CHARACTERIZATION OF TRYPTIC FRAGMENTS OF HUMAN-COMPLEMENT FACTOR C-3
CHARACTERIZATION OF TRYPTIC FRAGMENTS OF HUMAN-COMPLEMENT FACTOR C-3
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DOI：
10.1016/0161-5890(85)90067-7
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发表时间：
1985-01-01
影响因子：
3.6
通讯作者：
SJOQUIST, J
中科院分区：
文献类型：
--
作者：
EGGERTSEN, G;HELLMAN, U;SJOQUIST, J
从胰蛋白酶消化的人C3中制备纯的C3 c和C3 d片段，并通过在Sepharose 4 B上的6 M盐酸胍中的凝胶过滤分离胰蛋白酶C3 c的各个链。未鉴别出低分子量片段。对多肽链的分子量、氨基酸组成和N末端氨基酸序列进行了表征。胰蛋白酶C3 c由1个来自β-链（MW 64，000）和2个来自α链。链（MW 40，000和23，000）。β-链片段衍生自该链的C-末端部分，23，000 MW组分构成α-链的氨基末端链40，000 MW的片段从α-半乳糖苷酶的C-末端发出。链胰蛋白酶C3 d在十二烷基硫酸钠中的聚丙烯酰胺凝胶电泳上显示微异质性，但具有均一的N-末端。利用抗C_3和C_3c亚基的抗血清进行免疫印迹，提出了胰蛋白酶降解C_3的方案，并指出了C_3片段在完整分子中的位置。
C3c and C3d fragments were prepared in pure form from trypsin-digested human C3, and the individual chains of tryptic C3c were isolated by gel filtration on Sepharose 4B in 6 M guanidinium hydrochloride. No low MW fragments were identified. The polypeptide chains were characterized with regard to MW, amino acid composition and N-terminal amino acid sequence. Tryptic C3c consisted of 1 fragment from the .beta.-chain (MW 64,000) and 2 from the .alpha.''-chain (MW 40,000 and 23,000). The .beta.-chain fragment was derived from the C-terminal part of the chain, and the 23,000 MW component constituted the amino terminal end of the .alpha.-chain. The 40,000 MW fragment emanated from the C-terminal end of the .alpha.-chain. Tryptic C3d displayed microheterogeneity on polyacrylamide gel electrophoresis in sodium dodecyl sulfate, but possessed a homogeneous N-terminal. By utilization of antisera against subunits of C3 and C3c in immunoblotting a degradation scheme for C3 by trypsin was proposed and the positions of the fragments in the intact molecule were indicated.