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鸡甲胎蛋白的纯化及其理化与免疫学分析

Purification and physicochemical and immunological analysis of chicken alpha-fetoprotein.

作者信息

Ido E, Matsuno T

出版信息

Jpn J Med Sci Biol. 1982 Jun;35(3):87-96. doi: 10.7883/yoken1952.35.87.

DOI:10.7883/yoken1952.35.87
PMID:6182320
Abstract

Chicken alpha-fetoprotein was isolated from 12 to 13-day-old embryonic chicken serum by column chromatography on CM-Sephadex C-50. Hydroxyapatite and DEAE-Sephadex A-25. The purified protein was homogeneous based on polyacrylamide gel electrophoresis, immunoelectrophoresis and isoelectric focusing. The purified protein had the following physicochemical and immunological properties. (1) It was a glycoprotein with a single polypeptide chain. (2) The molecular weight of the protein was estimated at 71,000 by SDS-polyacrylamide gel electrophoresis. (3) The isoelectric point of the protein was 4.90. (4) The amino acid composition of the protein was similar to those of mammalian alpha-fetoproteins. (5) The protein showed no steroid-binding capacity. (6) It was immunologically distinct from mammalian alpha-fetoprotein. (7) No immunological cross-reaction was observed between the protein and chicken albumin.

摘要

通过在CM-葡聚糖凝胶C-50、羟磷灰石和二乙氨基乙基葡聚糖凝胶A-25上进行柱色谱,从12至13日龄鸡胚血清中分离出鸡甲胎蛋白。基于聚丙烯酰胺凝胶电泳、免疫电泳和等电聚焦,纯化后的蛋白质是均一的。纯化后的蛋白质具有以下物理化学和免疫学特性。(1)它是一种具有单条多肽链的糖蛋白。(2)通过十二烷基硫酸钠-聚丙烯酰胺凝胶电泳估计该蛋白质的分子量为71,000。(3)该蛋白质的等电点为4.90。(4)该蛋白质的氨基酸组成与哺乳动物甲胎蛋白的氨基酸组成相似。(5)该蛋白质不显示类固醇结合能力。(6)它在免疫学上与哺乳动物甲胎蛋白不同。(7)在该蛋白质与鸡白蛋白之间未观察到免疫交叉反应。

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Purification and physicochemical and immunological analysis of chicken alpha-fetoprotein.鸡甲胎蛋白的纯化及其理化与免疫学分析
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