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Pancreatic anionic trypsin: Evidence for the existence of a 30 kDa form

Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, ISSN: 0305-0491, Vol: 102, Issue: 1, Page: 37-41
1992
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1.1. An anionic form of trypsin has been isolated from pancreas of various species (rat, pig, dog and cow).2.2. The purification procedure included affinity chromatography on STI-Sepharose 4B and ion-exchange chromatography on DEAE-Sephadex A-50.3.3. The preparation was homogeneous as checked by SDS-polyacrylamide slab gel electrophoresis, resulting in an estimated molecular weight of 30 kilodaltons (kDa) for this anionic form.4.4. Antibodies against the anionic form from rat pancreas cross-reacted towards the anionic enzyme from porcine pancreas but not with the dog or bovine enzyme, nor with all the studied cationic forms.5.5. Limited proteolysis of tubulin, a cytoskeletal protein, with an anionic or cationic form of trypsin showed striking differences in the size of produced peptides.

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