TY - JOUR
T1 - On the Mechanism of Glucose‐6‐Phosphate Dehydrogenase Regulation in Mouse Liver
T2 - 2. Purification and Properties of the Mouse‐Liver Enzyme
AU - Hizi, Amnon
AU - Yagil, Gad
PY - 1974/6
Y1 - 1974/6
N2 - Glucose‐6‐phosphate dehydrogenase is purified from C57BL mouse liver to a specific activity of 116 units/mg protein. The molecular weight of the main active unit is 121000 and it is composed of three interconvertible subforms, as revealed by acrylamide electrophoresis. The main active unit is composed of two subunits of molecular weight 62000, and may aggregate to form higher oligomers. Amino acid composition and dependence of rate on pH and substrate concentration are reported. The kinetic data suggest the existence of two types of active sites with separate sets of Km and V values. The electrophoretic and kinetic properties of the enzyme from induced and non‐induced liver homogenates are compared.
AB - Glucose‐6‐phosphate dehydrogenase is purified from C57BL mouse liver to a specific activity of 116 units/mg protein. The molecular weight of the main active unit is 121000 and it is composed of three interconvertible subforms, as revealed by acrylamide electrophoresis. The main active unit is composed of two subunits of molecular weight 62000, and may aggregate to form higher oligomers. Amino acid composition and dependence of rate on pH and substrate concentration are reported. The kinetic data suggest the existence of two types of active sites with separate sets of Km and V values. The electrophoretic and kinetic properties of the enzyme from induced and non‐induced liver homogenates are compared.
UR - http://www.scopus.com/inward/record.url?scp=0016152387&partnerID=8YFLogxK
U2 - 10.1111/j.1432-1033.1974.tb03544.x
DO - 10.1111/j.1432-1033.1974.tb03544.x
M3 - ???researchoutput.researchoutputtypes.contributiontojournal.article???
AN - SCOPUS:0016152387
SN - 0014-2956
VL - 45
SP - 201
EP - 209
JO - European Journal of Biochemistry
JF - European Journal of Biochemistry
IS - 1
ER -