胎盘膜联蛋白II的Fcγ受体活性

Fc gamma-receptor activity of placental annexin II.

作者信息

Kristoffersen E K, Ulvestad E, Bjørge L, Aarli A, Matre R

机构信息

Department of Microbiology and Immunology, Gade Institute, University of Bergen, Norway.

出版信息

Scand J Immunol. 1994 Aug;40(2):237-42. doi: 10.1111/j.1365-3083.1994.tb03456.x.

DOI:10.1111/j.1365-3083.1994.tb03456.x

PMID:8047847

Abstract

We have previously produced a MoAb, B1D6, against a placental FcR. The antigen isolated using F(ab')2-fragments of B1D6 exhibits Fc-binding properties with low affinity for IgG. The antigen is a single-chained glycoprotein with a molecular weight of approximately 37 kDa and a pI of about 7.0-8.5. Amino acid sequences from enzymatic digests of the antigen indicated that it is annexin II. Immunoreactivity using anti-annexin antisera and purified placental annexin II have further established the specificity of B1D6 to annexin II. The B1D6 epitope appears to be intramembraneous and intracellular on placental syncytiotrophoblasts, monocytes and other cells investigated.

摘要

我们之前制备了一种抗胎盘FcR的单克隆抗体B1D6。使用B1D6的F(ab')2片段分离出的抗原对IgG具有低亲和力的Fc结合特性。该抗原是一种单链糖蛋白，分子量约为37 kDa，pI约为7.0 - 8.5。抗原酶切后的氨基酸序列表明它是膜联蛋白II。使用抗膜联蛋白抗血清和纯化的胎盘膜联蛋白II进行的免疫反应性进一步证实了B1D6对膜联蛋白II的特异性。在胎盘合体滋养层细胞、单核细胞和其他研究的细胞上，B1D6表位似乎位于膜内和细胞内。