Heparin binding peptides from the 23 N-terminal residues of αs1-casein present in commercial preparations of whey protein concentrate, glycomacropeptide and α-lactalbumin

D. E W Chatterton, E. S. Sørensen, T. E. Petersen, B. Lönnerdal

Research output: Contribution to journalArticle

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Abstract

α-Lactalbumin (α-La) and glycomacropeptide (GMP) were separated using heparin affinity chromatography and a one step elution with 1 M NaCl. The eluted peaks were separated by RP-HPLC and identified by N-terminal sequencing followed by matrix-assisted laser desorption/ionisation time-of-flight (MALDI-TOF) mass spectrometry. This study showed that proteolytic activity in whey results in cleavage of at least 12 sites in the 23 N-terminal amino acids of αs1-casein (CN). The greatest concentrations of the 1-23 N-terminal amino acids were found in the α-La product, whereas the greatest concentration of the 1-9 (heparin binding motif) and 1-13 fragments were found in GMP and whey protein concentrate (WPC). The finding of an intact heparin binding 1-23 peptide in the α-La product may account for some of its reported activity against enteropathogenic E. coli.

Original languageEnglish (US)
Pages (from-to)143-146
Number of pages4
JournalMilchwissenschaft
Volume56
Issue number3
StatePublished - 2001

Fingerprint

Lactalbumin
whey protein concentrate
lactalbumin
heparin
Caseins
Heparin
casein
peptides
Peptides
Enteropathogenic Escherichia coli
Amino Acids
enteropathogenic Escherichia coli
amino acids
matrix-assisted laser desorption-ionization mass spectrometry
affinity chromatography
whey
Affinity Chromatography
Mass Spectrometry
Lasers
high performance liquid chromatography

ASJC Scopus subject areas

  • Food Science

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Heparin binding peptides from the 23 N-terminal residues of αs1-casein present in commercial preparations of whey protein concentrate, glycomacropeptide and α-lactalbumin. / Chatterton, D. E W; Sørensen, E. S.; Petersen, T. E.; Lönnerdal, B.

In: Milchwissenschaft, Vol. 56, No. 3, 2001, p. 143-146.

Research output: Contribution to journalArticle

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AU - Chatterton, D. E W

AU - Sørensen, E. S.

AU - Petersen, T. E.

AU - Lönnerdal, B.

PY - 2001

Y1 - 2001

N2 - α-Lactalbumin (α-La) and glycomacropeptide (GMP) were separated using heparin affinity chromatography and a one step elution with 1 M NaCl. The eluted peaks were separated by RP-HPLC and identified by N-terminal sequencing followed by matrix-assisted laser desorption/ionisation time-of-flight (MALDI-TOF) mass spectrometry. This study showed that proteolytic activity in whey results in cleavage of at least 12 sites in the 23 N-terminal amino acids of αs1-casein (CN). The greatest concentrations of the 1-23 N-terminal amino acids were found in the α-La product, whereas the greatest concentration of the 1-9 (heparin binding motif) and 1-13 fragments were found in GMP and whey protein concentrate (WPC). The finding of an intact heparin binding 1-23 peptide in the α-La product may account for some of its reported activity against enteropathogenic E. coli.

AB - α-Lactalbumin (α-La) and glycomacropeptide (GMP) were separated using heparin affinity chromatography and a one step elution with 1 M NaCl. The eluted peaks were separated by RP-HPLC and identified by N-terminal sequencing followed by matrix-assisted laser desorption/ionisation time-of-flight (MALDI-TOF) mass spectrometry. This study showed that proteolytic activity in whey results in cleavage of at least 12 sites in the 23 N-terminal amino acids of αs1-casein (CN). The greatest concentrations of the 1-23 N-terminal amino acids were found in the α-La product, whereas the greatest concentration of the 1-9 (heparin binding motif) and 1-13 fragments were found in GMP and whey protein concentrate (WPC). The finding of an intact heparin binding 1-23 peptide in the α-La product may account for some of its reported activity against enteropathogenic E. coli.

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