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Título

Characterization of 6-phosphofructo-2-kinase from foetal-rat liver

AutorMartín-Sanz, Paloma ; Cascales, Maria; Boscá, Lisardo
Fecha de publicación15-ene-1992
EditorPortland Press
CitaciónBiochemical Journal 281(2): 457-463 (1992)
ResumenFoetal and adult liver 6-phosphofructo-2-kinase (PFK-2) were purified by identical protocols. The native molecular masses of both enzymes were determined by gel filtration and were 89.1 and 100.0 kDa respectively. No differences were found in SDS/PAGE in 10%-acrylamide gel (55 kDa per subunit). The kinetic properties displayed by both enzymes were similar, except for the sensitivity to inhibition by sn-glycerol 3-phosphate. Foetal PFK-2 was a good substrate for phosphorylation by cyclic AMP-dependent protein kinase and protein kinase C, whereas the adult enzyme was phosphorylated only by cyclic AMP-dependent protein kinase. However, the phosphorylation affected only the kinetic properties of the adult enzyme, suggesting the presence in both enzymes of different sites of phosphorylation by cyclic AMP-dependent protein kinase. These differences in primary structure were consistent with the distinct chromatographic profiles of the phosphopeptides after digestion of the protein with CNBr. Western-blot analysis with antibodies specific for the N-terminal region of the liver-type PFK-2 poorly recognized the foetal enzyme, suggesting that both enzymes differ at least in the N-terminal sequence.
Descripción7 pages, 6 figures, 1 table.
Versión del editorhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC1130707/pdf/biochemj00143-0160.pdf
URIhttp://hdl.handle.net/10261/23814
ISSN0264-6021
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