Wakabayashi Hiroyuki, Kuwata Hidefumi, Yamauchi Koji, Teraguchi Susumu, Tamura Yoshitaka
Nutritional Science Laboratory, Morinaga Milk Industry Co., Ltd., Zama, Kanagawa, Japan.
Biosci Biotechnol Biochem. 2004 Apr;68(4):853-60. doi: 10.1271/bbb.68.853.
We investigated the transfer of dietary bovine lactoferrin (LF) and its functional lactoferricin (LFcin) B-containing fragments to the portal blood of healthy adult rats by using several techniques. After a single administration of (125)I-labeled LF, radioactive bands were detected in autoradioluminograms of the portal blood, but similar bands were also observed after the administration of [(125)I]NaI. Although ovalbumin was detected by ELISA at 3-18 ng/ml in the portal blood plasma after an overnight administration, no LF was detected (< or =1.5 ng/ml). The antibody-captured ovalbumin fragments, but not the LF fragments, were detected in the plasma by surface-enhanced laser desorption/ionization affinity mass spectrometry (SELDI affinity MS). We finally attempted to detect the LFcin B-containing fragments by SELDI affinity MS with on-chip LFcin B-conversion, but could not detect them (< or =1 ng/ml) in the portal blood after the LF ingestion. The level of LF or its functional fragments transferred to the portal blood was therefore extremely low, if any.
我们运用多种技术研究了膳食来源的牛乳铁蛋白(LF)及其含功能性乳铁蛋白B(LFcin B)的片段向健康成年大鼠门静脉血中的转移情况。单次给予(125)I标记的LF后,在门静脉血的放射自显影片中检测到放射性条带,但给予[(125)I]NaI后也观察到类似条带。过夜给予后,通过ELISA在门静脉血浆中检测到卵清蛋白浓度为3 - 18 ng/ml,但未检测到LF(≤1.5 ng/ml)。通过表面增强激光解吸/电离亲和质谱(SELDI亲和质谱)在血浆中检测到抗体捕获的卵清蛋白片段,而非LF片段。我们最终尝试通过具有芯片上LFcin B转化功能的SELDI亲和质谱来检测含LFcin B的片段,但在摄入LF后,在门静脉血中未检测到它们(≤1 ng/ml)。因此,转移至门静脉血中的LF或其功能性片段的水平极低,即便存在的话。