Reznick A Z, Gershon D
Mech Ageing Dev. 1977 Sep-Oct;6(5):345-53. doi: 10.1016/0047-6374(77)90036-7.
Fructose-1,6-diphosphate aldolase has been purified to homogeneity 62.0 and 58.3 fold from young and old nematodes respectively. The aldolase preparations from young (7 days) and old (35 days) animals are indistinguishable in their electrophoretic mobility, molecular weight of the tetramer (158,000) and monomer (40,000), and Km, although the "old" enzyme is more heat stable than the "young" enzyme. Enzyme from old animals has only about 55% specific activity per mg purified protein of the "young" enzyme and its catalytic activity per unit of enzyme antigen is about 50% of that of the enzyme from young animals. Immunological identity of purified enzyme from old and young animals was established by the Ouchterlony technique by antiserum produced against purified "young" enzyme and antiserum against purified "old" enzyme. Thus, this work shows for the first time that the altered form of an enzyme which appears in senescent animals apparently does not possess extra antigenic sites which are acquired as a function of age.
果糖-1,6-二磷酸醛缩酶分别从幼年和老年线虫中纯化至均一，纯化倍数分别为62.0倍和58.3倍。来自幼年（7天）和老年（35天）动物的醛缩酶制剂在电泳迁移率、四聚体（158,000）和单体（40,000）的分子量以及米氏常数方面没有区别，尽管“老年”酶比“幼年”酶更耐热。老年动物的酶每毫克纯化蛋白的比活性仅为“幼年”酶的约55%，其每单位酶抗原的催化活性约为幼年动物酶的50%。通过免疫双扩散技术，用针对纯化的“幼年”酶产生的抗血清和针对纯化的“老年”酶产生的抗血清，确定了老年和幼年动物纯化酶的免疫同一性。因此，这项工作首次表明，衰老动物中出现的酶的改变形式显然不具有随年龄增长而获得的额外抗原位点。
