Moffat C F, Long W F, McLean M W, Williamson F B
Marischal College, University of Aberdeen, Aberdeen, AB9 1AS, Scotland, United Kingdom.
Arch Biochem Biophys. 1997 Feb 15;338(2):201-6. doi: 10.1006/abbi.1996.9745.
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.
目前，人们对制备具有特定且有用生物活性的修饰肝素和类肝素聚合物非常感兴趣。本文证明了一种特别通用的内切多糖裂解酶（肝素酶II）作为一种分析工具的潜力，可用于评估此类聚合物合成过程中发生的化学修饰以及酶活性最终产物的实际一级结构。此外，这项工作拓宽了我们对该酶特异性范围的认识。该研究涉及一种含有非天然N-丙酰基的肝素新型衍生物，它是由去N-硫酸化肝素制备而成的。在整个制备过程中，通过将样品与肝素酶II孵育并用高效液相色谱法分析酶催化降解的产物来跟踪化学修饰的程度。
