CYTOCHEMICAL INVESTIGATION OF THE INTESTINAL 

 PHOSPHATASES AND ESTERASES DURING DEVELOPMENT OF 

 GALLERIA MALLONELLA L. 



Цитохимические исследования фосфатаз и эстераз кишечника 

 восковой моли в течение онтогенеза 



А. PRZELECKA, М. SARZALA, А. WRO^ЧSZEWSKA and W. ZAWADZKA 



(Department of Biochemistry, Nencki Intitute of Experimental Biology, 

 Warsaw and Department of Animal Physiology, University of Warsaw, Poland) 



The alimentary canal of Galleria mellonella lan^ae, pupae and adults was 

 investigated for phosphatases and esterases activity. Cold formalin fixed 

 frozen sections were used. Both alkaline and acid phosphatases were detected 

 by the Gomori method (1953) — glycerophosphate as substrate (and by diazo 

 — coupling method) sodium salt of a — naphtyl phosphate as substrate — 

 after Pearse (1954). Esterases were detected by means of three groups of 

 substrates: 1. Tweens 20, 40, 60 and 80 (Gomori, 1953); 2. acetate esters of 

 naphtol and its derivatives, which couple after hydrolysis with corresponding 

 diazo salts; 3. 5-Bromoindoxyl acetate which gives indigo deposits as the reac- 

 tion products (Pearse, 1954). 



By means of all the methods used a specific distribution of the investigated 

 enzymes along the alimentary tract of feeding larvae was found. The midgut 

 epithelial cells showed a strong enzymatic activity against all the mentioned 

 substrates (Fig. I), лvhereas the foregut and hindgut remained rather inactive. 

 The alkaline phosphatase лтав localized chiefly in the apical part od the cells 

 and on the fresh border (Fig. I — 1), the acid phosphatase was present in the 

 cell nuclei (Fig. 1—5). 



Esterases were dispersed throughout the cytoplasm (Fig. I — 2, 3, 4, 6, 7, 8). 

 No differences were found between the localization of the esterases which hydro- 

 lyse the esters of acetic acid (Fig. 1 — 2 and 6) and those which splitt the esters 

 of long chained fatty acids (Fig. I — 3, 4, 7 and 8). No esterase activity was 

 found in the cell nuclei. 



The moulting causes some changes in the enzymatic activity of the intestinal 

 tract (Figs. II and III). Just before the moulting takes place the esterases 

 which hydrolize the esters of the long chained fatty acids, esp. Tween 80, 

 seem to be much less active than during the period of growth (Fig. II — 10 and 

 11). On the other hand, however, the esterases which split the Naphtol AS 

 acetate do not show a corresponding diminution in their activity (Fig. II —9). 



The decrease in the activity of the alkaline phosphatase during moulting 



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