Mizutani H, Urist M R
Clin Orthop Relat Res. 1982 Nov-Dec(171):213-23.
A bone morphogenetic protein (BMP) fraction consisting of 17.5K, as well as three other low MW components, was extracted from demineralized bovine bone matrix gelatin under dissociative conditions in 4 M GuHCl. This BMP fraction induces differentiation of mesenchymal cells into cartilage and bone when implanted in the thigh muscles of mice. The 17.5K component is a prime candidate for BMP, but the relationship to the 34K, 24K, and 14K components is not established completely. The 24K component is of special interest, because, when it is present in combination with 17.5K and other components, the resultant preparation has high biologic activity. The 24K component, when isolated from the 17.5K component, had no BMP activity. The 14K component, when isolated from the 17.5K component and all components, had no BMP activity. A 22K components completely isolated by CMC chromatography had no BMP activity. The tasks ahead are to examine further the conditions controlling aggregation of the four low MW glycoproteins and to determine whether it is possible to isolate a single 17.5K homogeneous polypeptide with BMP activity.
在4M盐酸胍的解离条件下，从脱矿牛骨基质明胶中提取出一种由17.5K的骨形态发生蛋白（BMP）组分以及其他三种低分子量组分组成的物质。当将该BMP组分植入小鼠大腿肌肉中时，可诱导间充质细胞分化为软骨和骨。17.5K的组分是BMP的主要候选物，但与34K、24K和14K组分的关系尚未完全明确。24K的组分特别引人关注，因为当它与17.5K及其他组分结合存在时，所得制剂具有高生物活性。从17.5K组分中分离出的24K组分没有BMP活性。从17.5K组分及所有组分中分离出的14K组分没有BMP活性。通过羧甲基纤维素色谱法完全分离出的22K组分没有BMP活性。接下来的任务是进一步研究控制这四种低分子量糖蛋白聚集的条件，并确定是否有可能分离出具有BMP活性的单一17.5K同源多肽。
