The primary structure of two molecular species of porcine organ-common type acylphosphatase.
Electrophoretically homogeneous preparations of organ-common type acylphosphatase from porcine testis and brain were separated into two molecular species by reversed-phase liquid chromatography. From tryptic peptide map analysis, it was inferred that each of the two testis proteins is the same as the corresponding one of the two brain proteins. The complete primary structures of the two acylphosphatases from testis were then determined. The one molecular species consists of 100 amino acid residues: [sequence; see text] The other consists of 98 amino acid residues identical to the 3rd-100th residues of the above sequence and is also acetylated at the amino-terminal alanine. The 98-residue sequence has only 59% homology with porcine muscle acylphosphatase, but has 92% homology with human erythrocyte acylphosphatase. It was thus confirmed that the major acylphosphatases in testis, brain, and erythrocyte belong to the same organ-common type isoenzyme, distinct from the muscle type isoenzyme.
Mizuno
Y
Y
Section of Biochemistry, Hokkaido University.
Kanesaka
Y
Y
Fujita
H
H
Minowa
O
O
Shiokawa
H
H
D017766:Acid Anhydride Hydrolases; D000595:Amino Acid Sequence; D000818:Animals; D001921:Brain / Q000201:enzymology*; D006801:Humans; D006868:Hydrolysis; D008297:Male; D008666:Metalloendopeptidases; D008969:Molecular Sequence Data; D009928:Organ Specificity; D010446:Peptide Fragments / Q000737:chemistry; D010449:Peptide Mapping; D010744:Phosphoric Monoester Hydrolases / Q000737:chemistry / Q000302:isolation & purification*; D012689:Sequence Homology, Nucleic Acid; D013552:Swine; D013737:Testis / Q000201:enzymology*; D000097024:Acylphosphatase
D017766:Acid Anhydride Hydrolases; D008666:Metalloendopeptidases; D010446:Peptide Fragments; D010744:Phosphoric Monoester Hydrolases; D000097024:Acylphosphatase; C022653:auR protein, Staphylococcus aureus