Berchtold M W, Wilson K J, Heizmann C W
Biochemistry. 1982 Dec 7;21(25):6552-7. doi: 10.1021/bi00268a035.
Neuronal parvalbumin has been isolated from rat brain and purified to homogeneity by high-performance liquid chromatography (HPLC) on reverse-phase supports. This procedure includes four consecutive chromatographic steps with an overall protein recovery of 74% and a 26 400-fold purification. The concentration of parvalbumin was found to be approximately 10 mg/kg wet weight in brain tissue, which is about 100 times lower than that in rat muscle. The physical properties of brain parvalbumin are described and compared with those of the muscle counterpart. These proteins were identical in their molecular weights (12 000), isoelectric points (4.9), retention times on C-18 reverse-phase HPLC columns, Ca2+ content (two per molecule), amino acid compositions, and immunological properties. A comparison of the tryptic peptide maps of brain and muscle parvalbumin by analytical HPLC also revealed identity and showed that the isolation method described here did not alter the chemical structure of the protein.
已从大鼠脑中分离出神经元小白蛋白，并通过反相支持物上的高效液相色谱（HPLC）将其纯化至同质。该过程包括四个连续的色谱步骤，总蛋白回收率为74%，纯化倍数为26400倍。发现脑组织中小白蛋白的浓度约为10mg/kg湿重，比大鼠肌肉中的浓度低约100倍。描述了脑小白蛋白的物理性质，并与肌肉中的对应物进行了比较。这些蛋白质在分子量（12000）、等电点（4.9）、在C-18反相HPLC柱上的保留时间、Ca2+含量（每个分子两个）、氨基酸组成和免疫特性方面均相同。通过分析HPLC对脑和肌肉小白蛋白的胰蛋白酶肽图进行比较，也显示出一致性，并表明此处描述的分离方法未改变蛋白质的化学结构。
