Nakano M, Tauchi H
Institute for Medical Science of Aging, Aichi Medical University, Japan.
Mech Ageing Dev. 1988 Oct;45(1):51-8. doi: 10.1016/0047-6374(88)90018-8.
Renal brush border enzyme activities were significantly decreased with age. The decrease was observed in the homogenate and brush border fractions. Purified leucine aminopeptidase was significantly decreased in Vmax and Km value for leucyl-beta-naphthylamide in the old rats. Heat stability of leucine aminopeptidase from both old and young rats showed biphasic, and the enzyme from old rats was more stable at 60 degrees C than that of the young. However, other properties such as molecular weight, antigenicity, charge, and optimum pH were not significantly different between young and old rats. From these results, it is suggested that age-related alteration of leucine aminopeptidase is due to a conformational change of enzyme molecule; the conformational change might occur at the active sites of the enzyme.
肾刷状缘酶活性随年龄增长显著降低。在匀浆和刷状缘组分中均观察到这种降低。老年大鼠中纯化的亮氨酸氨肽酶对亮氨酰-β-萘酰胺的Vmax和Km值显著降低。老年和幼年大鼠的亮氨酸氨肽酶热稳定性均呈双相性,且老年大鼠的酶在60℃时比幼年大鼠的酶更稳定。然而,老年和幼年大鼠之间的其他性质,如分子量、抗原性、电荷和最适pH值没有显著差异。从这些结果表明,亮氨酸氨肽酶与年龄相关的改变是由于酶分子的构象变化;这种构象变化可能发生在酶的活性位点。