Inhibition of bovine trypsin by the phosphorylated N‐terminal part β(1–105) of β‐casein

Medientyp: E-Artikel

Titel: Inhibition of bovine trypsin by the phosphorylated N‐terminal part β(1–105) of β‐casein

Beteiligte: BOUHALLAB, S.; SAPIN, B.; MOLLÉ, D.; HENRY, G.; LÉONIL, J.

Erschienen: Wiley, 1997

Sprache: Englisch

DOI: 10.1111/j.1399-3011.1997.tb01117.x

ISSN: 1397-002X

Schlagwörter: Endocrinology ; Biochemistry

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Beschreibung: The sensitivities of the R25‐I26 bond on bovine β‐casein and on its N‐terminal fragment β(1–105) to trypsin digestion were compared by monitoring the liberation of the β(1–25) product. It was shown that this peptide bond was poorly and slowly hydrolysed on β(1–105), while it is highly susceptible to trypsin attack when whole protein is used as substrate. The marked resistance of β(1–105) is linked to its inhibitory effect on trypsin activity (apparent K′i= 1.2 × 10−6, M), as demonstrated by using a related chromogenic substrate. Indeed, a preincubation step of trypsin with β(1–105) leads to a more pronounced inhibitory effect. The progress curves obtained with and without preincubation show that β(1–105) acts as a slow binding inhibitor on trypsin activity. These findings promise further insight into the action and the regulation of proteolytic enzymes. © Munksgaard 1997.

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