Document Detail


Heparinase II from Flavobacterium heparinum. Action on chemically modified heparins.
MedLine Citation:
PMID:  2026167     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Five chemically modified heparins were derived from native pig mucosal heparin (pig heparin Is). These were de-N-sulphated heparin (heparin IH), N-acetylheparin (heparin IA), de-N/O-sulphated heparin (heparin IVH), de-O-sulphated heparin (heparin IVs) and de-O-sulphated N-acetyl-heparin (heparin IVA). Their structures were studied by 13C-NMR spectroscopy at 90.56 MHz. Native heparin and the derivatives were incubated with Flavobacterium heparinase II at 25 degrees C. The progress of degradation was followed by the delta A235 and the final composition examined by gel filtration with Bio-Gel P-4. Native heparin (Is) was readily degraded by heparinase II and, with the exception of heparin IVH for which degradation was negligible, the chemically modified derivatives were also degraded. Approximately 90% of the saccharides from heparins Is, IA, IVs and IVA were disaccharides and tetrasaccharides. For heparin IH, which was degraded more slowly, the proportion was 65%. Heparins Is, IVs and IVA underwent initial rapid degradation. The digestion of heparin Ia proceeded rapidly after an initial lag phase. The undegraded polymers produced similar elution profiles from Bio-Gel P-4. Following the action of heparinase II on heparins Is, IA, IVs and IVA, the elution profiles revealed a major peak of disaccharides and minor peaks of higher oligomers. The profile of heparin IH revealed a greater proportion of intermediate-molecular-mass saccharides. Our results demonstrate a broad specificity for heparinase II. It is capable of lysing both N-acetylated and N-sulphated heparins independent of O-sulphation. Heparinase II will also degrade heparin derivatives that are non-N-substituted provided that they are O-sulphated.
Authors:
C F Moffat; M W McLean; W F Long; F B Williamson
Related Documents :
16636727 - Photochemical reactions in the tropospheric aqueous phase and on particulate matter.
16856757 - Photodegradation kinetics of some thiols and thiones in aqueous suspension of zinc oxide.
21737747 - An atp-binding cassette subfamily g full transporter is essential for the retention of ...
22018917 - Impact of ultraviolet-b radiation on planktonic fish larvae: alteration of the osmoregu...
11560377 - An efficient screening approach for anti-microcystis compounds based on knowledge of aq...
19053487 - Zeolite-inspired low-k dielectrics overcoming limitations of zeolite films.
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  European journal of biochemistry / FEBS     Volume:  197     ISSN:  0014-2956     ISO Abbreviation:  Eur. J. Biochem.     Publication Date:  1991 Apr 
Date Detail:
Created Date:  1991-06-10     Completed Date:  1991-06-10     Revised Date:  2007-07-23    
Medline Journal Info:
Nlm Unique ID:  0107600     Medline TA:  Eur J Biochem     Country:  GERMANY    
Other Details:
Languages:  eng     Pagination:  449-59     Citation Subset:  IM    
Affiliation:
Department of Biochemistry, University of Aberdeen, Scotland.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Animals
Chromatography, Gel
Flavobacterium / enzymology*
Heparin Lyase
Magnetic Resonance Spectroscopy
Polysaccharide-Lyases / chemistry*
Sulfuric Acids / chemistry
Swine
Chemical
Reg. No./Substance:
0/Sulfuric Acids; EC 4.2.2.-/Polysaccharide-Lyases; EC 4.2.2.7/Heparin Lyase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  pH-dependent mechanism in the catalysis of prolyl endopeptidase from pig muscle.
Next Document:  Binding of long-chain fatty acids to serum albumin in healthy humans. Relationship to obesity.