Journal
JOURNAL OF NUTRITIONAL BIOCHEMISTRY
Volume 11, Issue 3, Pages 128-131Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/S0955-2863(99)00083-2
Keywords
peptide from casein; free radical scavenging activity; superoxide anion radical; DPPH radical; hydroxyl radical; tetrazolium salt XTT; ESR
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A peptide having the strong free radical scavenging activities was separated from casein protein hydrolysate by chromatographic analyses such as ion-exchange and gel filtration. SP-II fraction obtained by SP-Sephadex C-25 chromatography showed the most potent superoxide anion scavenging activity (SOSA), and it was further separated into a peptide using an octadecylsilano-high performance liquid chromatography. The amino acid sequence of the peptide was Tyr-Phe-Tyr-Pro-Glu-Leu (YFYPEL). The concentration of the test compound required to reduce the produced superoxide anion to one-half (IC50) value for SOSA, was 79.2 mu M using tetrazolium salt 3'-{1-[(phenylamino)-carbonyl]-3,4-tetrazolium}-bis(4-methoxy-6-nitro)benzenesulfonic acid hydrate method. The IC50 value for the 1,1-diphenyl-2-picrylhydrazyl radical and hydroxyl radical scavenging activities were 98 and 251 mu M, respectively, based on the electron spin resonance method We characterized SOSA of the C-terminal sequence using EL, PEL, YPEL, and FYPEL. The activities of preferred sequences were EL > YFYPEL > FYPEL > YPEL > PEL, suggesting that the Glu-Leu sequence is important for the activity (C) Elsevier Science Inc. 2000. All rights reserved.
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