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- W2063253668 abstract "Aims: To purify and characterize a peptidase that can catalyse C-terminal processing of antihypertensive peptide from Lactobacillus helveticus CM4. Methods and Results: An endopeptidase which seems to process the carboxyl terminal end of two antihypertensive peptides, Val-Pro-Pro and Ile-Pro-Pro, was purified from Lactobacillus helveticus CM4 by four stages of column chromatography, using synthetic pro-peptide as a substrate. The molecular weight of the purified enzyme was estimated to be 67 000 by SEPHACRYL S-200 and 70 000 by SDS-PAGE analysis. The purified enzyme generated: (i) Val-Pro-Pro from Val-Pro-Pro-Phe-Leu and Val-Pro-Pro-Phe-Leu-Gln-Pro, and (ii) Ile-Pro-Pro from Ile-Pro-Pro-Leu-Thr and Ile-Pro-Pro-Leu-Thr-Gln-Thr, but theses peptides could not be generated from Val-Pro-Pro-Phe, Val-Pro-Pro-Phe-Leu-Gln, Ile-Pro-Pro-Leu and Ile-Pro-Pro-Leu-Thr-Gln. Part of the amino terminal sequence of the purified enzyme had homology to a previously reported pepO gene product. Conclusion: These results suggest that the purified endopeptidase isolated in this study have an important role in the carboxyl terminal processing of two antihypertensive peptides in Lact. helveticus CM4." @default.
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- W2063253668 date "2004-10-01" @default.
- W2063253668 modified "2023-09-23" @default.
- W2063253668 title "Purification and characterization of an endopeptidase that has an important role in the carboxyl terminal processing of antihypertensive peptides in Lactobacillus helveticus CM4" @default.
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- W2063253668 doi "https://doi.org/10.1111/j.1472-765x.2004.01560.x" @default.
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