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Chemical modification of insulin by N-phosphorylation
Liu, Y ; Xu, PX ; Hou, JB ; Yang, LF ; Chen, JA ; Zhao, YF
2010-05-06 ; 2010-05-06
关键词bovine insulin CD ESI-MS HPLC MALDI-TOF phosphorylation DERIVATIVES PEPTIDES PRODRUGS Biochemistry & Molecular Biology
中文摘要In 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.
语种英语 ; 英语
出版者SPRINGER ; NEW YORK ; 233 SPRING STREET, NEW YORK, NY 10013 USA
内容类型期刊论文
源URL[http://hdl.handle.net/123456789/13513]  
专题清华大学
推荐引用方式
GB/T 7714
Liu, Y,Xu, PX,Hou, JB,et al. Chemical modification of insulin by N-phosphorylation[J],2010, 2010.
APA Liu, Y,Xu, PX,Hou, JB,Yang, LF,Chen, JA,&Zhao, YF.(2010).Chemical modification of insulin by N-phosphorylation..
MLA Liu, Y,et al."Chemical modification of insulin by N-phosphorylation".(2010).
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