The complete amino acid sequence of bovine antithrombin (ATIII)
- 1 April 1991
- journal article
- research article
- Published by Springer Nature in Protein Journal
- Vol. 10 (2) , 205-212
- https://doi.org/10.1007/bf01024785
Abstract
Bovine antithrombin (ATIII) is a glycoprotein of Mr 56,600. Its primary structure was established using peptide sequences from five different digests. Bovine ATIII exhibits four glycosylation sites as well as human ATIII. The primary structures of bovine and human ATIII were compared: all the residues required for the integrity of the heparin-binding domain are strictly conserved. However, there are differences in the secondary structures of both proteins, bovine and human ATIII.Keywords
This publication has 37 references indexed in Scilit:
- Crystal structure of bovine antithrombin IIIActa crystallographica Section B, Structural science, crystal engineering and materials, 1990
- Crystallization and preliminary crystallographic data for bovine antithrombin IIIJournal of Molecular Biology, 1989
- Physiological variant of antithrombin‐III lacks carbohydrate sidechain at Asn 135FEBS Letters, 1987
- Structure-activity relationship in heparin: A synthetic pentasaccharide with high affinity for antithrombin III and eliciting high anti-factor Xa activityBiochemical and Biophysical Research Communications, 1983
- Mutation of Antitrypsin to AntithrombinNew England Journal of Medicine, 1983
- A simple method for displaying the hydropathic character of a proteinJournal of Molecular Biology, 1982
- The site in human antithrombin for functional proteolytic cleavage by human thrombinFEBS Letters, 1981
- The thrombin cleavage site in bovine antithrombinFEBS Letters, 1979
- Prediction of the Secondary Structure of Proteins from their Amino Acid SequencePublished by Wiley ,1979
- Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteinsJournal of Molecular Biology, 1978