The isolation and partial characterization of trypsin from the pancreas of the ostrich Struthio camelus.
Cationic trypsin was isolated and purified from the pancreas of the ostrich (Struthio camelus) by affinity chromatography on a Trasylol-Sepharose column. External activation of trypsinogen was required before trypsin could be isolated. The final preparation was homogeneous by SDS-PAGE and by sedimentation equilibrium centrifugation studies, resulting in Mr values of 24,547 and 22,091, respectively. The Mmin value obtained from amino acid analysis was 22,450. A mean sedimentation coefficient of 2S was obtained by sedimentation velocity centrifugation. Results obtained from N-terminal and amino acid analyses were similar to those from trypsins of other species. The effects of pH, temperature and inhibitors (LBTI, KBPTI and PMSF) on the tryptic activity were examined. The effect of calcium ions and enzyme concentration on the rate of self-digestion of ostrich trypsin was also investigated.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001717:Birds / Q000378:metabolism*; D002417:Cattle; D002846:Chromatography, Affinity; D004789:Enzyme Activation; D007700:Kinetics; D008970:Molecular Weight; D010179:Pancreas / Q000201:enzymology*; D014357:Trypsin / Q000302:isolation & purification* / Q000378:metabolism; D014362:Trypsinogen / Q000302:isolation & purification / Q000378:metabolism
D000596:Amino Acids; D014362:Trypsinogen; D014357:Trypsin