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使用金属螯合色谱法对妊娠相关血浆蛋白-A和α2-巨球蛋白进行的比较研究。

Comparative studies of pregnancy associated plasma protein-A and alpha 2-macroglobulin using metal chelate chromatography.

作者信息

Sinosich M J, Davey M W, Teisner B, Grudzinskas J G

出版信息

Biochem Int. 1983 Jul;7(1):33-42.

PMID:6206864
Abstract

Pregnancy Associated Plasma Protein-A (PAPP-A), shares many physicochemical and functional similarities with alpha-2-macroglobulin (alpha 2M). Comparative studies between these two proteins and various metal chelate Sepharoses have shown that both PAPP-A and alpha 2M bind to the copper and zinc, but not to the calcium, manganese or magnesium chelate gels. In addition to PAPP-A and alpha 2M, fibronectin and Pregnancy Zone Protein (PZP) were also found to bind to the copper and zinc chelate gels. Analysis of proteins bound to the zinc chelate Sepharose showed alpha 2M to have the highest affinity for the matrix, followed by PAPP-A and fibronectin, which coeluted, and then PZP. Following the zinc chelate chromatography minor qualitative changes were detected only in PAPP-A, but the eluted proteins retained in-vitro functional activity. By atomic absorption, PAPP-A, alpha 2M and fibronectin were found to contain zinc.

摘要

妊娠相关血浆蛋白-A(PAPP-A)与α-2-巨球蛋白(α2M)在许多物理化学和功能特性上相似。对这两种蛋白质与各种金属螯合琼脂糖的比较研究表明,PAPP-A和α2M都能与铜和锌螯合凝胶结合,但不能与钙、锰或镁螯合凝胶结合。除了PAPP-A和α2M,还发现纤连蛋白和妊娠区蛋白(PZP)也能与铜和锌螯合凝胶结合。对结合到锌螯合琼脂糖上的蛋白质分析表明,α2M对基质的亲和力最高,其次是PAPP-A和共同洗脱的纤连蛋白,然后是PZP。经过锌螯合层析后,仅在PAPP-A中检测到微小的定性变化,但洗脱的蛋白质保留了体外功能活性。通过原子吸收法发现,PAPP-A、α2M和纤连蛋白都含有锌。

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