[Primary structure of the cytoplasmic aspartate aminotransferases from the swine myocardium. Isolation, purification and characteristics of the peptides from cyanogen bromide cleavage].
Cytoplasmic aspartate aminotransferase from pig heart muscle was cleaved with cyanogen bromide and 8 peptide fragments were isolated. The high tendency of the large peptides for aggregation was overcome only by the utilization of special procedures of the denaturation and acylation of the lysine residues of peptide with citraconic anhydride. Peptides were separated by gel chromatography on sephadex G-50 and G-75 and by ion exchange chromatography on cellulose DE-22 and DE-32 with use of concentrated urea solutions. Amino acid composition and N-terminal residues of isolated peptides were determined.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001219:Aspartate Aminotransferases / Q000302:isolation & purification*; D002850:Chromatography, Gel; D003488:Cyanogen Bromide / Q000494:pharmacology*; D003593:Cytoplasm / Q000201:enzymology*; D004591:Electrophoresis, Polyacrylamide Gel; D008968:Molecular Conformation; D009206:Myocardium / Q000166:cytology / Q000201:enzymology*; D010443:Peptide Chain Termination, Translational; D010446:Peptide Fragments / Q000302:isolation & purification; D010455:Peptides / Q000302:isolation & purification*; D011489:Protein Denaturation; D013552:Swine
D000596:Amino Acids; D010446:Peptide Fragments; D010455:Peptides; D001219:Aspartate Aminotransferases; D003488:Cyanogen Bromide
Pervichnaia struktura tsitoplazmaticheskoĭ aspartat-aminotransferazy iz serdechnoĭ myshtsy svin'i. Vydelenie, ochistka i kharakteristika peptidov bromtsianovogo rasshchepleniia