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Guinea pig acylphosphatase: The amino acid sequence |
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| Authors: | Giampaolo Manao Gianni Cappugi Alessandra Modesti Massimo Stefani Riccardo Marzocchini Donatella Degl'Innocenti and Guido Camici |
| Institution: | (1) Institute of Biological Chemistry, University of Florence, 50134 Florence, Italy |
| 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. |
| Keywords: | acylphosphatase guinea pig primary structure sequence comparison |
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