Assignment of a single disulfide bridge in rat liver methionine adenosyltransferase.
作者： María L. Martínez-Chantar , María A. Pajares
DOI: 10.1046/J.1432-1327.2000.00974.X
关键词: Chemistry 、 Dithiothreitol 、 Thiol 、 Residue (chemistry) 、 Enzyme 、 Biochemistry 、 Methionine 、 Denaturation (biochemistry) 、 Protein subunit 、 Methionine Adenosyltransferase
摘要: Rat liver methionine adenosyltransferase incorporated 8 mol of N-ethylmaleimide per mol subunit upon denaturation in the presence 8 m urea, whereas 10 such groups were labelled when dithiothreitol was also included. This observation prompted a re-examination state thiol groups, which carried out using peptide mapping, amino acid analysis and N-terminal sequencing. The results obtained revealed disulfide bridge between Cys35 Cys61. did not appear to be conserved because cysteines homologous residue 61 do exist adenosyltransferases other origins, therefore suggesting its importance for differential aspects liver-specific enzyme.
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