Abstract: 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.
Guinea pig acylphosphatase: the amino acid sequence / G. Manao; G. Cappugi; A. Modesti; M. Stefani; R. Marzocchini; D. Degl'Innocenti; G. Camici. - In: JOURNAL OF PROTEIN CHEMISTRY. - ISSN 0277-8033. - STAMPA. - 7:(1988), pp. 417-426.
Guinea pig acylphosphatase: the amino acid sequence
MANAO, GIAMPAOLO;CAPPUGI, GIANNI;MODESTI, ALESSANDRA;STEFANI, MASSIMO;MARZOCCHINI, RICCARDO;DEGL'INNOCENTI, DONATELLA;CAMICI, GUIDO
1988
Abstract
Abstract: 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.
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