Heparinase-II-catalyzed degradation of N-propionylated heparin.
Currently there is great interest in the preparation of modified heparins and heparin-like polymers that possess specific and useful bioactivities. This paper demonstrates the potential of a particularly versatile endopolysaccharide lyase (heparinase II) as an analytical tool with which to assess both the chemical modification occurring during synthesis of such polymers and the actual primary structure of the final product of the enzyme activity. Additionally, the work widens our knowledge of the specificity range of this enzyme. The study involved a novel derivative of heparin containing the unnatural N-propionyl group, which was prepared from de-N-sulfated heparin. The extent of the chemical modification was followed throughout the preparation process by incubating samples with heparinase II and analyzing, with HPLC, the products of degradation catalyzed by the enzyme.
Moffat
C F
CF
Marischal College, University of Aberdeen, Aberdeen, AB9 1AS, Scotland, United Kingdom.
Long
W F
WF
McLean
M W
MW
Williamson
F B
FB
D000215:Acylation; D005417:Flavobacterium / Q000201:enzymology; D006493:Heparin / Q000031:analogs & derivatives* / Q000737:chemistry / Q000378:metabolism; D019763:Heparin Lyase; D009682:Magnetic Resonance Spectroscopy; D011133:Polysaccharide-Lyases / Q000378:metabolism*; D011422:Propionates; D013329:Structure-Activity Relationship
D011422:Propionates; D006493:Heparin; D011133:Polysaccharide-Lyases; D019763:Heparin Lyase