Yuan J M, Hsiung L M, Gagnon J
Biochem J. 1986 Jan 15;233(2):339-45. doi: 10.1042/bj2330339.
The light chain and heavy chain of reduced and alkylated human complement Factor I were purified by high-pressure gel-permeation chromatography. CNBr cleavage of Factor I light chain yielded four major fragments, which were purified by gel filtration. N-Terminal sequence analysis of the CNBr-cleavage fragments allowed identification of 200 of the approx. 240 amino acid residues of the light chain. An alignment is proposed, based on sequence analysis of peptides obtained after cleavage at arginine residues of the light chain and on homology of the sequence determined with that of other serine proteinases. The sequence around the active-site serine residue was established and three potential attachment sites for carbohydrate moieties were identified.
通过高压凝胶渗透色谱法纯化还原和烷基化的人补体I因子的轻链和重链。用溴化氰裂解I因子轻链产生四个主要片段,通过凝胶过滤对其进行纯化。对溴化氰裂解片段进行N端序列分析,从而鉴定出轻链约240个氨基酸残基中的200个。基于轻链精氨酸残基裂解后所得肽段的序列分析以及所确定序列与其他丝氨酸蛋白酶序列的同源性,提出了一种比对。确定了活性位点丝氨酸残基周围的序列,并鉴定出三个潜在的碳水化合物部分附着位点。