The precursor to rat liver mitochondrial aspartate aminotransferase has been expressed in Escherichia coli JM105 using the pKK233-2 expression vector. This mammalian natural precursor has been isolated as a soluble dimeric protein. The amino-terminal sequence and the amino acid composition of the isolated protein correspond to those predicted from the inserted cDNA (Mattingly, J. R., Jr., Rodriguez-Berrocal, F. J., Gordon, J., Iriarte, A., and Martinez-Carrion, M. (1987) Biochem. Biophys. Res. Commun. 149, 859-865). The isolated precursor contains bound pyridoxal phosphate and shows catalytic activity with a specific activity equal to that of the mature form of the enzyme. This precursor can also be processed by mitochondria into a form with the sodium dodecyl sulfate-polyacrylamide gel electrophoresis mobility of mature enzyme. The isolation of this precursor as a stable and catalytically active entity indicates that the presequence peptide does not necessarily interfere with much of the folding and basic structural properties of the mature protein component.

Isolation and properties of a liver mitochondrial precursor protein to aspartate aminotransferase expressed in Escherichia coli / Altieri, Fabio; Mattingly JR, Jr; Rodriguez Berrocal, Fj; Youssef, J; Iriarte, A; Wu, Th; Martinez Carrion, M.. - In: JOURNAL OF BIOLOGICAL CHEMISTRY. - ISSN 1083-351X. - STAMPA. - 264:(1989), pp. 4782-4786.

Isolation and properties of a liver mitochondrial precursor protein to aspartate aminotransferase expressed in Escherichia coli.

ALTIERI, Fabio;
1989

Abstract

The precursor to rat liver mitochondrial aspartate aminotransferase has been expressed in Escherichia coli JM105 using the pKK233-2 expression vector. This mammalian natural precursor has been isolated as a soluble dimeric protein. The amino-terminal sequence and the amino acid composition of the isolated protein correspond to those predicted from the inserted cDNA (Mattingly, J. R., Jr., Rodriguez-Berrocal, F. J., Gordon, J., Iriarte, A., and Martinez-Carrion, M. (1987) Biochem. Biophys. Res. Commun. 149, 859-865). The isolated precursor contains bound pyridoxal phosphate and shows catalytic activity with a specific activity equal to that of the mature form of the enzyme. This precursor can also be processed by mitochondria into a form with the sodium dodecyl sulfate-polyacrylamide gel electrophoresis mobility of mature enzyme. The isolation of this precursor as a stable and catalytically active entity indicates that the presequence peptide does not necessarily interfere with much of the folding and basic structural properties of the mature protein component.
1989
01 Pubblicazione su rivista::01a Articolo in rivista
Isolation and properties of a liver mitochondrial precursor protein to aspartate aminotransferase expressed in Escherichia coli / Altieri, Fabio; Mattingly JR, Jr; Rodriguez Berrocal, Fj; Youssef, J; Iriarte, A; Wu, Th; Martinez Carrion, M.. - In: JOURNAL OF BIOLOGICAL CHEMISTRY. - ISSN 1083-351X. - STAMPA. - 264:(1989), pp. 4782-4786.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11573/392659
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