Yoo S H, Kang Y K
Laboratory of Neurochemistry, NIDCD, National Institutes of Health, Bethesda, MD 20892-3320, USA.
FEBS Lett. 1997 Apr 14;406(3):259-62. doi: 10.1016/s0014-5793(97)00276-7.
In the past a synthetic peptide representing the conserved near N-terminal region of chromogranin B (CGB) (residues 17-36) has been shown to interact with the vesicle membrane. Hence, it was necessary to confirm this observation with CGB deletion proteins. In order to address this need and to confirm the published sequence of CGB, we cloned a CGB gene and produced various CGB deletion proteins. The recombinant CGB protein lacking the first 15 (rCGB 16-626) or 16 amino acid residues (rCGB 17-626) bound to the vesicle membrane as well as the full-length CGB. However, rCGB 49-626, lacking the conserved near N-terminal region, failed to interact with the vesicle membrane, indicating an anchor role for the conserved near the N-terminal region.
过去已证明，一种代表嗜铬粒蛋白B（CGB）保守近N端区域（第17 - 36位氨基酸残基）的合成肽可与囊泡膜相互作用。因此，有必要用CGB缺失蛋白来证实这一观察结果。为满足这一需求并确认已发表的CGB序列，我们克隆了CGB基因并制备了各种CGB缺失蛋白。缺失前15个（rCGB 16 - 626）或16个氨基酸残基（rCGB 17 - 626）的重组CGB蛋白与全长CGB一样，都能与囊泡膜结合。然而，缺少保守近N端区域的rCGB 49 - 626未能与囊泡膜相互作用，这表明N端附近的保守区域具有锚定作用。
