Tosi M, Duponchel C, Bourgarel P, Colomb M, Meo T
Gene. 1986;42(3):265-72. doi: 10.1016/0378-1119(86)90230-1.
Genetic and acquired diseases in man show that the proteolytic activity of the complement component C1 is crucially regulated by C1 inhibitor (C1-INH), a plasma protein whose suspected relatedness to other serine proteinase inhibitors (serpins) contrasts with its atypically large size and high degree of glycosylation. Indeed we have found that the C1-INH polypeptide precursor synthesized in a cell-free system is a 64-kDa protein, hence it exceeds the length of the precursor forms of typical serpins. Seeking more conclusive sequence information and a probe for the structural locus, we isolated C1-INH cDNA clones from a library representing size-enriched human liver mRNA. Nucleotide sequence analysis of a clone covering the carboxyterminal half of C1-INH conclusively documents the relatedness of this protein with the serpins, and reveals 27% amino acid identity with alpha 1-antitrypsin.
人类的遗传和后天疾病表明，补体成分C1的蛋白水解活性关键受C1抑制剂（C1-INH）调节，C1-INH是一种血浆蛋白，它与其他丝氨酸蛋白酶抑制剂（丝氨酸蛋白酶抑制剂家族）疑似的相关性与其非典型的大尺寸和高度糖基化形成对比。实际上，我们发现在无细胞系统中合成的C1-INH多肽前体是一种64 kDa的蛋白质，因此它超过了典型丝氨酸蛋白酶抑制剂前体形式的长度。为了寻求更确凿的序列信息和结构基因座的探针，我们从一个代表大小富集的人肝mRNA的文库中分离出C1-INH cDNA克隆。对覆盖C1-INH羧基末端一半的克隆进行核苷酸序列分析，最终证明了该蛋白与丝氨酸蛋白酶抑制剂家族的相关性，并揭示了与α1-抗胰蛋白酶27%的氨基酸同一性。
