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Purification and Characterization of Angiotensin I Converting Enzyme Inhibition Peptides from Sandworm Sipunculus nudus

ISSN号：1672-5182
期刊名称：《中国海洋大学学报：英文版》
时间：0
分类：TS201.23[轻工技术与工程—食品科学;轻工技术与工程—食品科学与工程] S986[农业科学—捕捞与储运;农业科学—水产科学]
作者机构：[1]Guangxi Institute of Traditional Medical and Pharmaceutical Science & Guangxi Key Laboratory of Traditional Chinese Medicine Quality Standards, Nanning 530022, P. R. China, [2]Fengxian Hospital Affiliated to Southern Medical University, Shanghai 201499, P R. China, [3]Guangxi Institute of Oceanology, Guangxi Key Laboratory of Marine Biotechnology, Beihai 536000, P R. China
相关基金：This work is supported by research grant of Guangxi Key Laboratory Traditional Chinese Medicine Quality Standards （No. GXGZZK201501） and the Open Research Fund Program of Guangxi Key Laboratory of Marine Biotechnology （No. GLMBT-201407）, and partly supported by Shanghai Fengxian District Science and Technology Project （Nos. 20141001 and 20151205）, Shanghai No. 6 People＇s Medical Group Project and research project of Shanghai municipal health and Family Planning Com- mission （No. 201540027）.

作者： SUN Xueping[1], WANG Man[2], LIU Buming[1], SUN Zhenliang[2,3]

关键词：血管紧张素转换酶抑制肽, 纯化鉴定, 方格星虫, 沙虫, 反相高效液相色谱法, ACE抑制肽, ACE抑制活性, 水解蛋白质, hydrolysis converting purification exclusion Angiotensin Inhibition shrimp isolate purified Enzyme

中文摘要：

三血管收缩素我变换的酶(王牌) 抑制肽从用 protamex 准备的 sandworm Sipunculus nudus 蛋白质 hydrolysate 被孤立。包括尺寸排除层析和反向阶段的高效液体层析(RP-HPLC ) ，连续纯化方法被用来孤立王牌抑制肽。肽的氨基酸序列作为 Ile-Asn-Asp 被识别， Val-Glu-Pro-Gly 并且 Leu-Ala-Asp-Glu-Phe。为王牌抑制活动的净化的肽的 IC ₅₀ 价值是 34.72 摩尔 L ¹, 20.55 摩尔 L ¹ 和 22.77 摩尔 L ¹, 分别地。这些结果建议了那 S。nudus 蛋白质包含能被酶的水解作用释放的特定的肽。这研究可以为进一步系统的研究，合理发展和 sandworm 资源的临床的利用提供一个试验性的基础。

英文摘要：

Three angiotensin I converting enzyme（ACE） inhibition peptides were isolated from sandworm Sipunculus nudus protein hydrolysate prepared using protamex. Consecutive purification methods, including size exclusion chromatography and reverse-phase high performance liquid chromatography（RP-HPLC）, were used to isolate the ACE inhibition peptides. The amino acid sequences of the peptides were identified as Ile-Asn-Asp, Val-Glu-Pro-Gly and Leu-Ala-Asp-Glu-Phe. The IC_（50） values of the purified peptides for ACE inhibition activity were 34.72 μmol L^-1, 20.55 μmol L^-1 and 22.77 μmol L^-1, respectively. These results suggested that S. nudus proteins contain specific peptides that can be released by enzymatic hydrolysis. This study may provide an experimental basis for further systematic research, rational development and clinical utilization of sandworm resources.

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