tailieunhanh - Báo cáo khoa hoc:" A heparin binding synthetic peptide from human HIP / RPL29 fails to specifically differentiate between anticoagulantly active and inactive species of heparin"

Tuyển tập báo cáo các nghiên cứu khoa học quốc tế ngành y học dành cho các bạn tham khảo đề tài: A heparin binding synthetic peptide from human HIP / RPL29 fails to specifically differentiate between anticoagulantly active and inactive species of heparin | Journal of Negative Results in BioMedicine BioMed Central Research Open Access A heparin binding synthetic peptide from human HIP RPL29 fails to specifically differentiate between anticoagulantly active and inactive species of heparin David E Hoke1 2 Daniel D Carson3 and Magnus Hook 1 Address 1Center for Extracellular Matrix Biology The Texas A M University System Health Science Center Institute of Biosciences and Technology Houston Texas 77030 2Current Address Department of Pathology University of Melbourne Parkville Victoria 3010 Australia and 3Department of Biological Sciences University of Delaware Newark Delaware 19716 Email David E Hoke - dehoke@ Daniel D Carson - dcarson@ Magnus Hook - mhook@ Corresponding author Published 25 February 2003 Received 29 August 2002 Accepted 25 February 2003 Journal of Negative Results in BioMedicine 2003 2 1 This article is available from http content 2 1 1 2003 Hoke et al licensee BioMed Central Ltd. This is an Open Access article verbatim copying and redistribution of this article are permitted in all media for any purpose provided this notice is preserved along with the article s original URL. Abstract Despite extensive progress in determining structures within heparin and heparan sulfate Hp HS and the discovery of numerous proteinaceous binding partners for Hp HS so far the only detailed characterization of a specific protein-glycosaminoglycan interaction is antithrombin III ATIII binding to a Hp pentasaccharide containing a unique 3-O-sulfated glucosamine residue. Previously it was reported from our laboratories that a 16 amino acid synthetic peptide derived from the C-terminus of human HIP RPL29 HIP peptide-1 enriched for ATIII-dependent anticoagulant activity presumably by specifically binding the ATIII pentasaccharide. Herein we demonstrate that HIP peptide-1 cannot enrich ATIII-dependent anticoagulant activity from a starting pool of porcine intestinal .