Grandier-Vazeille X, Tetaert D
J Chromatogr. 1984 Jul 27;296:301-8. doi: 10.1016/s0021-9673(01)96424-6.
To aid in structural studies of pig cardiac myosin light chains (L27 and L28), a procedure of ion-exchange chromatography (IEC) on Trisacryl M (noted for its high capacity) in combination with reversed-phase high-performance liquid chromatography (RP-HPLC) and volatile buffers has been developed. In contrast with other IEC methods (resins or HPIEC), the use of Trisacryl M facilitates subsequent peptide purifications by RP-HPLC. The advantage of the present combination of techniques is also that it enables the isolation of hydrophobic peptides in high yield, e.g., the N-terminal chymotryptic peptide from L27 was thus purified and, after sub-digestion with trypsin, its sequence has been established.
为了辅助猪心肌肌球蛋白轻链（L27和L28）的结构研究，已开发出一种在Trisacryl M（以其高容量著称）上进行离子交换色谱（IEC）并结合反相高效液相色谱（RP-HPLC）和挥发性缓冲液的方法。与其他IEC方法（树脂或高效离子交换色谱）相比，使用Trisacryl M便于后续通过RP-HPLC进行肽段纯化。本技术组合的优势还在于它能够高收率地分离疏水性肽段，例如，L27的N端胰凝乳蛋白酶肽段就是这样被纯化出来的，在用胰蛋白酶进行亚消化后，其序列已被确定。
