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机构地区:[1]上海交通大学农业与生物学院,上海200240 [2]马里兰大学营养与食品科学系,美国马里兰州20742
出 处:《上海交通大学学报(农业科学版)》2016年第4期52-56,共5页Journal of Shanghai Jiaotong University(Agricultural Science)
基 金:国家863计划项目(2013AA102207-6)
摘 要:乳清蛋白经碱性蛋白酶酶解的产物,经超滤、凝胶过滤色谱以及反向高效液相色谱分离纯化得到一种纯度较高的多肽。多肽经液质分析,初步确定其氨基酸序列为Asp-Gln-Trp-Leu,为一种新的肽段。本文采用核磁共振波谱法[包括~1H、^(13)C、~1H-~1H COSY(~1H-~1H correlation spectroscopy),HMBC(heteronuclear multiple bond correlation),HMQC(heteronuclear multiple quantum coherence),TOCSY(total correlation spectroscopy),NOESY(nuclear overhauser effect spectroscopy)]对其结构进行了解析,并对核磁信号进行了归属。实验结果显示TOCSY、HMBC和NOESY技术在多肽核磁共振信号的归属中发挥着关键的作用。A novel whey peptide was purified by uhrafihration, Sephadex G-25 gel filtration chromatography and preparative HPLC from whey protein hydrolytes with alcalase. Its amino acid sequence was determined to be Asp-Gln-Trp-Leu by LC-MS, which is a novel peptide. This study focused on the structural elucidation of this peptide by NMR spectra (1H,13 C,1H-1H COSY (1H-1H correlation Spectroscopy), HMBC(heteronuclear multiple bond correlation), HMQC(heteronuclear multiple quantum coherence), TOCSY (total correlation spectroscopy), NOESY (nuclear overhauser effect spectroscopy)). Our results showed that TOCSY, HMBC and NOESY play an important role in the assignment of NMR data for the structural elucidation of peptides.
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