Weiss T L, Zieske J D, Bernstein I A
Biochim Biophys Acta. 1981 Oct 13;661(2):221-9. doi: 10.1016/0005-2744(81)90007-3.
Fructose-1,6-bisphosphate aldolase (D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate lyase, EC 4.1.2.13) partitions between the microsomes and the cytosol when a rat liver homogenate is fractionated by differential centrifugation. Gel electrophoresis and immunodiffusion indicate that the one isozyme present in the liver of the young adult rat is found in both fractions. The association of the aldolase with membranes is differentially sensitive to a variety of metabolites and inorganic salts. In the absence of cellular salts, 1 mM fructose 1,6-bisphosphate or glucose 1,6-bisphosphate elutes 50% of the enzyme from the microsomes. About 9 mM Pi or citrate is necessary to produce the same effect. With other metabolites or inorganic salts higher concentrations are required. The fraction of total enzyme which partitions with the microsomes when a homogenate is submitted to high speed centrifugation, correlates inversely with the level of fructose 1,6-bisphosphate in the supernatant solution and this concentration is higher when the tissue concentration in the homogenate is greater. The Km for fructose 1,6-bisphosphate of 3 . 10(-4) for aldolase bound to microsomes is decreased to 6 . 10(-6) M when the enzyme is dissociated from the membranes with salt. These observations appear relevant to the ongoing discussion regarding the physiological relevance of the subcellular localization of glycolytic enzymes.
果糖-1,6-二磷酸醛缩酶（D-果糖-1,6-二磷酸D-甘油醛-3-磷酸裂解酶，EC 4.1.2.13）在大鼠肝脏匀浆通过差速离心进行分级分离时，会在微粒体和胞质溶胶之间进行分配。凝胶电泳和免疫扩散表明，成年幼鼠肝脏中存在的一种同工酶在这两个级分中都能找到。醛缩酶与膜的结合对多种代谢物和无机盐具有不同的敏感性。在没有细胞盐的情况下，1 mM果糖1,6-二磷酸或葡萄糖1,6-二磷酸可从微粒体中洗脱50%的酶。产生相同效果大约需要9 mM的磷酸根离子（Pi）或柠檬酸根离子。对于其他代谢物或无机盐，则需要更高的浓度。当匀浆进行高速离心时，与微粒体分配在一起的总酶的比例与上清液中果糖1,6-二磷酸的水平呈负相关，并且当匀浆中的组织浓度较高时，该浓度也较高。与微粒体结合的醛缩酶对果糖1,6-二磷酸的米氏常数（Km）为3×10⁻⁴，当用盐使酶从膜上解离时，该常数降至6×10⁻⁶ M。这些观察结果似乎与正在进行的关于糖酵解酶亚细胞定位的生理相关性的讨论相关。
