Périn J P, Bonnet F, Maillet P, Jollès P
Laboratoire des Protéines (U.A. C.N.R.S. n. 1188), Université de Paris V, France.
Biochem J. 1988 Nov 1;255(3):1007-13. doi: 10.1042/bj2551007.
Human platelet proteoglycan (P.PG) was prepared from a 4 M-guanidinium chloride platelet extract in the presence of proteinase inhibitors. The purification procedure included CsCl-density-gradient centrifugation, DEAE-Sepharose CL-6B ion-exchange chromatography and f.p.l.c. on a Mono Q HR 5/5 column. P.PG was recovered as a polydisperse molecule, but the protein core appeared to be at least 90% homogeneous. This observation could be due to partial proteolysis of the core protein during extraction. The N-terminal sequence of the human P.PG core protein was determined up to residue 66 and was shown to be highly homologous to the propeptide of an embryonic rat yolk-sac tumour proteoglycan (PG19); the significance of this homology is discussed.
人血小板蛋白聚糖（P.PG）是在蛋白酶抑制剂存在的情况下，从4M氯化胍血小板提取物中制备的。纯化过程包括氯化铯密度梯度离心、DEAE-琼脂糖CL-6B离子交换色谱和在Mono Q HR 5/5柱上进行快速蛋白质液相色谱（f.p.l.c.）。P.PG作为一种多分散分子被回收，但蛋白质核心似乎至少90%是均一的。这一观察结果可能是由于提取过程中核心蛋白的部分蛋白水解所致。已确定人P.PG核心蛋白的N端序列直至第66位残基，并显示与胚胎大鼠卵黄囊肿瘤蛋白聚糖（PG19）的前肽高度同源；讨论了这种同源性的意义。
