Horse brain acylphosphatase: purification and characterization.
Two structurally different acylphosphatases found in horse brain were purified; they were not immunologically related. The molecular masses were almost identical and the kinetic parameters were rather similar. The data reported indicate that one of the purified brain acylphosphatases and an enzyme, previously isolated from horse muscle, are the same protein. The presence of this acylphosphatase form in the brain has not been reported before. The other acylphosphatase seemed to be the same as the enzyme which had been purified from calf brain and partially characterized by Diederich and Grisolia [(1969) J. Biol. Chem. 244, 2412-2417]. Furthermore, this enzyme seems to be identical to the acylphosphatase recently purified in our laboratory from human erythrocytes.
Stefani
M
M
Department of Biochemistry, University of Florence, Italy.
Berti
A
A
Camici
G
G
Manao
G
G
Degl'Innocenti
D
D
Prakash
G
G
Marzocchini
R
R
Ramponi
G
G
D017766:Acid Anhydride Hydrolases; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001921:Brain / Q000201:enzymology*; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D004912:Erythrocytes / Q000201:enzymology; D006736:Horses; D007118:Immunoassay; D005779:Immunodiffusion; D009132:Muscles / Q000201:enzymology; D010744:Phosphoric Monoester Hydrolases / Q000302:isolation & purification* / Q000378:metabolism; D000097024:Acylphosphatase
D017766:Acid Anhydride Hydrolases; D000596:Amino Acids; D010744:Phosphoric Monoester Hydrolases; D000097024:Acylphosphatase