Coleman M P, Anderton B H
Department of Cellular and Molecular Science, St. George's Hospital Medical School, London, England.
J Neurochem. 1990 May;54(5):1548-55. doi: 10.1111/j.1471-4159.1990.tb01203.x.
Five phosphate-dependent monoclonal antibodies to the neurofilament heavy polypeptide bound strongly to a phosphorylated synthetic peptide, which contains a single Lys-Ser-Pro sequence that occurs in human neurofilaments. Three of the antibodies label Alzheimer's disease neurofibrillary tangles and two do not, suggesting that in tangles an epitope similar to the peptide is available to some but not all of the antibodies. In addition, some antibodies were found to be more affected than others by enzymatic dephosphorylation of the antigen, but because all the antibodies bound the same synthetic phosphopeptide they do not bind to mutually exclusive phosphorylation sites. Instead the more phosphate-dependent antibodies might bind the phosphate group more directly, as suggested by their inhibition by inorganic phosphate and free phosphoserine.
五种针对神经丝重多肽的磷酸依赖性单克隆抗体与一种磷酸化合成肽紧密结合，该合成肽含有一个存在于人类神经丝中的单一赖氨酸 - 丝氨酸 - 脯氨酸序列。其中三种抗体标记阿尔茨海默病神经原纤维缠结，另外两种则不标记，这表明在缠结中，一些但不是所有抗体都能识别与该肽相似的表位。此外，发现一些抗体比其他抗体受抗原酶促去磷酸化的影响更大，但由于所有抗体都结合相同的合成磷酸肽，它们并非结合相互排斥的磷酸化位点。相反，如无机磷酸盐和游离磷酸丝氨酸对其的抑制作用所示，磷酸依赖性更强的抗体可能更直接地结合磷酸基团。
