Gozin D, Ollier-Hartmann M P, Lerable J, Hartmann L, Soulier J P
Biomed Pharmacother. 1983;37(5):228-30.
A purification method for C1 esterase is described. The final product significantly improved the sensitivity and the specificity of the enzymatic measurement of its plasma inhibitor C1-INH or alpha 2-neuraminoglycoprotein (alpha 2-NGP) by esterolysis of a synthetic substrate N-acetyl-L-tyrosine ethyl ester (ALTEe). A comparative study was done between the chromatographed C1 esterase and the native serum euglobulins: qualitative and quantitative determination of the serum contaminants, enzymatic activity measurement of C1-INH in normal subjects and in patients suffering from hereditary angioneurotic oedema (OANH) as well as in therapeutical C1-inhibitor concentrates.
本文描述了一种C1酯酶的纯化方法。最终产物通过合成底物N-乙酰-L-酪氨酸乙酯(ALTEe)的酯解作用,显著提高了其血浆抑制剂C1-INH或α2-神经氨酸糖蛋白(α2-NGP)酶促测定的灵敏度和特异性。对经色谱分离的C1酯酶和天然血清优球蛋白进行了对比研究:对血清污染物进行定性和定量测定,对正常受试者、遗传性血管性水肿(OANH)患者以及治疗用C1抑制剂浓缩物中的C1-INH进行酶活性测定。