肽
钙化
钙
小龙虾
碳酸钙
化学
克氏原螯虾
生物化学
重组DNA
生物物理学
生物
细胞生物学
内科学
生态学
医学
有机化学
基因
作者
Hirokazu Inoue,Tsuyoshi Ohira,Hiromichi Nagasawa
出处
期刊:Peptides
[Elsevier]
日期:2007-03-01
卷期号:28 (3): 566-573
被引量:23
标识
DOI:10.1016/j.peptides.2006.12.005
摘要
Calcification-associated peptide (CAP)-1 is considered to play an important role in calcification of the exoskeleton of the crayfish, Procambarus clarkii. In this study, in order to clarify the molecular mechanism of calcification, we constructed expression systems of recombinant molecules of CAP-1 and its related peptides in Escherichia coli, and verified the structure–activity relationship of these peptides. The inhibitory assay on calcium carbonate precipitation and the calcium-binding assay showed that the C-terminal acidic region was most important for both activities. The CD spectra of these peptides varied depending on calcium concentration and showed that the N-terminal region is associated with the peptide conformation. These results indicate that the C-terminal part of CAP-1 may concentrate calcium ions for nucleation and/or interact with calcium carbonate precipitate to control the growth and that the N-terminal part contribute to maintaining the peptide conformation.
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