-transparent.png){kind=logo}
1. Purification of four isozymes of pyruvate kinase (ATP:pyruvate 2-O-phosphotransferase, EC 2.7.1.40) L, M1, M2 and R was much improved to give good yields by affinity elution chromatography. The enzyme was eluted from a phosphocellulose column with 0.5 mM phosphoenolpyruvate. Types L, M2 and R were stabilized with fructose 1,6-diphosphate throughout the purification procedures. 2. The isozymes were crystallized under various conditions: types L and R were readily crystallized from medium of low ionic strength, types L, M1, and M2 were crystallized from ammonium sulfate solution in different forms in the presence and absence of phosphoenolpyruvate. Type M1 was also crystallized in different forms in the presence and absence of fructose 1,6-diphosphate. 3. Amino acid analyses showed that the compositions of types L and R, and of types M1 and M2, respectively, were very similar.
K Harada, and
S Saheki, and
K Wada, and
T Tanaka
October 1978,
The Biochemical journal,
K Harada, and
S Saheki, and
K Wada, and
T Tanaka
January 1975,
Acta biologica et medica Germanica,
K Harada, and
S Saheki, and
K Wada, and
T Tanaka
September 1978,
FEBS letters,
K Harada, and
S Saheki, and
K Wada, and
T Tanaka
July 1980,
Analytical biochemistry,
K Harada, and
S Saheki, and
K Wada, and
T Tanaka
February 1977,
The Biochemical journal,
K Harada, and
S Saheki, and
K Wada, and
T Tanaka
December 1992,
Journal of chromatography,
K Harada, and
S Saheki, and
K Wada, and
T Tanaka
July 1976,
Biochimica et biophysica acta,
K Harada, and
S Saheki, and
K Wada, and
T Tanaka
June 1982,
Biochimica et biophysica acta,
K Harada, and
S Saheki, and
K Wada, and
T Tanaka
January 1978,
Preparative biochemistry,
K Harada, and
S Saheki, and
K Wada, and
T Tanaka
January 2000,
Methods in enzymology,
