Abstract: Human skeletal muscle acylphosphatase, purified by a technique based on affinity chromatography on immunoadsorbent, has been sequenced completely using tryptic and peptic peptide series, prepared by reverse-phase high-pressure liquid chromatography. The sequence analysis was carried out on all the isolated tryptic peptides using a manual Edman degradation technique and time-course analysis of the released amino acids by carboxypeptidase A. The enzyme is NH2-blocked and the blocking group has been identified by fast atom bombardment mass spectrometry
Human skeletal muscle acylphosphatase: the primary structure / G. Manao; G. Camici; A. Modesti; G. Liguri; A. Berti; M. Stefani; G. Cappugi; G. Ramponi. - In: MOLECULAR BIOLOGY & MEDICINE. - ISSN 0735-1313. - STAMPA. - 2:(1984), pp. 369-378.
Human skeletal muscle acylphosphatase: the primary structure
MANAO, GIAMPAOLO;CAMICI, GUIDO;MODESTI, ALESSANDRA;LIGURI, GIANFRANCO;BERTI, ANDREA;STEFANI, MASSIMO;CAPPUGI, GIANNI;RAMPONI, GIAMPIETRO
1984
Abstract
Abstract: Human skeletal muscle acylphosphatase, purified by a technique based on affinity chromatography on immunoadsorbent, has been sequenced completely using tryptic and peptic peptide series, prepared by reverse-phase high-pressure liquid chromatography. The sequence analysis was carried out on all the isolated tryptic peptides using a manual Edman degradation technique and time-course analysis of the released amino acids by carboxypeptidase A. The enzyme is NH2-blocked and the blocking group has been identified by fast atom bombardment mass spectrometry
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