1.
FEBS Lett
; 171(2): 293-6, 1984 Jun 11.
Artículo
en Inglés
| MEDLINE
| ID: mdl-6723988
RESUMEN
Previous evidence has shown that the M1 and L pyruvate kinase isozymes differ markedly in kinetic and immunological properties, amino acid compositions and peptide maps. However, the amino acid sequence results we present here for the N-terminal region and for a region of the C domain show that the M1 and L isozymes are very similar. The variable length of the N-terminal sequences also explains the difference in regulation by phosphorylation between the M1 and L isozymes. The M1 isozyme lacks the serine residue that has been shown to be phosphorylated in the L isozyme.
Asunto(s)
Isoenzimas/análisis , Hígado/enzimología , Músculos/enzimología , Piruvato Quinasa/análisis , Secuencia de Aminoácidos , Aminoácidos/análisis , Animales , Gatos , Cristalografía , Cinética , Sustancias Macromoleculares , Ratas
2.
Clin Chem
; 37(10 Pt 1): 1794-5, 1991 Oct.
Artículo
en Inglés
| MEDLINE
| ID: mdl-1914186