Abstract:
:Alkaline phosphatase activity was histochemically localized in adult whiteflies (Bemisia tabaci B biotype, syn. B. argentifolii) with a chromogenic substrate (5-bromo-4-chloro-3-indolylphosphate) and a fluorogenic substrate (ELF-97). The greatest amount of staining was in the basal regions of adult salivary glands with additional activity traced into the connecting salivary ducts. Other tissues that had alkaline phosphatase activity were the accessory salivary glands, the midgut, the portion of the ovariole surrounding the terminal oocyte, and the colleterial gland. Whitefly nymphs had activity in salivary ducts, whereas activity was not detected in two aphid species (Rhodobium porosum and Aphis gossypii). Whitefly diet (15% sucrose) was collected from whitefly feeding chambers and found to have alkaline phosphatase activity, indicating the enzyme was secreted in saliva. Further studies with salivary alkaline phosphatase collected from diet indicated that the enzyme had a pH optimum of 10.4 and was inhibited by 1 mM cysteine and to a lesser extent 1 mM histidine. Dithiothreitol, inorganic phosphate, and ethylenediaminetetraacetic acid (EDTA) also inhibited activity, whereas levamisole only partially inhibited salivary alkaline phosphatase. The enzyme was heat tolerant and retained approximately 50% activity after a 1-h treatment at 65 degrees C. The amount of alkaline phosphatase activity secreted by whiteflies increased under conditions that stimulate increased feeding. These observations indicate alkaline phosphatase may play a role during whitefly feeding.
journal_name
Arch Insect Biochem Physioljournal_title
Archives of insect biochemistry and physiologyauthors
Funk CJdoi
10.1002/arch.1026subject
Has Abstractpub_date
2001-04-01 00:00:00pages
165-74issue
4eissn
0739-4462issn
1520-6327pii
10.1002/arch.1026journal_volume
46pub_type
杂志文章abstract::Insect cellular immune responses include encapsulation, nodule formation, and phagocytosis. Hemichannels and gap junctions are involved in these cellular actions. Innexins (Inxs: analogous to the vertebrate connexins) form hemichannels and gap junctions, but the molecular mechanisms underlying their biology is still u...
journal_title:Archives of insect biochemistry and physiology
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journal_title:Archives of insect biochemistry and physiology
pub_type: 杂志文章
doi:10.1002/arch.940250202
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journal_title:Archives of insect biochemistry and physiology
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journal_title:Archives of insect biochemistry and physiology
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journal_title:Archives of insect biochemistry and physiology
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journal_title:Archives of insect biochemistry and physiology
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journal_title:Archives of insect biochemistry and physiology
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journal_title:Archives of insect biochemistry and physiology
pub_type: 杂志文章
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journal_title:Archives of insect biochemistry and physiology
pub_type: 杂志文章
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更新日期:1992-01-01 00:00:00
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journal_title:Archives of insect biochemistry and physiology
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journal_title:Archives of insect biochemistry and physiology
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journal_title:Archives of insect biochemistry and physiology
pub_type: 杂志文章
doi:10.1002/arch.20332
更新日期:2010-01-01 00:00:00
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journal_title:Archives of insect biochemistry and physiology
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journal_title:Archives of insect biochemistry and physiology
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journal_title:Archives of insect biochemistry and physiology
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journal_title:Archives of insect biochemistry and physiology
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journal_title:Archives of insect biochemistry and physiology
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journal_title:Archives of insect biochemistry and physiology
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journal_title:Archives of insect biochemistry and physiology
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journal_title:Archives of insect biochemistry and physiology
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abstract::Plant protease inhibitors (PIs) are elements of a common plant defense mechanism induced in response to herbivores. The fall armyworm, Spodoptera frugiperda, a highly polyphagous lepidopteran pest, responds to various PIs in its diet by expressing genes encoding trypsins. This raises the question of whether the PI-ind...
journal_title:Archives of insect biochemistry and physiology
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