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Cited by 252

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

Identification of a novel angiotensin‐I‐converting enzyme inhibitory peptide corresponding to a tryptic fragment of bovine β‐lactoglobulin

Open access
Mullally, Margaret M, Meisel, Hans, FitzGerald, Richard J·1997·FEBS Letters
DOI 10.1016/s0014-5793(96)01503-7
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Abstract

The angiotensin‐I‐converting enzyme (ACE) inhibitory activity of a tryptic digest of bovine β‐lactoglobulin (β‐lg) was investigated. Intact β‐lg essentially did not inhibit ACE while the tryptic digest gave an 84.3% inhibition of ACE. Peptide material eluting between 20 and 25% acetonitrile during C 18 solid‐phase extraction of the β‐lg tryptic digest inhibited ACE by 93.6%. This solid‐phase extraction fraction was shown by mass spectroscopy to contain β‐lg f(142–148). This peptide had an ACE IC 50 value of 42.6 μmol/l. The peptide was resistant to further digestion with pepsin and was hydrolysed to a very low extent with chymotrypsin. The contribution of specific amino acid residues within the peptide to ACE inhibitory activity and the potential application of this peptide as a nutraceutical is discussed.

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Metadata

Authors
Mullally, M. M., Meisel, H., & FitzGerald, R. J.
Venue
FEBS Letters
Publisher
Wiley
Published
1997-01-27
Volume
402
Issue
2-3
Pages
99-101
ISSN
  • 0014-5793 (ISSN-L)
  • 1873-3468
DOI
10.1016/s0014-5793(96)01503-7
OpenAlex
W2056357797
Cited by
252
References
1
FWCI
1.57
Type
journal article
Language
en
Open access
bronze

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