Chemistry: molecular biology and microbiology – Enzyme – proenzyme; compositions thereof; process for... – Hydrolase
Patent
1994-08-17
2000-11-21
Naff, David M.
Chemistry: molecular biology and microbiology
Enzyme , proenzyme; compositions thereof; process for...
Hydrolase
435178, 435180, 435181, 435196, 435815, 436529, 436824, 530413, 530813, 536 21, C12N 924, G01N 33544, C07K 122, C07K 1710
Patent
active
061501514
ABSTRACT:
An affinity chromatographic matrix for purification of a biological material is provided having an ionically charged polymeric ligand such as glycoaminoglycan non-covalently bound directly by an ionic bond to an oppositely ionically charged group on a chromatographic matrix. Having the ligand non-covalently bound to the matrix by an ionic bond, allows the ligand to be easily washed off the matrix and replaced for subsequent purifications without having to replace the matrix. A biological material in a crude mixture is purified by non-covalently binding the material to the bound ligand and dissociating the material from the ligand. Matrices that may be used include crosslinked agarose, crosslinked dextran, crosslinked cellulose, crosslinked dextran and bisacrylamide, or matrices based on silica or plastic polymers. The charged group may be a quaternary amine or diethylaminoethyl group. Chondroitinase is purified from a crude mixture containing contaminating proteins by contacting the crude mixture with an anion exchange resin containing chondroitin sulfate non-covalently bound by an ionic bond. Chondroitinase non-covalently binds to the bound chondroitin sulfate and contaminating proteins pass through the matrix. Chondroitinase is then dissociated from the matrix.
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Messing, Ralph, A., Methods in Enzymology, Vol. XLIV, 1976 (pp. 148-167).
American Cyanamid Company
Barrett Rebecca R.
Naff David M.
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