دورية أكاديمية
أعرض في EDS

Controllable production of low molecular weight heparins by combinations of heparinase I/II/III.

التفاصيل البيبلوغرافية
العنوان: Controllable production of low molecular weight heparins by combinations of heparinase I/II/III.
المؤلفون: Wu J; Key Laboratory for Industrial Biocatalysis of Ministry of Education, Institute of Biochemical Engineering, Department of Chemical Engineering, Tsinghua University, Haidian, Beijing 100084, People's Republic of China. Electronic address: wujingjun2009@foxmail.com., Zhang C, Mei X, Li Y, Xing XH
المصدر: Carbohydrate polymers [Carbohydr Polym] 2014 Jan 30; Vol. 101, pp. 484-92. Date of Electronic Publication: 2013 Sep 23.
نوع المنشور: Journal Article; Research Support, Non-U.S. Gov't
اللغة: English
بيانات الدورية: Publisher: Elsevier Applied Science Publishers Country of Publication: England NLM ID: 8307156 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1879-1344 (Electronic) Linking ISSN: 01448617 NLM ISO Abbreviation: Carbohydr Polym Subsets: MEDLINE
أسماء مطبوعة: Publication: <1992-> : Barking : Elsevier Applied Science Publishers
Original Publication: London [Eng.] : Applied Science Publishers, c1981-
مواضيع طبية MeSH: Heparin/*chemistry , Polysaccharide-Lyases/*metabolism, Heparin Lyase/metabolism ; Molecular Weight ; Polymerization
مستخلص: 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.
(Copyright © 2013 Elsevier Ltd. All rights reserved.)
فهرسة مساهمة: Keywords: 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
المشرفين على المادة: 9005-49-6 (Heparin)
EC 4.2.2.- (Polysaccharide-Lyases)
EC 4.2.2.- (heparinase II)
EC 4.2.2.7 (Heparin Lyase)
EC 4.2.2.8 (heparitinsulfate lyase)
تواريخ الأحداث: Date Created: 20131205 Date Completed: 20140819 Latest Revision: 20131204
رمز التحديث: 20230127
DOI: 10.1016/j.carbpol.2013.09.052
PMID: 24299802
قاعدة البيانات: MEDLINE
الوصف
تدمد:1879-1344
DOI:10.1016/j.carbpol.2013.09.052