Purification and structural studies of rabbit erythrocyte cytochrome b5.
Purification and structural studies of rabbit erythrocyte cytochrome b5.
复制标题
兔红细胞色素b5的纯化及结构研究。
DOI：
10.1016/s0006-291x(83)80006-0
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发表时间：
1983
影响因子：
3.1
通讯作者：
Hultquist,DE
中科院分区：
文献类型：
--
作者：
Schafer,DA;Hultquist,DE
用DE-52纤维素柱、Sephadex G-75柱层析和DEAE-Sephadex A50柱层析，从兔红细胞胞浆组分中分离到一种高度纯化的单一形式的细胞色素b5。该细胞色素在结构上与兔肝微粒体细胞色素b5的N-末端、血红素结合区相似。像肝脏蛋白一样，它在氨基末端被阻断。其氨基酸组成与微体蛋白的1-97位残基相似。除一个例外，来自兔红细胞脱细胞色素b5的胰蛋白肽与从微粒体细胞色素b5的可溶性血肽片段获得的胰蛋白肽共同洗脱。这些发现，再加上对羧基末端胰蛋白酶多肽的氨基酸序列分析，确定红细胞细胞色素b5是一个97个残基的多肽。
A single form of cytochromeb5has been isolated in highly purified form from the cytosolic fraction of rabbit erythrocytes by sequential chromatography on DE-52 cellulose, Sephadex G-75, and DEAE-Sephadex A50. The cytochrome is structurally similar to the N-terminal, heme-binding domain of rabbit liver microsomal cytochromeb5. Like the liver protein, it is blocked at the amino terminus. Its amino acid composition is similar to that of residues 1–97 of the microsomal protein. With one exception, tryptic peptides derived from apo-cytochromeb5of rabbit erythrocytes co-elute with the tryptic peptides obtained from a soluble hemepeptide fragment of microsomal cytochromeb5. These findings, together with amino acid sequence analysis of the carboxyl terminal tryptic peptides, identify the erythrocyte cytochromeb5as a 97-residue peptide.