Brand H S, Korver G H, van de Stadt R J, van Kampen G P, van der Korst J K
Jan van Breemen Instituut, Amsterdam.
Biol Chem Hoppe Seyler. 1990 Jul;371(7):581-7. doi: 10.1515/bchm3.1990.371.2.581.
Large proteoglycan monomers and small dermatan sulfate proteoglycans were extracted from explants of bovine articular cartilage with increasing (0-4 M) concentrations of guanidinium chloride (GuHCl). The first extractions were followed by a second extraction with 4 M GuHCl. The amount of proteoglycans extracted in the first buffer depended on the GuHCl concentration. At low concentrations of GuHCl, a relatively high amount of small proteoglycans was obtained. Fifty percent of the small proteoglycans was extracted in buffer with 0.85 M GuHCl, while 2.0-2.2 M GuHCl was needed to extract half of the large proteoglycans. Immediately after synthesis, 35S-labeled large proteoglycans were extracted much easier (50% at 1.4 M GuHCl), and those extracted at low concentrations of GuHCl were less capable of aggregation with hyaluronic acid. After 7 days of 'chase' these differences between endogenous and 35S-labeled proteoglycans had disappeared.
用浓度递增（0 - 4M）的盐酸胍（GuHCl）从牛关节软骨外植体中提取大分子蛋白聚糖单体和小分子硫酸皮肤素蛋白聚糖。首次提取后，再用4M GuHCl进行二次提取。首次缓冲液中提取的蛋白聚糖量取决于GuHCl浓度。在低浓度GuHCl时，可获得相对大量的小分子蛋白聚糖。50%的小分子蛋白聚糖在含0.85M GuHCl的缓冲液中被提取出来，而提取一半的大分子蛋白聚糖则需要2.0 - 2.2M GuHCl。合成后立即提取的35S标记大分子蛋白聚糖要容易得多（在1.4M GuHCl时提取50%），且在低浓度GuHCl下提取的那些与透明质酸聚集的能力较弱。经过7天的“追踪”，内源性和35S标记蛋白聚糖之间的这些差异消失了。
