Multiple forms of midgut alkaline phosphatase in the silkworm: Separation and comparison of two isoenzymes

Eguchi, Masaharu; Sawaki, Masahiko; Suzuki, Yasutaka

doi:10.1016/0020-1790(72)90050-9

Cited by 26 publications

(5 citation statements)

References 15 publications

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“…ALPs can be divided into two groups: soluble (s-ALP) and membranebound (m-ALP) (Eguchi et al, 1972;Azuma and Eguchi, 1989;Itoh et al, 1999). In insects, both ALPs are found in larval midgut epithelium cells; however, they are expressed in different cell types.…”

Section: Introductionmentioning

confidence: 99%

Functional expression in insect cells of glycosylphosphatidylinositol-linked alkaline phosphatase from Aedes aegypti larval midgut: A Bacillus thuringiensis Cry4Ba toxin receptor

Dechklar

Tiewsiri

Angsuthanasombat

et al. 2011

Insect Biochemistry and Molecular Biology

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Section: Introductionmentioning

confidence: 99%

Functional expression in insect cells of glycosylphosphatidylinositol-linked alkaline phosphatase from Aedes aegypti larval midgut: A Bacillus thuringiensis Cry4Ba toxin receptor

Dechklar

Tiewsiri

Angsuthanasombat

et al. 2011

Insect Biochemistry and Molecular Biology

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“…It is located in the midgut, Malpighian tube, muscles, nerve fibres and silk glands of the silkworm, Bombyx mori L. (H ORIE , 1958). The midgut has the highest ALKP activity among these tissues (E GUCHI et al, 1972, 1990; O KADA et al., 1989). The activity of these enzymes is related to the physiological situation of silkworms and reflects the absorption, digestion and positive transportation of nutrients in the midgut (Y OSHITAKE , 1966; E GUCHI and I WAMOTO , 1975; E GUCHI et al, 1990).…”

Section: Introductionmentioning

confidence: 99%

Studies on the activity of the alkaline phosphatase in the midgut of infected silkworm, Bombyx mori L.

Miao

2002

J Applied Entomology

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The effects of several factors on the activity of alkaline phosphatase (ALKP) in the midgut of the silkworm, Bombyx mori L were studied. The ALKP activity varied greatly among the tested strains. There was positive correlation between ALKP activity and cocoon quality. The ALKP activity of the midgut decreased when the silkworm was infected with cytoplasmic polyhedrosis virus (CPV); whereas, infection with nuclear polyhedrosis virus (NPV) did not affect ALKP activity. This suggests that the pathogenic mechanism of CPV differs from that of NPV. Bacillus thuringiensis caused direct damage to the midgut tissues of the silkworm with a rapid decline in ALKP activity. Activation of ALKP by Mg2+ was more evident than the other chemicals. Ascorbic acid, Ca2+, citric acid and Cl– were inhibitory to ALKP in vitro.

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“…The appearance of multiple phosphatase activity bands in P. varians and I. balthica extracts could represent isoenzymes, which can be expressed under certain dietary conditions (Guérin and Kerambrun 1982). Eguchi et al (1972) found isoforms of alkaline phosphatase in the silkworm Bombyx mori and Lee and Chuang (1991) found three isoforms of alkaline phosphatase in the shrimp Penaeus monodon, one having a molecular mass of 43 kDa and the other two of 31 kDa. These molecular masses are similar to those of phosphatases from the shrimp faeces and digestive tissue extracts (40 kDa and 33 kDa).…”

Section: Functional Propertiesmentioning

confidence: 99%

Extracellular phosphoesterases of invertebrate origin: underrated actors in phosphorus recycling?

Böök

Saborowski

2020

Mar Biol

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Extracellular enzymes contribute substantially to the remineralisation of organic matter in aquatic systems. Marine invertebrates release endogenous enzymes through activities such as sloppy feeding or egestion, but the significance of such processes is widely unexplored. We compared functional key properties such as activity, stability, and apparent molecular masses of extracellular phosphatases from faeces of the marine crustaceans Idotea balthica, Palaemon varians, and Homarus gammarus with those of their digestive organs. A fluorescent substrate was used to examine enzyme activity qualitatively on agarose plates and quantitatively in microplate assays. Apparent molecular masses and enzyme stability were examined by native substrate gel electrophoresis (NSGE). Active extracellular phosphatase were present in the faeces of all tested species. NSGE activity band patterns were similar in digestive tissue extracts and faeces extracts. The initial enzyme activity retained for about 2 days, but thereafter rapidly decreased. Activity band patterns of digestive organs and faeces of I. balthica remained consistent for up to 72 h. Antibiotic treatment did not reduce phosphatase activity in the faeces of I. balthica and H. gammarus but in the faeces P. varians. Because of the comparatively high activities in the faeces, the electrophoretic similarity between faeces and digestive organs, and the limited durability of the enzymes in faeces extracts, we conclude that the studied crustaceans release predominantly endogenous, rather than bacterial phosphatases through faeces. These can substantially contribute to the pool of active extracellular phosphatases and the recycling of phosphorus in aquatic systems. The wider physiological and ecological context is discussed.

show abstract

Multiple forms of midgut alkaline phosphatase in the silkworm: Separation and comparison of two isoenzymes

Cited by 26 publications

References 15 publications

Functional expression in insect cells of glycosylphosphatidylinositol-linked alkaline phosphatase from Aedes aegypti larval midgut: A Bacillus thuringiensis Cry4Ba toxin receptor

Functional expression in insect cells of glycosylphosphatidylinositol-linked alkaline phosphatase from Aedes aegypti larval midgut: A Bacillus thuringiensis Cry4Ba toxin receptor

Studies on the activity of the alkaline phosphatase in the midgut of infected silkworm, Bombyx mori L.

Extracellular phosphoesterases of invertebrate origin: underrated actors in phosphorus recycling?

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