ISOLATION AND CHARACTERIZATION OF IRON-BINDING PROTEINS FROM RAT INTESTINAL-MUCOSA
ISOLATION AND CHARACTERIZATION OF IRON-BINDING PROTEINS FROM RAT INTESTINAL-MUCOSA
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DOI：
10.1111/j.1432-1033.1976.tb10569.x
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发表时间：
1976-01-01
期刊：
影响因子：
--
通讯作者：
CRICHTON, RR
中科院分区：
文献类型：
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作者：
HUEBERS, H;HUEBERS, E;CRICHTON, RR
从大鼠肠粘膜中分离到两种铁结合蛋白。从测定它们的分子量，它们的电泳和铁结合特性，它被确定为一个是粘膜铁蛋白和其他粘膜转铁蛋白。比较了粘膜铁蛋白的分子量、等电点、氨基酸组成和胰蛋白酶肽谱，并与大鼠脾和肝的铁蛋白进行了比较。所有3种铁蛋白彼此明显不同。此外，粘膜铁蛋白的铁含量远低于肝和脾铁蛋白。通过等电聚焦将粘多糖转铁蛋白分离成2种组分，血浆转铁蛋白也是如此。血浆和粘膜转铁蛋白的等电点和氨基酸组成不同。差异也被发现在体外的粘膜转铁蛋白的铁结合相比，血浆转铁蛋白。这些粘膜蛋白在铁的吸收中的作用进行了简要讨论。
Two Fe-binding proteins were isolated from rat intestinal mucosa. From determination of their molecular weights, their electrophoretic and iron-binding properties it was established that one was a mucosal ferritin and the other a mucosal transferrin. The mucosal ferritin is compared in its molecular weight, isoelectric point, amino acid composition and tryptic peptide pattern with the ferritins of rat spleen and liver. All 3 ferritins are distinctly different from one another. In addition the Fe content of mucosal ferritin was much lower than that of liver and spleen ferritins. Mucosal transferrin was separated into 2 components by isoelectric focusing, as was plasma transferrin. The plasma and mucosal transferrins differ in their isoelectric points and in their amino acid compositions. Differences were also found in vitro in the Fe-binding of mucosal transferrin as compared with plasma transferrin. The role of these mucosal proteins in the absorption of Fe is briefly discussed.