摘要
目的从牡蛎蛋白质的酶解产物中分离制备具有活性的多肽并对其结构进行研究。方法采用胰蛋白酶对牡蛎蛋白质进行酶解,使其释放出具备特殊活性的肽,将含有活性肽的粗提物分别用Sephadex G25凝胶柱层析,DEAE-Sepharose FF离子交换柱层析和C18反相柱进行分离和纯化。结果牡蛎酶解产物经过分离纯化制备得到纯度较高的多肽F32,红外光谱的测定表明该肽的肽链是以α-螺旋的构型存在。电喷雾串联质谱法分析多肽F32完整的氨基酸序列为:Arg-Gln-Ile或Leu-Gly-Ala-Thr-Asn-Ala。结论本研究将为牡蛎酶解多肽F32构效关系的研究提供基础。
Objective To study the preparation and the structure identification of peptides from hydrolyzates of oyster. Methods The oyster protein was hydrolyzed with trypsin. The hydrolysates were purified using Sephadex G25 gel chromatography, DEAE-Sepharose FF ion exchange chromatography, reversed-phase HPLC on C18 column. Results The peptide F32 was finally isolated from the oyster hydrolysates . The oyster protein was hydrolyzed with trypsin. IR spectrum showed the conformation of peptide chain was α-helix, the amino acid sequence of F32 was determined by ESI-MS/MS. The sequence of F32 was as follows. Arg- Gln-Ile or Leu-Gly-Ala-Thr-Asn-Ala. Conclusion The research result would provide foundation for the structure-activity research of the peptide F32.
出处
《中国海洋药物》
CAS
CSCD
2009年第2期1-5,共5页
Chinese Journal of Marine Drugs
基金
山东省科技攻关计划资助项目(No.021100102)
