title: Bacterial aspartate kinase-like activity in human platelet.
abstract: One form of a group of enzymes known as aspartate kinases, primarily reported in prokaryotes and plants, might also exist in animal cells. Here we report the immunodetection of an aspartate kinase-like activity in human platelets using antibodies against the pure form of the enzyme purified from Escherichia coli. Moreover, the enrichment of platelet extracts with the bacterial kinase results in the phosphorylation of discrete forms mainly of membrane-bound endogenous polypeptides.
authors.affiliation: Laboratorios de Fisiología Celular, Universidad Católica de Valparaíso, Chile. garenas@aix1.ucv.cl
authors.forename: G
authors.initials: G
authors.lastname: Arenas-Díaz
authors.forename: L A
authors.initials: LA
authors.lastname: Mercado
authors.forename: S H
authors.initials: SH
authors.lastname: Marshall
mesh_terms: D000255:Adenosine Triphosphate / Q000378:metabolism; D001222:Aspartate Kinase / Q000032:analysis / Q000097:blood* / Q000737:chemistry; D001792:Blood Platelets / Q000201:enzymology*; D002458:Cell Fractionation; D004926:Escherichia coli / Q000201:enzymology*; D006801:Humans; D008565:Membrane Proteins / Q000378:metabolism; D008970:Molecular Weight; D010766:Phosphorylation
chemical_list: D008565:Membrane Proteins; D000255:Adenosine Triphosphate; D001222:Aspartate Kinase