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
- 10Citations
- 5Captures
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Metrics Details
- Citations10
- Citation Indexes10
- 10
- CrossRef2
- Captures5
- Readers5
Article Description
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.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/030504919290269W; http://dx.doi.org/10.1016/0305-0491(92)90269-w; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0026535120&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/1526131; http://linkinghub.elsevier.com/retrieve/pii/030504919290269W; http://api.elsevier.com/content/article/PII:030504919290269W?httpAccept=text/xml; http://api.elsevier.com/content/article/PII:030504919290269W?httpAccept=text/plain; https://linkinghub.elsevier.com/retrieve/pii/030504919290269W; http://dx.doi.org/10.1016/0305-0491%2892%2990269-w; https://dx.doi.org/10.1016/0305-0491%2892%2990269-w
Elsevier BV
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