DIGESTIVE ENZYMES IN MIDGUT CELLS, ENDOPERITROPHIC AND ECTOPERITROPHIC CONTENTS, AND PERITROPHIC MEMBRANES OF SPODOPTERA-FRUGIPERDA (LEPIDOPTERA) LARVAE
C. Ferreira et al., DIGESTIVE ENZYMES IN MIDGUT CELLS, ENDOPERITROPHIC AND ECTOPERITROPHIC CONTENTS, AND PERITROPHIC MEMBRANES OF SPODOPTERA-FRUGIPERDA (LEPIDOPTERA) LARVAE, Archives of insect biochemistry and physiology, 26(4), 1994, pp. 299-313
In the midgut of Spodoptera frugiperda larvae, subcellular fractionati
on data suggest that am in opeptidase and part of amylase, carboxypept
idase A, dipeptidase, and trypsin are bound to the microvillar membran
es; that major amounts of soluble dipeptidase, cellobiase, and maltase
are trapped in the cell glycocalyx; and finally that soluble carboxyp
eptidase, amylase, and trypsin occur in intracellular vesicles. Most l
uminal acetylglucosaminidase is soluble and restricted to the ectoperi
trophic contents. Aminopeptidase occurs in minor amounts bound to memb
ranes both in the ectoperitrophic contents and incorporated in the per
itrophic membrane. Amylase, carboxypeptidase A, and trypsin are found
in minor amounts in the ectoperitrophic contents (both soluble and mem
brane-bound) and in major amounts in the peritrophic membrane with con
tents. Part of the activities recovered in the last mentioned contents
corresponds to enzyme molecules incorporated in the peritrophic membr
ane. The results suggest that initial digestion is carried out in majo
r amounts by enzymes in the endoperitrophic space and, in minor amount
s, by enzymes immobilized in the peritrophic membrane. Intermediate an
d 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 releas
ed in soluble form by a microapocrine mechanism, and are partly incorp
orated into the peritrophic membrane. (C) 1994 Wiley-Liss, Inc.