Digestive enzymes in midgut cells, endo‐and ectoperitrophic contents, and peritrophic membranes of Spodoptera frugiperda (lepidoptera) larvae

生物 中肠 生物化学 氨肽酶 羧肽酶 胰蛋白酶 淀粉酶 二肽酶 夜蛾 氨基酸 亮氨酸 植物 幼虫 基因 重组DNA
作者
Clélia Ferreira,Adriana N. Capella,Roberta Sitnik,Walter R. Terra
出处
期刊:Archives of Insect Biochemistry and Physiology [Wiley]
卷期号:26 (4): 299-313 被引量:79
标识
DOI:10.1002/arch.940260406
摘要

Abstract In the midgut of Spodoptera frugiperda larvae, subcellular fractionation data suggest that aminopeptidase and part of amylase, carboxypeptidase A, dipeptidase, and trypsin are bound to the microvillar membranes; that major amounts of soluble dipeptidase, cellobiase, and maltase are trapped in the cell glycocalyx; and finally that soluble carboxypeptidase, amylase, and trypsin occur in intracellular vesicles. Most luminal acetylglucosaminidase is soluble and restricted to the ectoperitrophic contents. Aminopeptidase occurs in minor amounts bound to membranes both in the ectoperitrophic contents and incorporated in the peritrophic membrane. Amylase, carboxypeptidase A, and trypsin are found in minor amounts in the ectoperitrophic contents (both soluble and membrane‐bound) and in major amounts in the peritrophic membrane with contents. Part of the activities recovered in the last mentioned contents corresponds to enzyme molecules incorporated in the peritrophic membrane. The results suggest that initial digestion is carried out in major amounts by enzymes in the endoperitrophic space and, in minor amounts, by enzymes immobilized in the peritrophic membrane. Intermediate and final digestion occur at the ectoperitrophic space or at the surface of midgut cells. The results also lend support to the hypothesis that amylase and trypsin are derived from membrane‐bound forms, are released in soluble form by a microapocrine mechanism, and are partly incorporated into the peritrophic membrane. © 1994 Wiley‐Liss, Inc.
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