Primary structures of MCP-1 and MCP-2, natural peptide antibiotics of rabbit lung macrophages.
Primary structures of MCP-1 and MCP-2, natural peptide antibiotics of rabbit lung macrophages.
复制标题
DOI：
10.1016/s0021-9258(17)43888-9
复制
发表时间：
1983-12
期刊：
影响因子：
--
通讯作者：
M. Selsted;D. Brown;R. Delange;R. Lehrer
中科院分区：
文献类型：
--
作者：
M. Selsted;D. Brown;R. Delange;R. Lehrer
通过采用制备型凝胶电泳和高效液相色谱的改进程序纯化兔肺泡巨噬细胞的杀菌肽 MCP-1 和 MCP-2。这些肽富含精氨酸和胱氨酸，缺乏游离的巯基和可检测水平的碳水化合物。完整的序列测定表明，MCP-1与MCP-2的不同之处仅在于NH2末端第13位残基处的精氨酸替换为亮氨酸，并且这些分子各自为含有3个分子内二硫键的33个氨基酸残基的单链多肽。 MCP-1和MCP-2的完整氨基酸序列为：（正文中的序列）
The microbicidal peptides, MCP-1 and MCP-2, of rabbit alveolar macrophages were purified by an improved procedure that employed preparative gel electrophoresis and high performance liquid chromatography. The peptides were arginine- and cystine-rich and lacked free sulfhydryl groups and detectable levels of carbohydrate. Complete sequence determinations revealed that MCP-1 differed from MCP-2 only by the substitution of arginine for leucine at residue 13 from the NH2 terminus and that the molecules were each single chain polypeptides of 33 amino acid residues containing three intramolecular disulfide bonds. The complete amino acid sequences of MCP-1 and MCP-2 are: (sequence in text)