ISSN:
0025-116X
Schlagwort(e):
Chemistry
;
Polymer and Materials Science
Quelle:
Wiley InterScience Backfile Collection 1832-2000
Thema:
Chemie und Pharmazie
,
Physik
Notizen:
Biodegradation of homopolymers, poly-α-[Nγ-(2-hydroxyethyl)-L-glutamine] and poly-α-[Nγ-(2-hydroxypropyl)-L-glutamine], and of copolymers, poly-α-[Nγ-(2-hydroxyethyl)-L-glutamine-co-L-phenylalanine] with 3.7, 5.6, and 10.2 mol-% of Phe units was studied in vitro using pronase E, chymotrypsin A4 and extracts from native tissues. Gel permeation chromatography was used for evaluating the molecular-weight distribution of the original and partially degraded polymers. Homopolymers of Nγ-(2-hydroxyalkyl)-L-glutamines are biodegradable in the main chain by pronase as well as by native tissue extracts, yielding low-molecular-weight products. Although chymotrypsin does not catalyze hydrolysis of peptide bonds in the homopolymers, incorporation of phenylalanine units in the main chain by copolymerization renders the copolymer degradable by this enzyme, most probably in phenylalanyl-glutamine bonds.
Zusätzliches Material:
4 Ill.
Materialart:
Digitale Medien
URL:
http://dx.doi.org/10.1002/macp.1985.020091985117
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