Immuno-Affinity Purification of Heparinase

Authors
Llnhardt, Robert J.
Merchant, Zohar M.
Persinger, David W.
ORCID
https://orcid.org/0000-0003-2219-5833
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Other Contributors
Issue Date
1985-01-01
Keywords
Biology , Chemistry and chemical biology , Chemical and biological engineering , Biomedical engineering
Degree
Terms of Use
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Full Citation
Immuno-Affinity Purification of Heparinase, R.J. Linhardt, Z.M. Merchant, D.W. Persinger, The International Journal of Biochemistry, 17, 1179-1183 (1985).
Abstract
Polyclonal IgG rabbit antibodies were prepared against a purified heparinase from Flavobacterium heparinum. Immuno-affinity purification of crude and partially purified heparinase is described. The resulting enzyme was of comparable purity to that prepared using the standard multistep purification scheme. The antibodies prepared were found to increase the activity of bound heparinase.
Description
The International Journal of Biochemistry, 17, 1179-1183
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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
International Journal of Biochemistry
https://harc.rpi.edu/
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