Partial characterization of amyloid proteins in inherited amyloidosis with lattice corneal dystrophy and in secondary amyloidosis.
Partial characterization of amyloid proteins in inherited amyloidosis with lattice corneal dystrophy and in secondary amyloidosis.
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遗传性淀粉样变性伴格子状角膜营养不良和继发性淀粉样变性中淀粉样蛋白的部分特征。
DOI：
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发表时间：
1978
期刊：
影响因子：
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通讯作者：
R. Penttinen
中科院分区：
文献类型：
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作者：
J. Meretoja;T. Hollmén;T. Meretoja;R. Penttinen
本文采用免疫、电泳和色谱技术对2例遗传性系统性淀粉样变性和晶格型角膜营养不良患者和慢性肾小球肾炎继发性淀粉样变性患者分离的淀粉样原纤维进行了研究。两种淀粉样蛋白的氨基酸水解产物均含有较高比例的酸性和脂肪氨基酸残基，但总体氨基酸组成不相同。这些制剂还含有12- 16%的脂质。两种类型的盐酸胍变性淀粉样蛋白原纤维在Sepharose 6B层析中被分解为4个组分，分子量分别为160 000、45 000、20 000和8 000。在遗传淀粉样蛋白的色谱中，16 000 mol. wt的部分占主导地位，在十二烷基硫酸钠（SDS）聚丙烯酰胺凝胶电泳中，进一步分解为17 000 mol. wt和15 000 mol. wt的两个主要部分。这些来自遗传淀粉样蛋白的部分与组织源性淀粉样蛋白A （AA）的免疫特性均不一致，而来自继发性淀粉样蛋白的四个部分均与抗AA抗血清发生反应。次级淀粉样蛋白原纤维的三个主要Sepharose 6B组分在不含尿素的sds -聚丙烯酰胺凝胶电泳中溶解为25 000 mol. wt.的组分，而在含8M尿素的凝胶中溶解为12 000 mol. wt.的组分。
Amyloid fibrils isolated from two patients, one with inherited systemic amyloidosis and lattice corneal dystrophy, and the other with secondary amyloidosis due to chronic glomerulonephritis, were studied using immunologic, electrophoretic and chromatographic techniques. Amino acid hydrolysates of both amyloid types showed a high proportion of acidic and aliphatic amino acid residues but were non-identical in the overall amino acid composition. The preparations also contained 12--16% lipids. Guanidine hydrochloride denaturated amyloid fibrils of both types were resolved into four fractions in Sepharose 6B chromatography with molecular weights of ca. 160 000, 45 000, 20 000 and 8 000. The 160 000 mol. wt. fraction predominated in the chromatograms of inherited amyloid protein and was further resolved into two main fractions of 17 000 and 15 000 mol. wt. in sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis. None of these fractions from inherited amyloid protein showed immunologic identity with tissue-derived amyloid protein A (AA) whereas all four fractions from secondary amyloid reacted against anti-AA antiserum. The three major Sepharose 6B fractions of secondary amyloid fibrils were resolved into a 25 000 mol. wt. fraction in SDS-polyacrylamide gel electrophoresis without urea but into a 12 000 mol. wt. fraction in gels containing 8M urea after more drastic dissolving conditions of the fibrils.