Levy L M, Lehre K P, Rolstad B, Danbolt N C
Anatomical Institute, University of Oslo, Norway.
FEBS Lett. 1993 Feb 8;317(1-2):79-84. doi: 10.1016/0014-5793(93)81495-l.
A monoclonal antibody (9C4) shows that an [Na(+)+K+]coupled glutamate transporter protein purified from rat brain runs electrophoretically as a wide band and is localized in neuroglial cell bodies and processes, but not in neurons. This confirms the findings with polyclonal antibodies [Neuroscience 51 (1992) 295-310], and shows that the apparent heterogeneity in relative molecular mass is accounted for by a single antigenic epitope. By testing several synthetic peptides derived from the deduced amino acid sequences of two cloned rat brain glutamate transporters, the antigenic epitope was identified as residing within the peptide TQSVYDDTKNHRESNSNQC (residues 518-536) of one of these [Nature 360 (1992) 464-467].
一种单克隆抗体（9C4）显示，从大鼠脑内纯化出的一种[Na⁺+K⁺]偶联型谷氨酸转运蛋白在电泳时呈宽带状，定位于神经胶质细胞体和突起中，而不在神经元中。这证实了用多克隆抗体得出的研究结果[《神经科学》51（1992）295 - 310]，并表明相对分子质量的明显异质性是由单一抗原表位引起的。通过测试从两个克隆的大鼠脑谷氨酸转运蛋白推导的氨基酸序列衍生出的几种合成肽，抗原表位被确定位于其中一种转运蛋白的肽TQSVYDDTKNHRESNSNQC（第518 - 536位氨基酸残基）内[《自然》360（1992）464 - 467]。
