Eguchi M
Department of Applied Biology, Kyoto Institute of Technology, Japan.
Comp Biochem Physiol B Biochem Mol Biol. 1995 Jun;111(2):151-62. doi: 10.1016/0305-0491(94)00248-s.
Studies of insect alkaline phosphatases (ALPs) are reviewed, including general insect isozyme papers from earlier periods. Results of biochemical and genetic investigations of the silkworm midgut ALPs are described. The membrane-bound (m-ALP) and soluble form (s-ALP) are controlled by distinct genes on the same chromosome. These isozymes were different in tissue localization, antigenicity, stability under alkaline conditions and sugar chains. Compared with mammalian ALPs, silkworm ALPs represented specificity in the monomeric structure, tissue localization and inhibition by amino acids. The amino acid sequence deduced from cDNA sequence of silkworm m-ALP showed 42.7-44.6% homology to three human types of ALP. Comparison of the amino acid sequences in functionally important parts of various ALP isozymes showed a significant conservation. Physiological roles of ALPs were discussed and the significance of the study in temporal and spatial regulations of both silkworm ALP genes was pointed out. In addition, the evolutionary relationship among various genes was discussed.
本文综述了昆虫碱性磷酸酶（ALP）的研究，包括早期的一般昆虫同工酶论文。描述了家蚕中肠碱性磷酸酶的生化和遗传研究结果。膜结合型（m-ALP）和可溶性形式（s-ALP）由同一染色体上的不同基因控制。这些同工酶在组织定位、抗原性、碱性条件下的稳定性和糖链方面存在差异。与哺乳动物碱性磷酸酶相比，家蚕碱性磷酸酶在单体结构、组织定位和氨基酸抑制方面表现出特异性。从家蚕m-ALP的cDNA序列推导的氨基酸序列与三种人类碱性磷酸酶类型具有42.7-44.6%的同源性。对各种碱性磷酸酶同工酶功能重要部分的氨基酸序列比较显示出显著的保守性。讨论了碱性磷酸酶的生理作用，并指出了该研究在家蚕碱性磷酸酶基因时空调控中的意义。此外，还讨论了各种基因之间的进化关系。
