Strömqvist M, Lindgren K, Hansson L, Juneblad K
ASTRA HASSLE AB, Umeå, Sweden.
J Chromatogr A. 1995 Dec 1;718(1):53-8. doi: 10.1016/0021-9673(95)00632-x.
The milk of some mammals contains a bile salt-stimulated lipase (BSSL). Human milk BSSL is heavily glycosylated (30-40% carbohydrate) and present at a concentration of approximately 100-200 mg/l, thereby being one of the most abundant human whey proteins. BSSL has been shown to have an important role in the uptake of energy from human milk. The risk of HIV contamination has restricted the use of banked human milk for nutritional purposes. This has evoked an interest in the production of a recombinant form of the protein for supplementation of formula. We have produced BSSL in mouse C127 and hamster CHO cells, and used chromatographic methods for the characterization of the products. This study was focused on study of the glycosylation of the protein by using peptide mapping and isolation of glycosylated fragments. The results show how human BSSLs from different sources differ both in extent of glycosylation, in glycan heterogeneity, and in lectin binding.
一些哺乳动物的乳汁中含有一种胆汁盐刺激脂肪酶（BSSL）。人乳中的BSSL高度糖基化（碳水化合物含量为30%-40%），其浓度约为100-200毫克/升，因此是最丰富的人乳清蛋白之一。研究表明，BSSL在从人乳中摄取能量方面起着重要作用。由于存在HIV污染风险，用于营养目的的储存人乳的使用受到了限制。这引发了人们对生产重组形式的该蛋白质以补充配方奶粉的兴趣。我们已在小鼠C127细胞和仓鼠CHO细胞中生产了BSSL，并使用色谱方法对产物进行表征。本研究重点通过肽图分析和糖基化片段分离来研究该蛋白质的糖基化。结果显示了来自不同来源的人BSSL在糖基化程度、聚糖异质性和凝集素结合方面的差异。
