Some Properties of Secretory IgA Purified from Bovine Colostrum
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概要
- 論文の詳細を見る
The major component of a purified sample of secretory IgA (SIgA) in colostrum was revealed as a single peak on gel filtration with Sepharose 6B, having an estimated molecular weight of 540, 000. The existence of a higher molecular weight component was suggested by a small shoulder on the ascending limb of the peak, but another component of IgA reported as IgA lacking the secretory component (SC) could not be found. When the purified SIgA was concentrated by dialysis against polyethylene glycol, its molecular size was apparently significantly decreased. Analysis by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate (SDS-PAGE) showed that all SC in SIgA binds covalently. The band corresponding to the J chain was easily detected when a reduced and alkylated sample was analysed. Estimation of the molecular weight by SDS-PAGE gave the following values for each of the constituent polypeptide chains of bovine colostral SIgA: SC, 76, 000; H chain, 62, 000; L chain, 23, 000; and J chain, 18, 000. The molecular weight of the whole molecule was calculated to be 434, 000. Analysis of carbohydrates by gas-liquid chromatography showed 6.8% neutral and amino hexoses, consisting of 0.4% fucose, 1.8% mannose, 1.1% galactose and 3.5% glucosamine. Galactosamine, which has been found in bovine free secretory component from milk, could not be detected.
- 社団法人 日本農芸化学会の論文
著者
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Kuzuya Yasuo
Department Of Food Science Faculty Of Agriculture Gifu University
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Kanamaru Yoshihiro
Department Of Applied Life Science Faculty Of Applied Biological Sciences Gifu University
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Tanahashi Tamotsu
Department of Cardiology, Suzuka National Hospital, Japan
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