Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1255158 | Chinese Chemical Letters | 2012 | 4 Pages |
Abstract
A novel peptide designated secapin-1, was purified and characterized from Apis mellifera. The molecular weight of 25 amino acid peptide secapin-1 was found to be 2821.5625 Da by ESI-FTICR-MS. It showed high identity to secapin. The sequence of secapin-1 was determined to be YIINVPPRCPPGSKFVKNKCRVIVP by automatic Edman degradation. A disulfide bond was formed between Cys9 and Cys20 residues. In addition, an analogue of secapin-1 was synthesized by solid phase peptide synthesis method. The synthesis product was successfully purified and identified to homogeneity by using a combination of SEC, IEC, and RP-HPLC techniques.
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Physical Sciences and Engineering
Chemistry
Chemistry (General)
Authors
Yu Meng, Xiao Xiao Yang, Yu Xin Sheng, Jin Lan Zhang, De Quan Yu,