摘要
目的：从药用露峰房（Ｎｉｄｕｓｖｅｓｐａｅ）筛选出的具有较好的抗炎、免疫活性蛋白粗品———ＮＶ３中分离纯化，得到一多肽类化合物，命名为ＮＶＰＰ１，并检测其理化性质。方法：以离子交换层析、排阻层析、ＨＰＬＣ等进行分离纯化，并以高效凝胶排阻色谱（ＨＰＳＥＣ）、高效毛细管等电聚焦电泳（ＩＥＦＨＰＣＥ）、亲水性分子排阻液相ＰｒｏｔｅｉｎＰａｋＴＭ６０柱、氨基酸分析、ＤＮＳＣｌ法的Ｎ末端测定检测其理化性质。结果：高效凝胶排阻色谱（ＨＰＳＥＣ）及高效毛细管等电聚焦电泳（ＩＥＦＨＰＣＥ）检测其皆为单峰。亲水性分子排阻液相ＰｒｏｔｅｉｎＰａｋＴＭ６０柱测得其分子量为７．０７９ｋＤ。ＩＥＦＨＰＣＥ确定其ＰＩ值为４．０８。紫外吸收最高峰为２７４ｎｍ。氨基酸分析表明其含有近５６个氨基酸残基，其中谷氨酸、丝氨酸、甘氨酸较多，还有天冬氨酸等，是一酸性多肽。末端测定表明其Ｎ末端封闭。结论：酸性多肽ＮＶＰＰ１是从药用露蜂房抗炎蛋白粗品中首次分离得到的成分。
OBJECTIVES:To isolate and purify a new peptide named as NV PP 1,from anti inflammatory protein extracts of Nidus Vespae and to characterize it.METHODS:It was purified by ammonium sulfate precipitation,DEAE Sephadex A50 ionexchange chromatography,Sephadex G-50 gel filtration and HPLC,respectively.Then it was characterized by HPLC on Protein Pak TM 60 column,IEF HPCE(isoelectric focusing high performance capillary electrophoresis),UV spectrum,amino acid analysis,and the N terminal analysis with DNS Cl.RESULT:Both HPLC on Protein Pak TM 60 column and IEF HPCE showed its homogeneity.Its molecular weight was estimated to be 7.079 kD by HPSEC.UV spectrum indicated its maximum absorption at 274nm.Its PI was determined to be 4.08 according to IEF HPCE.The terminal analysis showed its N terminal amino acid was blocked.Amino acid analysis of NV PP 1 indicated that it was rich in Ser,Glu,Gly.CONCLUSION:NV PP 1 is the first peptide isolated from the anti inflammatory protein extracts of Nidus vespae.
出处
《中国药学杂志》
CAS
CSCD
北大核心
1999年第4期233-236,共4页
Chinese Pharmaceutical Journal
