Reassessment of changes in substrate specificity of aldolase isozymes during embryogenesis in Bombyx mori
Reassessment of changes in substrate specificity of aldolase isozymes during embryogenesis in Bombyx mori
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家蚕胚胎发生过程中醛缩酶同工酶底物特异性变化的重新评估
DOI：
10.11416/kontyushigen1930.63.171
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发表时间：
1994
期刊：
影响因子：
--
通讯作者：
K. Koga
中科院分区：
文献类型：
--
作者：
S. Nagaoka;Y. Sugimoto;M. Yara;K. Koga
1，6-二磷酸果糖醛缩酶[EC4.1.2.131]是一种糖酵解酶，催化1，6-二磷酸果糖(FBP)的羟醛裂解生成磷酸二羟丙酮和3-磷酸甘油醛。它也作用于1-磷酸果糖(F1P)，对这两种底物的活性比率，后来被命名为FBP/F1P活性比率，是研究醛缩酶同工酶的一个重要指标(Lebherz和Butt，1969)。在家蚕中检测到两种不同类型的醛缩酶，根据酶谱带的迁移率暂定为S和F，并报道了S和F酶显示不同的FBP/F1P活性比率(Sugimoto et al.，1992)。本文对用粗提物测得的FBP/F1P活性比值进行了重新检验。这些新的结果证实，在胚胎发育的后期，S酶被F型酶所取代。
Fructose 1, 6-bisphosphate aldolase [EC 4. 1. 2. 131 , one of the glycolytic enzymes, catalyzes the aldol cleavage of fructose 1, 6-bisphosphate (FBP) for the formation of dihydroxyacetone phosphate and glyceraldehyde 3-phosphate. It acts also on fructose 1phosphate (F1P), and the ratio of activities towards the two substrates, subsequently designated as FBP/F1P activity ratio, is an important index in studies of aldolase isozymes (LEBHERZ and BUTTER, 1969). In the silkworm, Bombyx mori, two distinct types of aldolases, tentatively designated as S and F according to the mobility of the zymogram bands, have been detected and the S and F enzymes were reported to show different FBP /F1P activity ratios (SUGIMOTO et al., 1992). In this paper, the FBP/F1P activity ratios measured by using crude extracts were reexamined. The new results obtained confirmed that the S-type enzyme was replaced by the F-type enzyme at a late stage of embryogenesis.