Pancreatic anionic trypsin: evidence for the existence of a 30 kDa form.
1. An anionic form of trypsin has been isolated from pancreas of various species (rat, pig, dog and cow). 2. The purification procedure included affinity chromatography on STI-Sepharose 4B and ion-exchange chromatography on DEAE-Sephadex A-50. 3. The preparation was homogenous as checked by SDS-polyacrylamide slab gel electrophoresis, resulting in an estimated molecular weight of 30 kilodaltons (kDa) for this anionic form. 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. Limited proteolysis of tubulin, a cytoskeletal protein, with an anionic or cationic form of trypsin showed striking differences in the size of produced peptides.
Gendry
P
P
INSERM U61, Unité de Biologie Cellulaire et de Physiopathologie Digestives, Strasbourg, France.
Launay
J F
JF
D000818:Animals; D000838:Anions; D002417:Cattle; D003429:Cross Reactions; D004285:Dogs; D007120:Immunochemistry; D008970:Molecular Weight; D010179:Pancreas / Q000201:enzymology*; D051381:Rats; D013045:Species Specificity; D013379:Substrate Specificity; D013552:Swine; D014357:Trypsin / Q000737:chemistry / Q000276:immunology / Q000302:isolation & purification*; D014404:Tubulin
D000838:Anions; D014404:Tubulin; D014357:Trypsin