| Trypsin from pyloric caeca of the red hind grouper, Epinephelus guttatus, was detected, purified 48 fold, and characterized. Groupers were obtained from southwestern coastal water of Puerto Rico. Enzyme purification procedures consisted of ammonium sulfate fractionation of pyloric caeca homogenate followed by size exclusion chromatography of protein from the resuspended 45% ammonium sulfate pellet. The anionic character of grouper trypsin was determined with ion-exchange chromatography. The enzyme has a molecular weight between 17,000 and 44,000d and displays optimal activity in the pH range of 7.0 to 8.0. Highest activity was observed at 40... |
