scholarly journals Purification and properties of rat brain pyruvate carboxylase

1975 ◽  
Vol 145 (1) ◽  
pp. 25-35 ◽  
Author(s):  
D E Mahan ◽  
I K Mushahwar ◽  
R E Koeppe
Keyword(s):  
Polyethylene Glycol ◽  
Rat Brain ◽  
Kinetic Parameters ◽  
Rat Liver ◽  
Pyruvate Carboxylase ◽  
Purification And Properties

Rat brain pyruvate carboxylase was purified 2000-fold and some of its properties and kinetic parameters were investigated. The use of (NH4)2SO4 gradient solubilization on a Celite column and precipitation with polyethylene glycol permitted purification to an estimated 20% purity. Except for a few subtle kinetic differences this enzyme is indistinguishable from rat liver pyruvate carboxylase.

Purification and properties of rat brain pyruvate carboxylase

1975 ◽  
Vol 147 (3) ◽  
pp. 385.b1-385.b1
Author(s):  
H. O. Spivey ◽  
W. Flory ◽  
B. D. Peczon ◽  
J. P. Chandler ◽  
R. E. Koeppe
Keyword(s):  
Rat Brain ◽  
Pyruvate Carboxylase ◽  
Purification And Properties

Purification and Properties of Pyruvate Carboxylase from Rat Liver

1971 ◽  
pp. 11-19 ◽  
Author(s):  
C.D. Seufert ◽  
E. Herlemann ◽  
E. Albrecht ◽  
W. Seubert
Keyword(s):  
Rat Liver ◽  
Pyruvate Carboxylase ◽  
Purification And Properties

scholarly journals Purification and properties of peroxisomal pyruvate (glyoxylate) aminotransferase from rat liver

1978 ◽  
Vol 175 (2) ◽  
pp. 765-768 ◽  
Author(s):  
T Noguchi ◽  
Y Takada
Keyword(s):  
Amino Acids ◽  
Kinetic Parameters ◽  
Rat Liver ◽  
Isoelectric Point ◽  
Enzyme Preparation ◽  
Ph Optimum ◽  
Purification And Properties ◽  
Amino Donor ◽  
Glyoxylate Aminotransferase ◽  
Liver Peroxisomes

Pyruvate (glyoxylate) aminotransferase from rat liver peroxisomes was highly purified and characterized. The enzyme preparation has a mol.wt. of approx. 80,000 with two identical subunits, and isoelectric point of 8.0 and a pH optimum between 8.0 and 8.5. The enzyme catalysed transamination between a number of L-amino acids and pyruvate or glyoxylate. The effective amino acceptors were pyruvate, phenylpyruvate and glyoxylate with serine, and glyoxylate and phenylpyruvate with alanine as amino donor. These properties and kinetic parameters of the enzyme are remarkably similar to those previously described for mitochondrial alanine-glyoxylate aminotransferase isoenzyme 1 from glucagon-injected rat liver [Noguchi, Okuno, Takada, Minatogawa, Okai & Kido (1978, Biochem. J. 169, 113-122].

scholarly journals The purification and properties of microsomal palmitoyl-coenzyme A synthetase

1971 ◽  
Vol 122 (3) ◽  
pp. 353-362 ◽  
Author(s):  
J. Bar–Tana ◽  
G. Rose ◽  
B. Shapiro
Keyword(s):  
Fatty Acid ◽  
Kinetic Parameters ◽  
Rat Liver ◽  
Enzyme Assay ◽  
Liver Microsomes ◽  
Acid Activation ◽  
Rat Liver Microsomes ◽  
Isolation And Purification ◽  
Purification And Properties ◽  
Fatty Acid Activation

The isolation and purification of palmitoyl-CoA synthetase from rat liver microsomes is described. Several methods suitable for enzyme assay are described. The general properties and kinetic parameters of the purified enzyme were determined and are discussed in relationship to microsomal fatty acid activation.

scholarly journals Purification and Properties of Rat Liver Tyrosine Aminotransferase

1969 ◽  
Vol 244 (13) ◽  
pp. 3618-3624 ◽  
Author(s):  
F A Valeriote ◽  
F Auricchio ◽  
G M Tomkins ◽  
D Riley
Keyword(s):  
Rat Liver ◽  
Tyrosine Aminotransferase ◽  
Purification And Properties
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