Palmert M R, Podlisny M B, Witker D S, Oltersdorf T, Younkin L H, Selkoe D J, Younkin S G
Department of Pharmacology, Case Western Reserve University School of Medicine, Cleveland, OH 44106.
Proc Natl Acad Sci U S A. 1989 Aug;86(16):6338-42. doi: 10.1073/pnas.86.16.6338.
In this study, we use antisera to synthetic beta-amyloid protein precursor (beta APP) peptides to identify, in human brain and cerebrospinal fluid (CSF), soluble approximately 125- and approximately 105-kDa derivatives of the beta APP that lack the carboxyl terminus of the full-length, membrane-associated forms. We show that the soluble approximately 125-kDa beta APP derivative contains the Kunitz protease inhibitor domain, whereas the approximately 105-kDa form does not, and we confirm that these two proteins are soluble beta APP derivatives by purifying each from human CSF and directly sequencing its amino terminus.
在本研究中，我们使用针对合成β-淀粉样蛋白前体（βAPP）肽段的抗血清，在人脑和脑脊液（CSF）中鉴定出βAPP的可溶性衍生物，其分子量约为125 kDa和105 kDa，缺乏全长膜相关形式的羧基末端。我们发现，可溶性约125 kDa的βAPP衍生物含有Kunitz蛋白酶抑制剂结构域，而约105 kDa的形式则没有，并且我们通过从人CSF中纯化每种蛋白质并直接对其氨基末端进行测序，证实这两种蛋白质是可溶性βAPP衍生物。
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