TY - JOUR
T1 - Chicken liver phosphofructokinase. I. Crystallization and physicochemical properties
AU - Kono, N.
AU - Uyeda, K.
AU - Oliver, R. M.
N1 - Copyright:
Copyright 2004 Elsevier B.V., All rights reserved.
PY - 1973
Y1 - 1973
N2 - Chicken liver and breast muscle phosphofructokinases were purified to homogeneity; the liver enzyme was crystallized. The liver phosphofructokinase is reversibly inactivated at low temperatures. This property appears to be unique to phosphofructokinases from avian livers; the enzyme from other tissues of chicken and from the livers of several other animals are stable in the cold. Sucrose density gradient centrifugation, gel filtration, and ultracentrifugal analysis reveal polymeric forms of the chicken liver enzyme, with the distribution depending upon the conditions and protein concentration. The molecular weight of the monomeric form of the liver enzyme is approximately 400,000. However, the enzyme in NaHCO3 at pH 10.5 has a molecular weight of about 210,000. In 7 M guanidine hydrochloride the enzyme dissociates into subunits of 60,000 ± 5,000 daltons. Peptide mapping and gel electrophoresis in sodium dodecyl sulfate suggest that these subunits are identical. Negative stain electron microscopy indicates that stable dimers and tetramers are formed by self association of these subunits. Under appropriate conditions, the higher polymeric forms result from aggregation of the tetramers into chains or sheets.
AB - Chicken liver and breast muscle phosphofructokinases were purified to homogeneity; the liver enzyme was crystallized. The liver phosphofructokinase is reversibly inactivated at low temperatures. This property appears to be unique to phosphofructokinases from avian livers; the enzyme from other tissues of chicken and from the livers of several other animals are stable in the cold. Sucrose density gradient centrifugation, gel filtration, and ultracentrifugal analysis reveal polymeric forms of the chicken liver enzyme, with the distribution depending upon the conditions and protein concentration. The molecular weight of the monomeric form of the liver enzyme is approximately 400,000. However, the enzyme in NaHCO3 at pH 10.5 has a molecular weight of about 210,000. In 7 M guanidine hydrochloride the enzyme dissociates into subunits of 60,000 ± 5,000 daltons. Peptide mapping and gel electrophoresis in sodium dodecyl sulfate suggest that these subunits are identical. Negative stain electron microscopy indicates that stable dimers and tetramers are formed by self association of these subunits. Under appropriate conditions, the higher polymeric forms result from aggregation of the tetramers into chains or sheets.
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M3 - Article
C2 - 4271655
AN - SCOPUS:0015766412
SN - 0021-9258
VL - 248
SP - 8592
EP - 8602
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 24
ER -