Isolation and characterization of a 21 kDa whey protein in Rhesus monkey (Macaca mulatta) milk

Clemens Kunz , Bo Lönnerdal
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引用次数: 11

Abstract

A soluble protein in Rhesus monkey milk was isolated to apparent homogeneity by FPLC gel filtration, anion-exchange and reverse-phase chromatography. It is a major milk protein and is present at 2.5—3.0 mg/ml milk throughout lactation. It is only found in the whey fraction of milk; acid precipitation of casein does not result in any significant change in its concentration. A molecular weight (MW) of about 21.6 kDa was estimated from gel filtration and SDS gel electrophoresis and also calculated from its amino acid composition. The amino acid composition of this protein is similar to that of bovine β-lactoglobulin (β-Lg), but it is larger in size, possibly representing a family of primate β-Lgs.

恒河猴(Macaca mulatta)牛奶中21 kDa乳清蛋白的分离与鉴定
采用FPLC凝胶过滤、阴离子交换和反相色谱法,从恒河猴乳中分离出一种具有明显均匀性的可溶性蛋白。它是一种主要的牛奶蛋白,在哺乳期每毫升牛奶中含有2.5-3.0毫克。它只存在于牛奶的乳清部分;酪蛋白的酸沉淀不会导致其浓度的显著变化。通过凝胶过滤和SDS凝胶电泳,以及氨基酸组成,估计其分子量约为21.6 kDa。该蛋白的氨基酸组成与牛β-乳球蛋白(β-Lg)相似,但它的大小更大,可能代表灵长类动物β-Lgs家族。
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