Differential Anticoagulant Activity of Heparin Fragments Prepared Using Microbial Heparinase
Authors
Linhardt, Robert J.
Grant, A.
Cooney, C.L.
Langer, R.
ORCID
https://orcid.org/0000-0003-2219-5833
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Other Contributors
Issue Date
1982
Keywords
Biology , Chemistry and chemical biology , Chemical and biological engineering , Biomedical engineering
Degree
Terms of Use
Attribution 3.0 United States
CC BY : this license allows reusers to distribute, remix, adapt, and build upon the material in any medium or format, so long as attribution is given to the creator. The license allows for commercial use. Credit must be given to the authors and the original work must be properly cited.
CC BY : this license allows reusers to distribute, remix, adapt, and build upon the material in any medium or format, so long as attribution is given to the creator. The license allows for commercial use. Credit must be given to the authors and the original work must be properly cited.
Full Citation
Differential 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).
Abstract
Heparin 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.
Description
The 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.
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.
Department
The Linhardt Research Labs.
The Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS)
The Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS)
Publisher
Elsevier
Relationships
The Linhardt Research Labs Online Collection
Rensselaer Polytechnic Institute, Troy, NY
https://harc.rpi.edu/
Rensselaer Polytechnic Institute, Troy, NY
https://harc.rpi.edu/
Access
Open Access
A full text version is available in DSpace@RPI
CC BY — Creative Commons Attribution
A full text version is available in DSpace@RPI
CC BY — Creative Commons Attribution