Partial amino acid sequences of the murine fourth component of complement (C4): demonstration of homology with human C4 and identification of the amino-terminal subunit in pro-C4.
Partial amino acid sequences of the murine fourth component of complement (C4): demonstration of homology with human C4 and identification of the amino-terminal subunit in pro-C4.
复制标题
鼠补体第四组分 (C4) 的部分氨基酸序列:证明与人 C4 的同源性并鉴定原 C4 中的氨基末端亚基。
DOI:
10.1073/pnas.77.7.4275
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发表时间:
1980
影响因子:
11.1
通讯作者:
Capra,JD
中科院分区:
文献类型:
--
作者:
Parker,KL;Shreffler,DC;Capra,JD
Radiolabeled murine C4 and C4 precursor (pro-C4) from cultured peritoneal macrophages were purified by immunoprecipitation and preparative gel electrophoresis. The partial NH2-terminal amino acid sequences of the isolated subunits demonstrated that murine C4 alpha, beta-, and gamma-chains all show sequence homology with the corresponding subunits of human C4; of the 10 residues identified in murine C4, all are identical to those in human C4. These data extend to the primary structural level the homology between the murine serum substance (Ss) protein and human C4. Comparisons of the amino acid sequences of murine pro-C4 and the constituent polypeptide chains of secreted C4 indicate that pro-C4 and the C4 beta-chain have an identical amino acid sequence. Both molecules have lysine at position 1, leucine at positions 4, 5, and 6, and phenylalanine at position 7. No sequence homology was found between pro-C4 and either the alpha- or gamma-subunits. These results define the beta-chain as the NH2-terminal subunit in the C4 precursor molecules.