| 总结: | Background: Carboxypeptidase A1 (CBPA1) is a well-known protease pancreatic enzyme family member. It catalyzes the hydrolysis of the carbonyl-terminal residue from peptide or ester substrates by cleavage of the peptide or ester bond. Objective: This study aimed to purify and characterize CBPA1 from bovine (Bos taurus) and sheep (Ovis aries) fresh pancreatic tissue. Methods: Bovine and sheep pancreas were collected freshly from Abattoir Complex, Department of Veterinary Services, Shah Alam. The fats were removed by trimming grossly visible fat and by extraction using organic solvents. The CBPA1 was further purified by anion exchange and gel filtration chromatography. Protein identification was performed via LC-MS/MS (liquid chromatography-mass spectrometry). The proteolytic activity was measured using protease assay. Results: Successful purification of CBPA1 from bovine and sheep was visualized as single protein bands on sodium dodecyl sulphate-polyacrylamide gel, which LC-MS/MS confirmed as CBPA1 with the molecular mass of 47.05kDa and 46.87kDa for bovine (Accession number – P00730) and sheep (Accession number – W5P5N4), respectively. The proteolytic enzyme activity was confirmed with protease assay whereby bovine CBPA1 showed higher protease activity than sheep. Conclusion: In conclusion, bovine and sheep CBPA1 were successfully purified from fresh pancreatic tissue and may have the potential for further applications as the proteolytic activity recorded was comparable to that of the porcine protease. Copyright © 2024 The Chinese Medical Association, Published by Wolters Kluwer Health, Inc.
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