Alkaline phosphatase isozymes in insects and comparison with mammalian enzyme.
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.
Eguchi
M
M
Department of Applied Biology, Kyoto Institute of Technology, Japan.
D000469:Alkaline Phosphatase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D000818:Animals; D007313:Insecta / Q000201:enzymology*; D007527:Isoenzymes / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D008322:Mammals
D007527:Isoenzymes; D000469:Alkaline Phosphatase