Differential Anticoagulant Activity of Heparin Fragments Prepared Using Microbial Heparinase
AuthorLinhardt, Robert J.; Grant, A.; Cooney, C.L.; Langer, R.
SubjectBiology; Chemistry and chemical biology; Chemical and biological engineering; Biomedical engineering
Full CitationDifferential Anticoagulant Activity of Heparin Fragments Prepared Using Microbial Heparinase, R.J. Linhardt, A. Grant, C.L. Cooney, R. Langer, The Journal of Biological Chemistry, 257, 7310-7313 (1982).
MetadataShow full item record
AbstractHeparin of an average molecular weight of 13,000 with known polydispersity was degraded using microbial heparinase. The kinetics of this degradation were followed by four assays which measured the anticoagulant activity of the heparin digestion products. Both clotting and amidolytic chromogenic assays were used to measure heparin-potentiated inhibition of both thrombin and Factor Xa. These assays showed different profiles throughout the digestion and were related to the average molecular weight of the digestion products.l The final products of this enzymatic digestion were fractionated on the basis of size and their anticoagulant activities were measured. Fragments causing Factor Xa inhibition but not thrombin inhibition were isolated. Anticoagulant activity was found in a fragment as small as a tetrasaccharide.;
DescriptionThe Journal of Biological Chemistry, 257, 7310-7313; Note : if this item contains full text it may be a preprint, author manuscript, or a Gold OA copy that permits redistribution with a license such as CC BY. The final version is available through the publisher’s platform.
DepartmentThe Linhardt Research Labs.; The Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS);
RelationshipsThe Linhardt Research Labs Online Collection; Rensselaer Polytechnic Institute, Troy, NY; https://harc.rpi.edu/;
AccessCC BY — Creative Commons Attribution; Open Access; A full text version is available in DSpace@RPI;
The following license files are associated with this item: