Identification of Endogenous Substrates for Drosophila Calpain from a Salt-Extracted Fraction of Drosophila Ovaries

Drosophila calpain (Dm-calpain) produced in Escherichia coli has a distinct Ca2+-depen-dent activity. By using a recombinant Dm-calpain, we searched for its substrates occurring in Drosophila ovaries, where Dm-calpain is expressed. Among a number of major proteins, several proteins in a salt-extract...

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Veröffentlicht in:	Journal of biochemistry (Tokyo) 1997-10, Vol.122 (4), p.865-871
Hauptverfasser:	Amano, Susumu, Kawasaki, Hiroshi, Ishiura, Shoichi, Kawashima, Seiichi, Suzuki, Koichi, Emori, Yasufumi
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Animals bacterial-expression calpain Calpain - genetics Calpain - metabolism Chromatography, High Pressure Liquid Cloning, Molecular Drosophila Drosophila melanogaster - enzymology EF-1α Escherichia coli - genetics Female Hydrolysis limited-proteolysis Ovary - metabolism Peptide Elongation Factor 1 Peptide Elongation Factors - isolation & purification Peptide Elongation Factors - metabolism Recombinant Proteins - genetics Recombinant Proteins - metabolism Substrate Specificity
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