狗小肠新生物活性肽的分离纯化及结构测定

研究了一种新的胃肠肽的分离纯化及其部分氨基酸序列测定．沸水处理后的狗小肠经醋酸提取、海藻酸吸附、盐酸洗脱、氯化钠盐析和乙醇沉淀，再经Sephadex G-25（fine）层析和两次RP-HPLC分离，从中纯化出一个热稳定多肽．用Tris-Tricine-SDS-PAGE鉴定其相对分子质量约为4 kD．该肽经胰酶水解，产物片断经RP-HPLC分离后，取其中之一主峰经CapLC-ESI-MS-MS（Q-TOF2）质谱仪测定氨基酸顺序为：T-E-Y-T-A-L-N-V-L-A-T-T-E-E-N-G．蛋白质数据库（Gen Bank和SWISS-PROT）查寻证明：此肽为首次发现的新多肽，正在进一步研究其生物学功能．

Isolation, purification and sequencing of a novel bioactive peptide from canine intestine

A novel bioactive peptide was purified from dog small intestine and part of its amino acid sequence has ben analyzed. With the boiling of the intestine tissue, acetic acid extraction, alginic acid adsorption, hydrochloric acid elution, sodium chloride salting out and the ethanol precipitation, followed by Sephadex G-25 (fine) column chromatography and a two-step reverse-phase HPLC purification, a thermo-stable peptide has been purified and its molecular size was determined about 4?kD by using the Tris-Tricine-SDS-PAGE. After the digestion of the peptide with trypsin and the separation of the trypsin-peptide, one of the fragments subjected to sequence with CapLC-ESI-MS-MS (Q-TOF2) and a clear amino acid sequence was obtained as following: T-E-Y-T-A-L-N-V-L-A-T-T-E-E-N-G. By searching the sequence from Gene Bank and SWISS-PORT, it has been found that the peptide is a novel peptide. The physiology function of the peptide deserves to be further investigated.