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Comparative properties of human α‐1‐proteinase inhibitor glycosylation variants
Author(s) -
Guzdek Amalia,
Potempa Jan,
Dubin Adam,
Travis James
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)80464-t
Subject(s) - glycosylation , proteinase inhibitor , elastase , biochemistry , carbohydrate , chemistry , pi , alpha (finance) , glycoprotein , inhibitory postsynaptic potential , enzyme , biology , medicine , endocrinology , construct validity , nursing , patient satisfaction
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.