Functional Fragments of Ingested Lactoferrin Are Resistant to Proteolytic Degradation in the Gastrointestinal Tract of Adult Rats

摘要: Pharmaceutical and food-related applications of lactoferrin, an 80-kDa iron-binding glycoprotein found predominantly in milk, have attracted interest lately, but the process digestion lactoferrin has been poorly characterized. The digestive fate bovine adult rats after oral administration a single dose dietary supplementation was studied by (125)I-labeling surface-enhanced laser desorption/ionization (SELDI) affinity mass spectrometry. latter method designed to detect multiple forms degraded as simple molecular ion peaks corresponding one core regions namely, lactoferricin region (Phe17-Ala42). Radioactive fragments with masses 42, 36, 33 29 kDa were observed at 20, 60 180 min postingestion contents lower small intestine. Rats given free access milk enriched 482 micromol/L (40 mg/mL). concentrations stomach, intestine determined SELDI spectrometry approximately 200, 20 1 micromol/L, respectively. These data indicate that functional LF such containing glycosaminoglycan-binding site(s), well large >20 kDa, indeed survive proteolytic degradation rats.