A Highly Stable Covalent Conjugated Heparin Biochip for Heparin-Protein Interactions Studies

Authors
Zhang, Fuming
Fath, Melissa
Marks, Rory
Linhardt, Robert J.
ORCID
https://orcid.org/0000-0003-2219-5833
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Other Contributors
Issue Date
2002-05-15
Keywords
Biology , Chemistry and chemical biology , Chemical and biological engineering , Biomedical engineering
Degree
Terms of Use
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Full Citation
A Highly Stable Covalent Conjugated Heparin Biochip for Heparin-Protein Interactions Studies, F. Zhang, M. Fath, R. Marks, R.J. Linhardt, Analytical Biochemistry, 304, 271-273, 2002.
Abstract
Heparin is a proteoglycan composed of highly sulfated linear polysaccharides of alternating uronic acid and glucosamine that interacts with a wide variety of proteins and peptides (1). Heparin and the structurally related heparan sulfate are the most acidic polysaccarides in the human body and, as a result, interact with many cationic proteins, giving rise to myriad biological activities (2). Some of these interactions have received extensive attention in recent years, including heparin’s binding to growth factors (3, 4) influencing angiogenesis and other proliferation-dependent processes, and its binding to the ectodomain proteins of pathogens influencing infection.
Description
Analytical Biochemistry, 304, 271-273
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Department
The Linhardt Research Labs.
The Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS)
Publisher
Relationships
The Linhardt Research Labs Online Collection
Rensselaer Polytechnic Institute, Troy, NY
Analytical Biochemistry
https://harc.rpi.edu/
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https://login.libproxy.rpi.edu/login?url=https://doi.org/10.1006/abio.2002.5617