Enzymic O-sulfation of tyrosine residues in hirudins by sulfotransferase from Eubacterium A-44
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1994.tb18988.x/fullpdf
Reference34 articles.
1. PHARMACOLOGICAL DATA ON PHYLLOKININ (BRADYKINYL-ISOLEUCYL-TYROSINE O-SULPHATE) AND BRADYKINYL-ISOLEUCYL-TYROSINE
2. Tyrosine sulfation is a trans-Golgi-specific protein modification.
3. [54] Hirudin
4. Cholecystokinin (pancreozymin). 4. Synthesis and properties of a biologically active analog of the C-terminal heptapeptide with .epsilon.-hydroxynorleucine sulfate replacing tyrosine sulfate
5. Use of site-directed mutagenesis to investigate the basis for the specificity of hirudin
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2. Enhanced anticoagulant activity of hirudin-i analogue co-expressed with arylsulfotransferase in periplasm of E. coli BL21(DE3);Journal of Biotechnology;2020-11
3. Structure-activity studies on C-terminal hirudin peptides containing sulfated tyrosine residues;International Journal of Peptide and Protein Research;2009-01-12
4. Toward a framework for sulfoproteomics: Synthesis and characterization of sulfotyrosine-containing peptides;Biopolymers;2007-08-06
5. Recombinant expression of selectively sulfated proteins in Escherichia coli;Nature Biotechnology;2006-10-29
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