Canioni P, Julien R, Rathelot J, Rochat H, Sarda L
Biochimie. 1977;59(11-12):919-25. doi: 10.1016/s0300-9084(78)80707-x.
Colipase was isolated from porcine pancreas homogenate prepared in the presence of detergent (Triton X 100). After precipitation by ammonium sulfate and ethanol, the cofactor was purified by chromatography on SP-Sephadex in the presence of Triton X 100 and on DEAE-cellulose in the absence of detergent. Two molecular forms of porcine colipase were obtained. They represent 80 per cent (colipase A) and 20 per cent (colipase B), respectively, of the total colipase. Valine is the N-terminal residue of both proteins. Their aminoacid composition is similar to that found by Borgstrom for the two forms of porcine colipase. Determination of the sequence of the first sixteen residues at the N-terminal end of colipase A indicates that the cofactor undergoes no proteolytic degradation in this region of the molecule when extraction is carried out in the presence of detergent. The recovery of colipase is about 30 per cent.
在存在去污剂（Triton X 100）的情况下制备猪胰腺匀浆，从中分离出辅脂酶。经硫酸铵和乙醇沉淀后，在存在Triton X 100的条件下通过SP - 葡聚糖凝胶色谱法以及在不存在去污剂的条件下通过DEAE - 纤维素色谱法对该辅因子进行纯化。获得了猪辅脂酶的两种分子形式。它们分别占总辅脂酶的80%（辅脂酶A）和20%（辅脂酶B）。缬氨酸是这两种蛋白质的N端残基。它们的氨基酸组成与Borgstrom发现的猪辅脂酶的两种形式相似。对辅脂酶A的N端前16个残基序列的测定表明，当在去污剂存在的情况下进行提取时，该辅因子在分子的这一区域未发生蛋白水解降解。辅脂酶的回收率约为30%。
