Kametani F, Takayasu T, Suzuki S, Shinoda T, Okuyama T, Shimizu A
J Biochem. 1983 Feb;93(2):421-9. doi: 10.1093/oxfordjournals.jbchem.a134196.
Amino acid sequence analysis was done on a human lambda Bence Jones protein NIG-64 with the major objective of determining the sequence of the variable region. Nineteen tryptic peptides covering 216 residues were isolated from the completely reduced and aminoethylated protein, and 17 of these were completely sequenced. These comprised the entire variable region and 11 from the constant region. For the remaining peptides covering the rest of the constant region, only partial sequences or the amino acid compositions were determined. All the tryptic peptides could be arranged in order on the basis of the above results and homology with other human lambda light chains of the same isotype. The sequence of the variable region of the protein is highly homologous with that of protein New of subgroup V lambda I as compared with other proteins of the same subgroup, suggesting that subgroup V lambda I may be further divided into subsubgroups, namely subsubgroups V lambda I-1 and V lambda I-2.
对人λ本斯-琼斯蛋白NIG-64进行了氨基酸序列分析，主要目的是确定可变区的序列。从完全还原和氨乙基化的蛋白质中分离出19个覆盖216个残基的胰蛋白酶肽段，其中17个被完全测序。这些肽段包括整个可变区和来自恒定区的11个肽段。对于覆盖恒定区其余部分的其余肽段，仅确定了部分序列或氨基酸组成。根据上述结果以及与相同同种型的其他人λ轻链的同源性，可以将所有胰蛋白酶肽段按顺序排列。与同一亚组的其他蛋白质相比，该蛋白可变区的序列与VλI亚组的New蛋白高度同源，这表明VλI亚组可能进一步分为亚亚组，即VλI-1亚亚组和VλI-2亚亚组。
