Granström G, Mångs H
Department of Histology, University of Gothenburg, Sweden.
Acta Odontol Scand. 1988 Oct;46(5):273-9. doi: 10.3109/00016358809004777.
Type MM phosphoglycerate mutase from free dissected mandibular processes from embryonic rats was reversibly inactivated by tetrathionate, p-chloromercuribenzoate, and Hg2+. Titration with p-chloromercuribenzoate showed the existence of two sulfhydryl groups per enzyme subunit, the modification of which produced a progressive decline in enzyme activity. The apparent Km values for substrate and cofactor were not affected by tetrathionate treatment. Phosphoglycerate mutase inactivated by tetrathionate and by p-chloromercuribenzoate was unable to form the functionally active phosphorylenzyme when mixed with glycerate-2,3-P2. Glycerate-2,3-P2 protected against tetrathionate but failed to protect against Hg2+ and p-chloromercuribenzoate.
从胚胎大鼠游离解剖的下颌突中提取的MM型磷酸甘油酸变位酶可被连四硫酸盐、对氯汞苯甲酸和Hg2+可逆性失活。用对氯汞苯甲酸滴定表明每个酶亚基存在两个巯基,其修饰会导致酶活性逐渐下降。底物和辅因子的表观Km值不受连四硫酸盐处理的影响。被连四硫酸盐和对氯汞苯甲酸失活的磷酸甘油酸变位酶与甘油酸-2,3-P2混合时无法形成功能活性的磷酰化酶。甘油酸-2,3-P2可防止连四硫酸盐的失活作用,但不能防止Hg2+和对氯汞苯甲酸的失活作用。