Lowenstein H
Int J Pept Protein Res. 1975;7(1):1-9.
Human ceruloplasmin from fresh serum has been purified by chromatography on hydroxyapatite and Con A-Sepharose. Quantitative immunoelectrophoretic analysis of fresh serum, stored serum and fractions from the different purification steps for human ceruloplasmin has been carried out. A combination of the latter, advanced technique with amino acid analysis, molecular weight determination by size chromatography, urea treatment, staining for oxidase activity and enzymatic proteolysis, has revealed that: 1) human cerulplasmin is a heterogeneous mixture of two glycoproteins (x) differing only in their carbohydrate content and 2) the protein part contains at least one very labile peptide bond which upon enzymatic hydrolysis gives rise to peptides with molecular weights of 93,000 (y) and 24,000 (z) dalton, respectively. The two glycoproteins are immunochemically identical. The y peptide is immunochemically partially identical, and the z peptide immunochemically non-identical, with the parent molecule. The y and z peptides are non-identical. On the basis of these observations a simplified two-dimensional model of human ceruloplasmin is proposed.
通过羟基磷灰石和伴刀豆球蛋白A - 琼脂糖柱层析法，已从新鲜血清中纯化出人类铜蓝蛋白。对新鲜血清、储存血清以及人类铜蓝蛋白不同纯化步骤的组分进行了定量免疫电泳分析。将后一种先进技术与氨基酸分析、尺寸排阻色谱法测定分子量、尿素处理、氧化酶活性染色以及酶促蛋白水解相结合，结果表明：1）人类铜蓝蛋白是两种糖蛋白（x）的异质混合物，仅在碳水化合物含量上有所不同；2）蛋白质部分含有至少一个非常不稳定的肽键，酶促水解后分别产生分子量为93,000（y）和24,000（z）道尔顿的肽段。这两种糖蛋白在免疫化学上是相同的。y肽段与母体分子在免疫化学上部分相同，z肽段与母体分子在免疫化学上不相同。y肽段和z肽段不相同。基于这些观察结果，提出了一个简化的人类铜蓝蛋白二维模型。
