A single arginine to tryptophan interchange at beta-chain residue 458 of human complement component C4 accounts for the defect in classical pathway C5 convertase activity of allotype C4A6. Implications for the location of a C5 binding site in C4.
A single arginine to tryptophan interchange at beta-chain residue 458 of human complement component C4 accounts for the defect in classical pathway C5 convertase activity of allotype C4A6. Implications for the location of a C5 binding site in C4.
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人补体成分 C4 的 β 链残基 458 处的单个精氨酸与色氨酸互换导致同种异型 C4A6 的经典途径 C5 转化酶活性缺陷。
DOI：
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发表时间：
1992
期刊：
影响因子：
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通讯作者：
Isenman,DE
中科院分区：
文献类型：
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作者：
Ebanks,RO;Jaikaran,AS;Carroll,MC;Anderson,MJ;Campbell,RD;Isenman,DE
