FERREASCIDIN - A HIGHLY AROMATIC PROTEIN CONTAINING 3,4-DIHYDROXYPHENYLALANINE FROM THE BLOOD-CELLS OF A STOLIDOBRANCH ASCIDIAN
FERREASCIDIN - A HIGHLY AROMATIC PROTEIN CONTAINING 3,4-DIHYDROXYPHENYLALANINE FROM THE BLOOD-CELLS OF A STOLIDOBRANCH ASCIDIAN
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DOI：
10.1021/bi00399a009
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发表时间：
1987-12-15
期刊：
影响因子：
2.9
通讯作者：
ROSS, IL
中科院分区：
文献类型：
--
作者：
DORSETT, LC;HAWKINS, CJ;ROSS, IL
建立了一种从海鞘血细胞中分离纯化主要蛋白的方法。该蛋白因其强大的铁结合能力（每个分子两个Fe3+）而被称为铁酪酸蛋白，是已表征的最芳香的蛋白质，含有67%的芳香氨基酸，包括42%的酪氨酸和17%的3,4-二羟基苯丙氨酸。它是一种糖蛋白，经蔗糖梯度离心测定，表观沉降系数为1.3 S，对应的分子量为10,000，与沉淀平衡分析（9800 .+-）所得的结果一致。100)。3,4-二羟基苯丙氨酸是一种参与无脊椎动物体外组织硬化的氨基酸，它的存在支持了早期的假设，即血细胞参与了海鞘的形成。整个细胞的圆二色性表明该蛋白被分离，没有发生重大的结构变化。
A method of isolation and purification was developed for the major protein from the blood cells of the stolidobranch ascidian Pyura stolonifera. The protein, called ferreascidin because of its strong iron binding capacity (two Fe3+ per molecule), is the most aromatic protein that has been characterized, with 67% aromatic amino acids including 42% tyrosine and 17%, 3,4-dihydroxyphenylalanine. It is a glycoprotein with an apparent sedimentation coefficient of 1.3 S determined by sucrose gradient centrifugation, corresponding to a molecular weight of 10,000 which is in agreement with that obtained from sedimentation equilibrium analysis (9800 .+-. 100). The presence of 3,4-dihydroxyphenylalanine, an amino acid involved in sclerotization of outer body tissues of invertebrates, supports the early proposition that the blood cells are involved in the formation of the test of the ascidian. Circular dichroism of whole cells indicated that the protein was isolated without major structural change.