By D. A. Murray
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The substrates were a and 3 naphthyl acetate. The determination of hydrolized substrates as a and 3 naphthol was performed with Fast Red TR, after the reaction was stopped by adding absolute ethanol. The developed dye, extracted in ethyl acetate, was aestimated spectrophotometrically at 490 nm. Protein determination was performed by the Bradford micromethod (1976). Fig. 1 show the calibration curve. Fig. 1. Calibration of protein content RESULTS In Figs. 2 and 3 are shown the calibration for a and 3 naphthol.
Pittkau, D. P. und P. Reiss (1978). In J. ), Limnofauna Europaea, Gustav Pischer Verlag Stuttgart, pp. 429-430. Keyl, H. G. (i960). Arch. Hydrobiol. 5 7 , 187-195. Keyl, H. G. (1961). Arch. Hydrobiol. 58, 1-6. Keyl, H. G. (1962). ) 1 3 , 464-514. Keyl, H. G. und I. Keyl (1959). Arch, gydrobiol. 56. 43-57. Klötzli, A. M. (1974). Arch. Hydrobiol. 7 4 , 68-81. Krieger-Wolff, E. und W. Wülker (1971). Beitr. naturk. Porsch. SüdwDtl. 2 0 , 133-145. Lenz, P. (1954-1962). In E. ), Die Pliegen der palaearktischen Region, Bd.
13, 110-124. Esterase Evidentiation and Characterization in the Course of Onthogenesis in Chironomus Thummi Kieff. L. Tallandini*, M. Turchetto* and U. , via Loredan 10, 1-35100 Padova, Italy Museo Civico di Storia Naturale, Lungadige Porta, Vittoria 9, Ί-37100 Verona, Italy ABSTRACT Esterases from larvae, pupae and adults of Chironomus thummi have been studied, as function of time, using a and (3 naphthyl acetate as substrates. Variation of esterasic activity in relation with pH, temperature, and specific inhibitors has been observed.