Feshchenko S P, Krasnopol'skaia K D, Shishkin S S
Biokhimiia. 1984 Oct;49(10):1679-85.
The components of proteoglycan aggregates--proteoglycan subunits and link proteins from articular cartilage extracts of newborns--were isolated and purified. The content of extracted uronic acids and protein per 1 g of wet weight was 4.77 +/- 0.52 and 3.19 +/- 0.14 mg, respectively. The components of proteoglycan aggregates were isolated and purified by caesium chloride density gradient ultracentrifugation under association and dissociation conditions, as well as by gel filtration on Sephacryl S-200. The uronic acids/protein ratio for proteoglycan subunits was equal to 59.13 +/- 10.19, their relative electrophoretic mobility was 0.54 +/- 0.01 (the mobility of the chondroitin sulfate was taken for unity). The IR spectra of proteoglycan subunits were characterized. Three link proteins with Mr 48 000, 44 000 and 41 500 were isolated from proteoglycan aggregates and characterized. The protein with Mr 48 000 was predominant.
分离并纯化了蛋白聚糖聚集体的成分——来自新生动物关节软骨提取物的蛋白聚糖亚基和连接蛋白。每1克湿重提取的糖醛酸和蛋白质含量分别为4.77±0.52毫克和3.19±0.14毫克。在缔合和解离条件下,通过氯化铯密度梯度超速离心以及在Sephacryl S - 200上进行凝胶过滤,分离并纯化了蛋白聚糖聚集体的成分。蛋白聚糖亚基的糖醛酸/蛋白质比值为59.13±10.19,其相对电泳迁移率为0.54±0.01(硫酸软骨素的迁移率设为1)。对蛋白聚糖亚基的红外光谱进行了表征。从蛋白聚糖聚集体中分离出三种分子量分别为48000、44000和41500的连接蛋白并进行了表征。分子量为48000的蛋白质占主导。