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dc.contributor.authorYan Liu
dc.contributor.authorPeng-xiang Xu
dc.contributor.authorJian-bo Hou
dc.contributor.authorLi-feng Yang
dc.contributor.authorJin-an Chen
dc.contributor.authorYu-fen Zhao
dc.contributor.author赵玉芬
dc.date.accessioned2011-11-13T11:08:10Z
dc.date.available2011-11-13T11:08:10Z
dc.date.issued2005
dc.identifier.citationINTERNATIONAL JOURNAL OF PEPTIDE RESEARCH AND THERAPEUTICS,2005,11(2):167-175zh_CN
dc.identifier.issn1573-3149
dc.identifier.urihttp://dx.doi.org/doi: 10.1007/s10989-005-4711-1
dc.identifier.urihttps://dspace.xmu.edu.cn/handle/2288/11172
dc.description.abstractIn this paper, the reactions of bovine insulin and small peptides, such as actin binding domain of thymosin (34 and Growth Hormone Releasing Factor (GRF 1-29 amino acids) with diisopropyloxyphosphite (DIPPH) and dimethyloxyphosphite (DMPH) were studied by modified Todd reaction. The MALDI-TOF or ESI-MS results showed that lysine, histidine and arginine residues in insulin could be phosphorylated under the water/ethanol system. The N,N,N-diisopropyloxyphosphorylated insulin analogues were characterized using MALDI-TOF and P-31 NMR. These insulin analogues with different phosphorylation degree were separated and identified through LC-ESI-MS. In addition, circular dichroism (CD) spectra showed that the conformation of N,N,N-dimethyloxyphosphorylated insulin were only changed a little, whereas, that of N,N,N-diisopropyloxyphosphorylated insulin was changed completely.zh_CN
dc.language.isoenzh_CN
dc.publisherSPRINGERzh_CN
dc.subjectbovine insulinzh_CN
dc.subjectCDzh_CN
dc.subjectESI-MSzh_CN
dc.subjectHPLCzh_CN
dc.subjectMALDI-TOFzh_CN
dc.subjectphosphorylationzh_CN
dc.titleChemical modification of insulin by N-phosphorylationzh_CN
dc.typeArticlezh_CN


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