Guinea pig acylphosphatase: The amino acid sequence

descriptionPublicationkeyboard_double_arrow_right Article 01 Aug 1988 Italy English Publisher:Springer Science and Business Media LLCJournal:Journal of Protein Chemistry, volume 7, pages 417-426 (issn: 0277-8033, eissn: 1573-4943,

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Authors: MANAO, GIAMPAOLO; CAPPUGI, GIANNI; MODESTI, ALESSANDRA; STEFANI, MASSIMO; MARZOCCHINI, RICCARDO; DEGL'INNOCENTI, DONATELLA; CAMICI, GUIDO;

doi: 10.1007/bf01024889

pmid: 2855598

handle: 2158/323449

Guinea pig acylphosphatase: The amino acid sequence

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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.

Country

Italy

Related Organizations

University of Florence
Italy
New York University
Italy

Keywords

Protein Conformation, Muscles, Guinea Pigs, Molecular Sequence Data, Acylphosphatase; Guinea pig acylphosphatase; Amino acid sequence; Primary structure, Mass Spectrometry, Peptide Fragments, Phosphoric Monoester Hydrolases, Acid Anhydride Hydrolases, Acylphosphatase, Animals, Amino Acid Sequence, Amino Acids, Chromatography, High Pressure Liquid

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Acylphosphatase-2
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AltName: Full=Acylphosphate phosphohydrolase 2;
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