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与肝素相互作用可保护组织转谷氨酰胺酶不被加热和蛋白水解失活。

Interaction with heparin protects tissue transglutaminase against inactivation by heating and by proteolysis.

作者信息

Gambetti Stefania, Dondi Alessia, Cervellati Carlo, Squerzanti Monica, Pansini Francesco S, Bergamini Carlo M

机构信息

Department of Biochemistry and Molecular Biology, University of Ferrara, Italy.

出版信息

Biochimie. 2005 Jun;87(6):551-5. doi: 10.1016/j.biochi.2005.01.012. Epub 2005 Feb 24.

Abstract

The considerable affinity of tissue transglutaminase for heparin was the basis for use of heparin-based affinity matrices for enzyme purification. Interaction of transglutaminase with heparin might mimic the physiological binding to membrane heparan sulfates, accounting for the limited but significant fraction of enzyme exposed at cell surface to crosslink ECM proteins. Exploring effects of heparin on transglutaminase activity and stability, we have noted that heparin only slightly affects activity in vitro, but the protein against heat treatment and proteolysis.

摘要

组织转谷氨酰胺酶与肝素具有相当高的亲和力,这是使用基于肝素的亲和基质进行酶纯化的基础。转谷氨酰胺酶与肝素的相互作用可能模拟其与膜硫酸乙酰肝素的生理结合,这解释了细胞表面暴露的有限但显著比例的酶用于交联细胞外基质蛋白的原因。在探索肝素对转谷氨酰胺酶活性和稳定性的影响时,我们注意到肝素在体外仅对活性有轻微影响,但能使该蛋白抵抗热处理和蛋白水解。

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