Glycosylation of two recombinant human uterine tissue plasminogen activator variants carrying an additional N-glycosylation site in the epidermal-growth-factor-like domain
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1994.tb19945.x/fullpdf
Reference62 articles.
1. Tyrosine 67 in the epidermal growth factor-like domain of tissue-type plasminogen activator is important for clearance by a specific hepatic receptor.
2. Studies on the acceptor specificity of asparagine-N -glycosyl-transferase from rat liver
3. Primary structural requirements for N -glycosylation of peptides in rat liver
4. A tissue-type plasminogen activator mutant with prolonged clearance in vivo. Effect of removal of the growth factor domain.
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