Purification, kinetic properties and primary structure of bovine erythrocyte acylphosphatase.
An erythrocyte isoenzyme of acylphosphatase was purified from bovine red cells. The protein was characterized as regards the kinetic parameters and amino acid sequence. A simple and rapid sequencing strategy, based on a few experiments, was used for reconstructing the primary structure of the enzyme, since the purification procedure gave a very low yield. The length of the polypeptide chain is 100 residues. Comparison with the analogous human isoenzyme indicates that the primary structure is about 90% conserved. The presence of two additional residues at the acetylated N-terminus confirms the hypervariability for this region found in other acylphosphatases.
Pazzagli
L
L
Dipartimento di Scienze Biochimiche, Università di Firenze, Italia.
Ikram
U K
UK
Liguri
G
G
Taddei
N
N
Gentilini
A
A
Cecchi
C
C
Manao
G
G
Cappugi
G
G
D017766:Acid Anhydride Hydrolases / Q000097:blood* / Q000737:chemistry; D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D002851:Chromatography, High Pressure Liquid; D017124:Conserved Sequence; D003488:Cyanogen Bromide; D004912:Erythrocytes / Q000201:enzymology*; D006801:Humans; D007527:Isoenzymes / Q000097:blood* / Q000737:chemistry; D007700:Kinetics; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism; D017421:Sequence Analysis; D017386:Sequence Homology, Amino Acid; D000097024:Acylphosphatase
D017766:Acid Anhydride Hydrolases; D003488:Cyanogen Bromide; D007527:Isoenzymes; D010446:Peptide Fragments; D000097024:Acylphosphatase