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一种具有抗肺炎克雷伯菌多糖K30和K33中3,4-丙酮酸化半乳糖抗体活性的人单克隆IgM(蛋白WEA)Fv区的氨基酸序列。

Amino acid sequence of the Fv region of a human monoclonal IgM (protein WEA) with antibody activity against 3,4-pyruvylated galactose in Klebsiella polysaccharides K30 and K33.

作者信息

Goñi F, Frangione B

出版信息

Proc Natl Acad Sci U S A. 1983 Aug;80(15):4837-41. doi: 10.1073/pnas.80.15.4837.

Abstract

We have determined the amino acid sequence of the Fv [variable heavy (VH) and variable light (VL)] region of a human monoclonal IgM-kappa with antibody activity against 3,4-pyruvylated galactose, isolated from the plasma of patient WEA with Waldenström macroglobulinemia. The VH region has 114 residues, belongs to subgroup III, and has a very short third complementarity-determining region (CDR3), probably due to a small D segment/or an unusual D-J rearrangement (D, diversity; J, joining). The VL region has 108 residues and belongs to subgroup V kappa I. Compared to other members of the human VHIII and V kappa I families, WEA Fv does not appear to have significant differences within the framework residues but has unique CDRs that might be responsible for the particular antibody activity. Another IgM-kappa (GAL), which has an as-yet-undetermined antibody activity, shares a striking homology in V kappa with WEA, including an identical CDR1.

摘要

我们已确定从患有华氏巨球蛋白血症的患者WEA血浆中分离出的、具有抗3,4-丙酮酸化半乳糖抗体活性的人单克隆IgM-κ的Fv[重链可变区(VH)和轻链可变区(VL)]区域的氨基酸序列。VH区域有114个残基,属于III亚组,且具有非常短的第三互补决定区(CDR3),这可能是由于D片段较小/或存在不寻常的D-J重排(D,多样性;J,连接)。VL区域有108个残基,属于VκI亚组。与人类VHIII和VκI家族的其他成员相比,WEA Fv在框架残基内似乎没有显著差异,但具有独特的互补决定区,这可能是其特定抗体活性的原因。另一种IgM-κ(GAL),其抗体活性尚未确定,在Vκ区域与WEA具有显著的同源性,包括相同的CDR1。

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