A phosphatase of undefined function is common to the photoreceptive microvilli of several arthropod species |
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Authors: | Dr Stephen C Trowell Alison McLean Margrit Carter Diane T Davis |
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Institution: | (1) Developmental Neurobiology Group, Research School of Biological Sciences, The Australian National University, Canberra, Australia;(2) University Transmission Electron Microscope Unit, Research School of Biological Sciences, The Australian National University, Canberra, Australia;(3) Molecular Biology Section, CSIRO Division of Entomology, G.P.O. Box 1700, 2601 Canberra, ACT, Australia |
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Abstract: | Summary It has previously been demonstrated, using an ultracytochemical technique, that the photoreceptive microvilli of crab retinae contain a magnesium-dependent phosphatase that hydrolyses the artificial substrate 4-nitrophenylphosphate. Whilst many phosphatases hydrolyse 4-nitrophenylphosphate, the properties of the microvillar enzyme indicated that it is not a conventional acid or alkaline phosphatase. Using the same technique, it is now shown that a similar activity resides in the rhabdomeric microvilli of both the lateral compound eye and the ventral photoreceptors of Limulus polyphemus as well as in the compound eyes of the freshwater crayfish Cherax destructor and the fly Lucilia cuprina. Control cytochemical procedures performed on crayfish and fly showed that in these species too the activity is magnesium-dependent and is not due to a Na+/K+ ATPase. |
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Keywords: | 4-Nitrophenylphosphatase Cytochemistry Phototransduction Photoreceptor cells invertebrate Limulus polyphemus (Chelicerata) Cherax destructor (Crustacea) Lucilia cuprina (Insecta) |
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