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核心技术专利：CN118964589B侵权必究

核心技术专利：CN118964589B侵权必究

van Heusden M C, van der Horst D J, van Doorn J M, Beenakkers A M

Department of Experimental Zoology, University of Utrecht, The Netherlands.

Comp Biochem Physiol B. 1987;88(2):523-7. doi: 10.1016/0305-0491(87)90338-5.

An attempt was made to purify lipoprotein lipase (LpL) from the flight muscle of the migratory locust based on affinity for heparin, which is known to avidly bind mammalian LpL. 2. However, locust LpL appeared to completely lack this property, which indicates that the suggested membrane-binding of locust LpL is very different from that of mammalian LpL: a heparin-like glycosaminoglycan is not involved. 3. Since locust LpL lacks heparin affinity, other purification methods were assayed. Solubilization of locust LpL was obtained by the detergent Tween 20. 4. Though both anion and cation exchange chromatography resulted in the complete loss of enzyme activity, partial purification of locust LpL was achieved by gel filtration chromatography.

基于对肝素的亲和力，人们尝试从飞蝗的飞行肌肉中纯化脂蛋白脂肪酶（LpL），已知肝素能强烈结合哺乳动物LpL。2. 然而，蝗虫LpL似乎完全缺乏这种特性，这表明蝗虫LpL的假定膜结合与哺乳动物LpL的膜结合非常不同：不涉及类肝素糖胺聚糖。3. 由于蝗虫LpL缺乏肝素亲和力，因此对其他纯化方法进行了测定。用去污剂吐温20可使蝗虫LpL溶解。4. 尽管阴离子和阳离子交换色谱法都会导致酶活性完全丧失，但通过凝胶过滤色谱法可实现蝗虫LpL的部分纯化。

van Heusden M C, van der Horst D J, van Doorn J M, Beenakkers A M

Department of Experimental Zoology, University of Utrecht, The Netherlands.

Comp Biochem Physiol B. 1987;88(2):523-7. doi: 10.1016/0305-0491(87)90338-5.

An attempt was made to purify lipoprotein lipase (LpL) from the flight muscle of the migratory locust based on affinity for heparin, which is known to avidly bind mammalian LpL. 2. However, locust LpL appeared to completely lack this property, which indicates that the suggested membrane-binding of locust LpL is very different from that of mammalian LpL: a heparin-like glycosaminoglycan is not involved. 3. Since locust LpL lacks heparin affinity, other purification methods were assayed. Solubilization of locust LpL was obtained by the detergent Tween 20. 4. Though both anion and cation exchange chromatography resulted in the complete loss of enzyme activity, partial purification of locust LpL was achieved by gel filtration chromatography.

基于对肝素的亲和力，人们尝试从飞蝗的飞行肌肉中纯化脂蛋白脂肪酶（LpL），已知肝素能强烈结合哺乳动物LpL。2. 然而，蝗虫LpL似乎完全缺乏这种特性，这表明蝗虫LpL的假定膜结合与哺乳动物LpL的膜结合非常不同：不涉及类肝素糖胺聚糖。3. 由于蝗虫LpL缺乏肝素亲和力，因此对其他纯化方法进行了测定。用去污剂吐温20可使蝗虫LpL溶解。4. 尽管阴离子和阳离子交换色谱法都会导致酶活性完全丧失，但通过凝胶过滤色谱法可实现蝗虫LpL的部分纯化。