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Nutritional Science Laboratory and * Biochemical Research Laboratory, Morinaga Milk Industry Company, Zama, Kanagawa 228-8583, Japan
2To whom correspondence should be addressed. E-mail: jcb00322{at}nifty.ne.jp.
Pharmaceutical and food-related applications of lactoferrin, an
80-kDa iron-binding glycoprotein found predominantly in milk, have
attracted interest lately, but the process of digestion of lactoferrin
has been poorly characterized. The digestive fate of bovine lactoferrin
in adult rats after oral administration of a single dose and after
dietary supplementation was studied by 125I-labeling and by
surface-enhanced laser desorption/ionization (SELDI) affinity mass
spectrometry. The latter method was designed to detect multiple forms
of degraded lactoferrin as simple molecular ion peaks corresponding to
one of the core regions of lactoferrin, namely, the lactoferricin
region (Phe17-Ala42). Radioactive fragments with molecular masses of
42, 36, 33 and 29 kDa were observed at 20, 60 and 180 min postingestion
in the contents of the lower small intestine. Rats were given free
access to milk enriched with lactoferrin at 482 µmol/L
(40 mg/mL). The concentrations of lactoferrin fragments in the contents
of the stomach, small intestine and lower small intestine as determined
by SELDI affinity mass spectrometry were 
200, 20 and 1
µmol/L, respectively. These data indicate that
functional fragments of LF such as fragments containing
glycosaminoglycan-binding site(s), as well as large fragments with
a mass >20 kDa, indeed survive proteolytic degradation in the small
intestine of adult rats.
KEY WORDS: • lactoferrin • lactoferricin • digestion • SELDI affinity mass spectrometry • rats
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