A serine proteinase in Drosophila embryos: Yolk localization and developmental activation

descriptionPublicationkeyboard_double_arrow_right Article 01 Jan 1989 Spain English Publisher:Elsevier BVJournal:Insect Biochemistry, volume 19, pages 687-691 (issn: 0020-1790,

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Authors: Medina, Miguel; Vallejo, Carmen G.;

doi: 10.1016/0020-1790(89)90105-4

handle: 10261/259178

A serine proteinase in Drosophila embryos: Yolk localization and developmental activation

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Abstract

A serine proteinase (molecular mass, about 25,000 Da) has been found in Drosophila mature oocytes. (1) The detected activity increases exponentially during embryogenesis. (2) The subcellular localization changes from the yolk granules, in oocytes, to the soluble fraction, in late embryos. (3) The proteinase cleaves by basic residues, but arginine is preferred (about 7-fold) over lysine.

This work has been supported by Comisión Asesora de Investigación Científica y Técnica.

Country

Spain

Related Organizations

Spanish National Research Council
Spain

Keywords

Preferred cleavage by arginine vs lysine, Developmental changes in subeellular localization, Developmentally regulated proteinase, Drosophila serine proteinase, Yolk granules associated proteinase

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