Tachibana H, Seki K, Murakami H
Graduate School of Genetic Resources Technology, Kyushu University, Fukuoka, Japan.
Biochim Biophys Acta. 1993 Oct 20;1182(3):257-63. doi: 10.1016/0925-4439(93)90067-b.
The carbohydrate chains on the light chains of human monoclonal antibody HB4C5 reactive to human lung adenocarcinoma tissue have been characterized. The HB4C5 antibody consists of two kinds of light chains (30 kDa and 32 kDa). Each chain has different carbohydrates of varying molecular masses linked to the variable regions. The 30 kDa light chain has been confirmed to be the active species for antibody binding. The carbohydrates on the light chains were characterized by lectin blot analysis combined with glycosidase treatment. A carbohydrate chain linked to the active 30 kDa light-chain species, and one of a few carbohydrate phenotypes on the 32 kDa light-chain species is characterized as "hybrid type". A sialylated complex-type carbohydrate could also bind to the 32 kDa light-chain species. Nucleotide sequence analysis revealed that one potential N-glycosylation site is located in the complementarity determining region 1 of the light chain, although no such site was found in the variable region of the heavy chain.
已对与人肺腺癌组织反应的人单克隆抗体HB4C5轻链上的碳水化合物链进行了表征。HB4C5抗体由两种轻链（30 kDa和32 kDa）组成。每条链在可变区连接有不同分子量的碳水化合物。已证实30 kDa轻链是抗体结合的活性成分。通过凝集素印迹分析结合糖苷酶处理对轻链上的碳水化合物进行了表征。与活性30 kDa轻链种类相连的一条碳水化合物链，以及32 kDa轻链种类上少数碳水化合物表型之一的特征为“杂合型”。一种唾液酸化的复合型碳水化合物也可与32 kDa轻链种类结合。核苷酸序列分析表明，一个潜在的N-糖基化位点位于轻链的互补决定区1，而在重链的可变区未发现此类位点。
