Comparative study on the structure of the light chains of human immunoglobulins. II. Assignment of a new subgroup.

Comparative study on the structure of the light chains of human immunoglobulins. II. Assignment of a new subgroup.
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人免疫球蛋白轻链结构的比较研究。

DOI:
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发表时间:
1979
期刊:
Journal of Biochemistry (Tokyo)
影响因子:
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通讯作者:
A. Shimizu
A. Shimizu
中科院分区:
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文献类型:
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作者:
N. Takahashi;T. Takayasu;T. Isobe;T. Shinoda;T. Okuyama;A. Shimizu

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人λ型Bence Jones蛋白NIG-48可变区的一级结构通过分析完全还原和氨乙基化的蛋白质的N-末端序列以及五个溴化氰片段来确定。NIG-48的可变区包含112个氨基酸残基。蛋白质NIG-48具有可变区的独特序列,与其他五个亚组的λ链具有低程度的同源性(约50%),并且在65附近添加了两个残基,可能代表一个新的亚组,即V λ VI。
The primary structure of the variable region of the human lambda type Bence Jones protein NIG-48 was determined by analysis of the N-terminal sequence of the completely reduced and aminoethylated protein, as well as of five cyanogen bromide fragments. The variable region of NIG-48 contains 112 amino acid residues. The protein NIG-48, having a unique sequence of the variable region, a low degree of homology (about 50%) with lambda chains of the five other subgroups and the addition of two residues around 65, may represent a new subgroup, namely V lambda VI.