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抗β43 - 47 Fab片段对纤维蛋白原E结构域中聚合位点表达的影响。

The effect of anti-beta 43-47 Fab fragments on expression of the polymerization sites in the E domain of fibrinogen.

作者信息

Cierniewski C S, Poniatowski J

机构信息

Department of Biophysics, Medical School in Lódź, Poland.

出版信息

Acta Biochim Pol. 1990;37(1):31-7.

PMID:2087914
Abstract

In order to assess the significance of the aminoterminal residues of the B beta chain in expression of polymerization sites of the E domain, we have prepared polyclonal antiserum against a synthetic peptide corresponding to beta 43-47 of human fibrinogen. Affinity purified immunoglobulin IgG and Fab prepared from these antibodies reacted strongly and specifically with the synthetic pentapeptide and intact fibrinogen molecule. This specificity was determined both by radioimmunoassay and Western blot analysis of fibrinogen and its plasmic fragments and described in our previous paper (Cierniewski et al., 1986, Biochim. Biophys. Acta, 884, 594-597). Immunochemically purified anti beta 43-47 antibodies and their Fab fragments were strong inhibitors of the fibrin monomer polymerization. Our results imply that amino acid sequence beta 43-47 recognized by these antibodies may be in a close vicinity to the contact sites of the E domain.

摘要

为了评估Bβ链氨基末端残基在E结构域聚合位点表达中的重要性,我们制备了针对与人纤维蛋白原β43 - 47相对应的合成肽的多克隆抗血清。从这些抗体制备的亲和纯化免疫球蛋白IgG和Fab与合成五肽和完整的纤维蛋白原分子强烈且特异性地反应。这种特异性通过对纤维蛋白原及其血浆片段的放射免疫测定和蛋白质印迹分析确定,并在我们之前的论文中有所描述(Cierniewski等人,1986年,《生物化学与生物物理学报》,884,594 - 597)。免疫化学纯化的抗β43 - 47抗体及其Fab片段是纤维蛋白单体聚合的强抑制剂。我们的结果表明,这些抗体识别的氨基酸序列β43 - 47可能紧邻E结构域的接触位点。

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