Guinea pig acylphosphatase: the amino acid sequence.
We determined the primary structure of guinea pig skeletal muscle acylphosphatase, using the high degree of homology with several vertebrate acylphosphatases to obtain correct alignment of the complete series of tryptic peptides. Their sequences were obtained mainly by Edman degradation; FAB mass spectrometry was used to identify the acyl group blocking the NH2-terminal residue and to elucidate the structure of the NH2-terminal tryptic peptide. The comparison among acylphosphatase sequences from skeletal muscle of several vertebrate species is presented and discussed.
Manao
G
G
Institute of Biological Chemistry, University of Florence, Italy.
Cappugi
G
G
Modesti
A
A
Stefani
M
M
Marzocchini
R
R
Degl'Innocenti
D
D
Camici
G
G
D017766:Acid Anhydride Hydrolases; D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D006168:Guinea Pigs; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D009132:Muscles / Q000201:enzymology; D010446:Peptide Fragments / Q000032:analysis; D010744:Phosphoric Monoester Hydrolases; D011487:Protein Conformation; D000097024:Acylphosphatase
D017766:Acid Anhydride Hydrolases; D000596:Amino Acids; D010446:Peptide Fragments; D010744:Phosphoric Monoester Hydrolases; D000097024:Acylphosphatase