Camici G, Manao G, Cappugi G, Berti A, Stefani M, Liguri G, Ramponi G
Eur J Biochem. 1983 Dec 1;137(1-2):269-77. doi: 10.1111/j.1432-1033.1983.tb07825.x.
The complete primary structure of turkey muscle acylphosphatase has been determined. The sequence was derived from peptides obtained by digestion of the carboxymethylated protein with pepsin and thermolysin and by subdigestion of some of the cyanogen bromide fragments with trypsin and Staphylococcus aureus protease. Peptides were purified by preparative finger prints and/or preparative high-performance liquid chromatography. Sequencing of the various peptides was achieved by manual Edman degradation and by time-course analysis of amino acids released by carboxypeptidases. The amino-terminal blocking group (acetyl) was determined by fast atom bombardment mass spectrometry. This sequence was compared with that of horse muscle enzyme determined previously.
