as trypsins 1 and 2, were purified from the pancreas of the eel Anguilla japonica by DEAE-cellulose column chromatography and Sephadex G-75 gel filtration. The final preparation of trypsin 1 was homogeneous but that of trypsin 2 still contained impurities. Both enzymes had similar pH optima of near 8.3 for the hydrolysis of N-tosyl-L-arginine methyl ester. Trypsin 1 was stabilized by calcium ions but the stability of trypsin 2 was not affected by calcium ions. Both enzymes were inhibited by typical trypsin inhibitors including serine proteinase inhibitors.
D000811:Anguilla / Q000378:metabolism*; D000818:Animals; D002118:Calcium / Q000494:pharmacology; D006863:Hydrogen-Ion Concentration; D014357:Trypsin / Q000302:isolation & purification*; D014361:Trypsin Inhibitors
D014361:Trypsin Inhibitors; D014357:Trypsin; D002118:Calcium