Ultrastructural localisation of acid phosphatase, non-specific esterase and β-glucuronidase in the midgut epithelium of Tenebrio molitor, Schistocerca gregaria and Carausius morosus

Histochemie ◽  
1971 ◽  
Vol 28 (3) ◽  
pp. 243-249 ◽  
Author(s):  
D. J. Beadle ◽  
D. C. Livingston ◽  
S. Read
1956 ◽  
Vol 33 (2) ◽  
pp. 311-324
Author(s):  
R. H. DADD

1. In Tenebrio secretion of protease occurs spontaneously after moult and adult emergence, and in response to feeding in the active larva and mature adult. Damp cellulose powder or water are effective in increasing secretion in the adult. 2. Since little enzyme is accumulated in the epithelial tissue when the total midgut enzyme is greatly increased, it is inferred that synthesis and discharge are interdependent. When synthesis (as indicated by comparatively high tissue enzyme) is accelerated, growth of the midgut epithelium occurs. 3. In starved Dytiscus protease is accumulated in the midgut tissue. Within one hour of feeding it is largely discharged into the crop. Protease recurs in the midgut tissue in a few hours, but remains low so long as the crop contains undigested material. When the crop is empty, discharge ceases and enzyme is again accumulated in the epithelium. Thus the process of discharge appears to be independent of synthesis. 4. The secretory mechanisms of Tenebrio and Dytiscus are discussed in relation to their feeding habits.


1968 ◽  
Vol 21 (5) ◽  
pp. 1047 ◽  
Author(s):  
SNH Ashrafi ◽  
MAH Qadri

Acid phosphatase activity was determined biochemically in a homogenate of the digestive tract of the desert locust, S. gregaria. p-Nitrophenol was used as colorimetric standard and disodium p.nitrophenyl phosphate as substrate.


1968 ◽  
Vol 100 (6) ◽  
pp. 649-655 ◽  
Author(s):  
S. N. H. Naqvi ◽  
Shahid H. Ashrafi ◽  
M. A. H. Qadri

AbstractThe acid and alkaline phosphatase activity was measured in the developing egg and in the alimentary canal of aging nymphs as well as adult males and females of different ages. Para-nitrophenol was used as colorimetric standard and disodium p-nitrophenyl phosphate as substrate. Activity was measured in terms of micromoles of p-nitrophenol liberated from the substrate as a result of enzyme action.Acid phosphatase activity was noticed to increase with the embryonic development and was higher than in the case of alkaline phosphatase. The alkaline phosphatase activity was lowest in the freshly laid egg, but increased more sharply than acid phosphatase during embryonic development.The activity of both the acid and alkaline phosphatases was highest in the first instar and declined gradually to the fifth instar. The activity of acid phosphatase was higher than alkaline phosphatase in all stages except the first instar where it was almost equal. The activity of both the enzymes was higher during the intermoulting period and declined at each moult indicating a hormone–enzyme relationship.In adults, activity of both the enzymes increased up to the maturation period after which the activity gradually decreased. Acid phosphatase activity was generally higher in males whereas alkaline phosphatase activity was generally higher in females. In almost all cases, the acid phosphatase activity was found to be higher than the alkaline phosphatase.


2004 ◽  
Vol 51 (1) ◽  
pp. 115-119 ◽  
Author(s):  
Iwona Woźnica ◽  
Wioletta Szeszel-Fedorowicz ◽  
Grzegorz Rosińskiand ◽  
Danuta Konopińska

Continuing our studies on proctolin (Arg-Tyr-Leu-Pro-Thr) we performed the synthesis and biological evaluation of 52 analogues substituted in position 2, 3, 4, and 5 of the peptide chain. The peptides were bioassayed for cardiotropic activity in vitro on Tenebrio molitor and myotropic activity on foregut of Schistocerca gregaria. Twenty analogues retained 20-80% of proctolin activity.


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