Kiefer C R, Patton H M, McGuire B S, Garver F A
J Immunol. 1980 Jan;124(1):301-6.
The complete variable region sequence of the glycosylated Bence-Jones protein Wh has revealed that the most hypervariable segments of the first and third complementarity-determing regions (CDR) are identical with those of another glycosylated Bence-Jones protein (Nei) of the same lambda-subgroup. The carbohydrate is attached in both proteins at the identical sequences in the third CDR, and the sequences of the first CDR differ at only one position in fourteen. Because CDR sequence comparisons more sensitively reflect overall germ-line V gene similarities, proteins Wh and Nei could possibly reflect a "set" relationship analogous to the mouse V kappa isotype. Cluster analyses of currently available V lambda sequences supported this suggested relationship.
糖基化本斯-琼斯蛋白Wh的完整可变区序列显示，第一和第三个互补决定区（CDR）中最具高变的片段与同一λ亚群的另一种糖基化本斯-琼斯蛋白（Nei）的片段相同。两种蛋白的碳水化合物均连接在第三个CDR的相同序列处，且第一个CDR的序列在14个位置中仅一处不同。由于CDR序列比较能更敏感地反映种系V基因的总体相似性，蛋白Wh和Nei可能反映了一种类似于小鼠Vκ同种型的“组”关系。对现有Vλ序列的聚类分析支持了这一推测的关系。
