Comparative properties of human α‐1‐proteinase inhibitor glycosylation variants

FEBS Letters

Travis, James¹  Potempa, Jan²  Guzdek, Amalia²  Dubin, Adam² 

[1] Department of Biochemistry, University of Georgia, Athens, GA 30602, USA;Institute of Molecular Biology, Jagiellonian University, 31 120 Krakow, Poland

关键词: α-1-Proteinase inhibitor;    Inhibitor of glycosylation;    Hep G 2 cell;   

DOI  :  10.1016/0014-5793(90)80464-T

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Variant forms of human α-1-proteinase inhibitor (α-1-PI), obtained by the treatment of human Hep G2 cells with specific inhibitors of glycosylation were tested for both inhibitory activity and heat stability. All were found to have the same second-order association rate with human neutrophil elastase, indicating a lack of importance of the carbohydrate moiety. In contrast, incompletely glycosylated forms of α-1-PI were found to be heat sensitive relative to the mature protein, suggesting a role for carbohydrate in protein stabilization.

【 授权许可】

Unknown