Stapleton A M, Simpson R J, Ryall R L
Department of Surgery, Flinders Medical Centre, Australia.
Biochem Biophys Res Commun. 1993 Sep 30;195(3):1199-203. doi: 10.1006/bbrc.1993.2171.
Crystal matrix protein (CMP) is the principal protein found in calcium oxalate (CaOx) crystals precipitated from whole human urine. It is a potent inhibitor of crystal aggregation and may therefore be important in the aetiology of kidney stone disease. CMP was isolated from CaOx crystals by EDTA dissolution and purified by Sephacryl S-200 column chromatography and reversed-phase high pressure liquid chromatography. Edman degradation revealed 81.8% sequence identity of the 11 N-terminal amino acids of CMP with the N-terminus of human prothrombin, which contains 10 gamma-carboxyglutamic acid residues in the first 32 amino acids. The apparent relationship between CMP and prothrombin was confirmed when an antibody to human prothrombin reacted with CMP upon Western blotting of sodium dodecyl sulphate polyacrylamide gels of the protein.
晶体基质蛋白（CMP）是从正常人尿液中沉淀出的草酸钙（CaOx）晶体中发现的主要蛋白质。它是晶体聚集的有效抑制剂，因此可能在肾结石疾病的病因学中起重要作用。通过EDTA溶解从CaOx晶体中分离出CMP，并通过Sephacryl S-200柱色谱法和反相高压液相色谱法进行纯化。埃德曼降解显示，CMP的11个N端氨基酸与人类凝血酶原的N端具有81.8%的序列同一性，后者在前32个氨基酸中含有10个γ-羧基谷氨酸残基。当用抗人凝血酶原抗体对该蛋白质的十二烷基硫酸钠聚丙烯酰胺凝胶进行蛋白质免疫印迹时，该抗体与CMP发生反应，从而证实了CMP与凝血酶原之间的明显关系。
