关键词： 2-O-sulfo-α-l-iduronic acid 3,6-di-O-sulfo-N-sulfo-α-d-glucosamine 6-O-sulfo-N-sulfo-α-d-glucosamine 6-O-sulfo-α-d-N-acetylglucosamine AT-III Enzymatic depolymerization GPC GlcA GlcNAc GlcNAc6S GlcNS GlcNS3S6S GlcNS6S H-d-phenylalanyl-l-pipecolyl-arginine-p-nitroaniline dihydrochloride HIT HPLC HepI HepII HepIII Heparin Heparinases IPTG IdoA IdoA2S LC–MS LMWHs Low molecular weight heparin M(n) M(w) MBP N-sulfo-α-d-glucosamine N-α-benzyloxycarbonyl-d-arginyl-l-glycyl-l-arginine-p-nitroaniline-dihydrochloride PA PAGE RI S-2238 S-2765 UV antithrombin III degree of polymerization dp gel permeation chromatography heparin-induced thrombocytopenia heparinase I heparinase II heparinase III high performance chromatography isopropyl-β-d-1-thiogalactopyranoside liquid chromatography–mass spectrometry low molecular weight heparins maltose binding protein number average molecular weight photodiode array polyacrylamide gel electrophoresis refractive index ultraviolet weight average molecular weight α-d-N-acetylglucosamine α-l-iduronic acid β-d-glucuronic acid

Mesh ： Heparin / chemistry Heparin Lyase / metabolism Molecular Weight Polymerization Polysaccharide-Lyases / metabolism

来  源：   DOI：10.1016/j.carbpol.2013.09.052

Abstract：
Enzymatic depolymerization of heparin by heparinases is promising for production of low molecular weight heparins (LMWHs) as anticoagulants, due to its mild reaction conditions and high selectivity. Here, different heparinase combinations were used to depolymerize heparin. Heparinase I and heparinase II can depolymerize heparin more efficiently than heparinase III, respectively, but heparinase III was the best able to protect the anticoagulant activities of LMWHs. Heparinase III and heparinase I/II combinations were able to efficiently depolymerize heparin to LMWHs with higher anticoagulant activity than the LMWHs produced by the respective heparinase I and heparinase II. HepIII and HepI is the best combination for maintaining high anti-IIa activity (75.7 ± 4.21 IU/mg) at the same Mw value. Furthermore, considering both the changes in molecular weight and anticoagulant activity, the action patterns of heparinase I and heparinase II were found not to follow the exolytic and processive depolymerizing mechanism from the reducing end of heparin.
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