首页> 美国卫生研究院文献>Biochemical Journal >Amino acid sequence of the Bb fragment from complement Factor B. Sequence of the major cyanogen bromide-cleavage peptide (CB-II) and completion of the sequence of the Bb fragment.
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Amino acid sequence of the Bb fragment from complement Factor B. Sequence of the major cyanogen bromide-cleavage peptide (CB-II) and completion of the sequence of the Bb fragment.

机译:来自补体因子B的Bb片段的氨基酸序列。主要的溴化氰裂解肽(CB-II)序列和Bb片段序列的完成。

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摘要

The amino acid sequence of peptide CB-II, the major product (mol.wt. 30 000) of CNBr cleavage of fragment Bb from human complement Factor B, is given. The sequence was obtained from peptides derived by trypsin cleavage of peptide CB-II and clostripain digestion of fragment Bb. Cleavage of two Asn-Gly bonds in peptide CB-II was also found useful. These results, along with those presented in the preceding paper [Gagnon & Christie (1983) Biochem. J. 209, 51-60], yield the complete sequence of the 505 amino acid residues of fragment Bb. The C-terminal half of the molecule shows strong homology of sequence with serine proteinases. Factor B has a catalytic chain (fragment Bb) with a molecular weight twice that of proteinases previously described, suggesting that it is a novel type of serine proteinase, probably with a different activation mechanism.
机译:给出了肽CB-II的氨基酸序列,该肽是CNBr从人补体因子B上裂解片段Bb的主要产物(分子量30000)。该序列得自通过胰蛋白酶切割肽CB-II和梭菌蛋白酶消化片段Bb衍生的肽。还发现裂解肽CB-II中的两个Asn-Gly键是有用的。这些结果以及先前的论文中提出的结果[Gagnon&Christie(1983)Biochem。 [J. 209,51-60]产生了片段Bb的505个氨基酸残基的完整序列。分子的C端一半显示出与丝氨酸蛋白酶的强序列同源性。因子B的催化链(片段Bb)的分子量是前述蛋白酶的两倍,这表明它是一种新型的丝氨酸蛋白酶,可能具有不同的激活机制。

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