Apisimin, a new serine-valine-rich peptide from honeybee (Apis mellifera L.) royal jelly:: purification and molecular characterization
Apisimin, a new serine-valine-rich peptide from honeybee (Apis mellifera L.) royal jelly:: purification and molecular characterization
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DOI：
10.1016/s0014-5793(02)03272-6
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发表时间：
2002-09-25
期刊：
影响因子：
3.5
通讯作者：
Simúth, J
中科院分区：
文献类型：
--
作者：
Bíliková, K;Hanes, J;Simúth, J
在蜜蜂（Apis mellifera L.）蜂王浆（RJ）中发现了一种名为apisimin的肽。n端测序结果表明，该肽段与从护理蜂头部cDNA表达文库中分离的cDNA克隆序列一致。分子质量为5540.4 Da的apisimin蛋白序列与Swiss-Prot数据库中保存的序列无同源性。apisimin的54个氨基酸不包括Cys、Met、Pro、Arg、His、Tyr和Trp残基。经CD谱分析，该肽具有明确的二级结构，并有形成低聚物的倾向。等电聚焦表明apisimin是一种酸性肽。(C) 2002年欧洲生化学会联合会。Elsevier Science B.V.版权所有。
A peptide named apisimin was found in honeybee (Apis mellifera L.) royal jelly (RJ). N-terminal sequencing showed that this peptide corresponded to the sequence of a cDNA clone isolated from an expression cDNA library prepared from heads of nurse honeybees. No homology was found between the protein sequence of apisimin with a molecular mass of 5540.4 Da and sequences deposited in the Swiss-Prot database. The 54 amino acids of apisimin do not include Cys, Met, Pro, Arg, His, Tyr, and Trp residues. The peptide shows a well-defined secondary structure as observed by CD spectroscopy, and has the tendency to form oligomers. Isoelectrofocusing showed apisimin to be an acidic peptide. (C) 2002 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.