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Biochem Biophys Res Commun. 1997 Mar 17;232(2):555-8.

Expression in Escherichia coli, phosphorylation with cAMP-dependent protein kinase and proteolysis by calpain of a 71-kDa domain of human endothelial actin binding protein.

Author information

1
Departamento de Cultivo de Tejidos, Instituto Nacional de Cardiologia, Mexico, Distrito Federal, Mexico.

Abstract

A middle region of human endothelial actin-binding protein (ABP) was subcloned and expressed in the pT7-7/E. coli BL21 (DE3) system. As predicted by the amino acid sequence this 71 kD truncated protein (residues 1717-2360) contained a calpain cleavage site and two of the three presumptive cAMP-dependent protein kinase phosphorylation sites. This peptide fragment comprised all the elements needed to confer stability against calpain proteolysis to ABP after PKA phosphorylation.

PMID:
9125221
DOI:
10.1006/bbrc.1997.6238
[Indexed for MEDLINE]

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