叶片细胞质果糖-1,6-二磷酸酶：低温胁迫的潜在靶标位点。
Leaf Cytosolic Fructose-1,6-bisphosphatase : A Potential Target Site in Low Temperature Stress.
机构信息
Division of Molecular Plant Biology, University of California, Berkeley, California 94720.
出版信息
Plant Physiol. 1983 May;72(1):259-61. doi: 10.1104/pp.72.1.259.
Leaf cytosolic fructose-1,6-bisphosphatase (FBPase), partially purified from both spinach (Spinacia oleracea, var Hipack) and peas (Pisum sativum, var Progress No. 9), is reversibly inactivated by exposure to low temperature. Thus, even though assays were conducted at 22 degrees C, samples incubated at 0 to 12 degrees C had greatly reduced activity relative to controls maintained at 22 degrees C. Following incubation at 22 degrees C prior to assay, the inactivated samples regained their initial activity. Chloroplast FBPase, by contrast, was unaffected by low temperature treatment. This feature as well as lack of a response of cytosolic FBPase to thioredoxins f or c(f) and to chloroplast FBPase antibody indicate that the FBPase isozymes of leaves are different proteins.
从菠菜（Spinacia oleracea，var Hipack）和豌豆（Pisum sativum，var Progress No. 9）中部分纯化的叶质体果糖-1,6-二磷酸酶（FBPase），在低温下会发生可逆失活。因此，即使在 22°C 下进行测定，在 0 至 12°C 下孵育的样品相对于在 22°C 下保持的对照物的活性大大降低。在测定之前于 22°C 下孵育后，失活的样品恢复其初始活性。相比之下，叶绿体 FBPase 不受低温处理的影响。该特征以及细胞质 FBPase 对硫氧还蛋白 f 或 c(f)和叶绿体 FBPase 抗体没有反应表明，叶片的 FBPase 同工酶是不同的蛋白质。
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