Chemistry: molecular biology and microbiology – Enzyme – proenzyme; compositions thereof; process for... – Stablizing an enzyme by forming a mixture – an adduct or a...
Patent
1995-05-17
1999-08-03
Naff, David M.
Chemistry: molecular biology and microbiology
Enzyme , proenzyme; compositions thereof; process for...
Stablizing an enzyme by forming a mixture, an adduct or a...
424 943, 435177, 435180, 435181, 525 541, 514 2, 530402, C12N 996, C12N 1106, C07K 1700, A01N 6300
Patent
active
059324627
ABSTRACT:
Multi-armed, monofunctional, and hydrolytically stable polymers are described having the structure ##STR1## wherein Z is a moiety that can be activated for attachment to biologically active molecules such as proteins and wherein P and Q represent linkage fragments that join polymer arms poly.sub.a and poly.sub.b, respectively, to central carbon atom, C, by hydrolytically stable linkages in the absence of aromatic rings and ester groups in the linkage fragments. R typically is hydrogen or methyl, but can be a linkage fragment that includes another polymer arm. A specific example is an mPEG disubstituted lysine having the structure ##STR2## where mPEG.sub.a and mPEG.sub.b have the structure CH.sub.3 O--(CH.sub.2 CH.sub.2 O).sub.n CH.sub.2 CH.sub.2 -- wherein n may be the same or different for mPEG.sub.a and mPEG.sub.b and can be from 1 to about 1,150 to provide molecular weights of from about 100 to 100,000. The mPEG disubstituted lysine can be purified from a reaction mixture by chromatography in water, including gel filtration chromatography and ion exchange chromatography because the carboxyl group is ionizable. Impurities are removed, including unreacted mPEG and mPEG monosubstituted lysine, to provide the polymer in pure form. Ion exchange chromatography permits fractionation of a greater amount of polymer per run.
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Caliceti Paolo
Harris J. Milton
Schiavon Oddone
Veronese Francesco Maria
Naff David M.
Shearwater Polymers, Inc.
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