Hogue-Angeletti R A, Sheetz P B
J Biol Chem. 1978 Aug 25;253(16):5613-6.
A unique soluble lipoprotein has been isolated from aqueous lysates of bovine adrenal medulla chromaffin granules by DEAE-cellulose chromatography and gel filtration. Chloroform/methanol extracts of this complex contain sphingomyelin, lecithin, and cholesterol. Gel filtration in aqueous media indicate an approximate molecular weight of 900,000 for the complex. Incubation with sodium dodecyl sulfate causes dissociation to a low molecular weight polypeptide; prolonged treatment with guanidine HCl does not promote dissociation at all. Amino acid analysis revealed a high content of hydrophobic amino acids. Analysis of the tryptic fingerprint indicates that a single type of polypeptide chain is present. The complex appears to contain approximately five copies of polypeptide per aggregate.
通过DEAE-纤维素色谱法和凝胶过滤,从牛肾上腺髓质嗜铬颗粒的水性裂解物中分离出一种独特的可溶性脂蛋白。该复合物的氯仿/甲醇提取物含有鞘磷脂、卵磷脂和胆固醇。在水性介质中的凝胶过滤表明该复合物的分子量约为900,000。与十二烷基硫酸钠孵育会导致解离为低分子量多肽;用盐酸胍长时间处理根本不会促进解离。氨基酸分析显示疏水氨基酸含量很高。胰蛋白酶指纹图谱分析表明存在单一类型的多肽链。该复合物似乎每个聚集体含有大约五个多肽拷贝。