Purification and characterization of acylphosphatase erythrocyte isoenzyme from turkey muscle.
An acylphosphatase has been purified from turkey muscle in a rapid and high-yield way. The enzyme has been characterized for structural, kinetic, and immunological parameters, as well as with regard to its stability to thermal, urea, and phenylglyoxal inactivation. The enzyme is quite different from the turkey muscular isoenzyme, and shows structural and kinetic properties that are very similar to those previously reported for the erythrocyte isoenzyme from human erythrocytes and from chicken muscle. From the data reported it appears that this enzyme corresponds to the acylphosphatase erythrocyte isoenzyme. Unlike the erythrocyte isoenzymes studied so far, this enzyme is able to cross-react with antibodies that are raised against the muscular isoenzyme.
Stefani
M
M
Department of Biochemical Sciences, University of Florence, Italy.
Degl'Innocenti
D
D
Berti
A
A
Cappugi
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G
Manao
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G
Camici
G
G
Ramponi
G
G
D017766:Acid Anhydride Hydrolases; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002846:Chromatography, Affinity; D004591:Electrophoresis, Polyacrylamide Gel; D004912:Erythrocytes / Q000201:enzymology*; D006358:Hot Temperature; D007124:Immunoenzyme Techniques; D007163:Immunosorbent Techniques; D007527:Isoenzymes / Q000737:chemistry / Q000302:isolation & purification*; D007700:Kinetics; D008970:Molecular Weight; D009132:Muscles / Q000201:enzymology*; D010658:Phenylglyoxal; D010744:Phosphoric Monoester Hydrolases / Q000737:chemistry / Q000302:isolation & purification*; D011489:Protein Denaturation; D014422:Turkeys / Q000378:metabolism*; D014508:Urea; D000097024:Acylphosphatase
D017766:Acid Anhydride Hydrolases; D000596:Amino Acids; D007527:Isoenzymes; D010658:Phenylglyoxal; D010744:Phosphoric Monoester Hydrolases; D014508:Urea; D000097024:Acylphosphatase