Development of a method for the efficient release of N-glycans from glycoproteins generating native deglycosylated proteins
作者： Shengjun Wang , Chuanliang Ma , Huili Yu , Changgan Huang , Qingsheng Qi
DOI: 10.1016/J.ENZMICTEC.2012.05.003
关键词: RNase P 、 Circular dichroism 、 Glycan 、 High concentration 、 Biochemistry 、 Glycoprotein 、 Yeast carboxypeptidase 、 Dithiothreitol 、 Chemistry 、 Irreversible denaturation
摘要: In many cases, it is desirable to maintain the native status of target glycoproteins when they are deglycosylated. However, most conventional deglycosylation process often causes irreversible denaturation glycoproteins. present study, we developed a method that could obtain deglycosylated proteins employing Png1p-ΔH1, which was confirmed tolerate high concentration dithiothreitol (DTT). To prove this process, ribonuclease B (RNase B) and Yeast carboxypeptidase (CPY) were employed as targeting Our results both them be completely in presence DTT refolded removed. The circular dichroism spectroscopy (CD) measurement CPY RNase indicated structure had recovered their status. This offers possibility efficiently releasing N-linked glycans from obtaining proteins.
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