Figure 1.

Purification of trypsin from pyloric caeca of crevalle jack. (a) Exclusion molecular chromatogram (Sephadex G-75) of dialyzed ammonium sulfate precipitate (F 0%–80%) obtained from crude extract of trypsin from crevalle jack: the eluted protein was monitored at 280 nm [○] and the activity (U) of each fraction was determined using BApNA as substrate [●]. (b) SDS-PAGE (12.5%) of crevalle jack trypsin (arrow) collected using Sephadex G-75 chromatography: (1) Molecular marker standards (myosin > β-galactosidase > bovine serum albumin > ovalbumin > carbonic anhydrase > soybean trypsin inhibitor > lysozyme); (2) crevalle jack trypsin under denaturing and reducing conditions.