title: Further characterization and amino acid sequence of m-type thioredoxins from spinach chloroplasts.
abstract: The complete primary structure of m-type thioredoxin from spinach chloroplasts has been sequenced by conventional sequencing including fragmentation, Edman degradation and carboxypeptidase digestion. As already reported [Tsugita, A., Maeda, K. & Schürmann, P. (1983) Biochem. Biophys. Res. Commun. 115, 1-7] these thioredoxins contain the same active-site sequence as thioredoxins from other sources. Based on the amino acid sequence thioredoxin mc contains 103 residues, has a relative molecular mass of 11425 and a molar absorption coefficient at 280 nm of 19 300 M-1 cm-1. The spinach thioredoxin mc has an overall homology of 44% with the thioredoxin from Escherichia coli mainly due to differences in the N-terminal and C-terminal regions.
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000302:isolation & purification*; D002736:Chloroplasts / Q000032:analysis*; D004926:Escherichia coli / Q000032:analysis; D006863:Hydrogen-Ion Concentration; D010084:Oxidation-Reduction; D010446:Peptide Fragments / Q000032:analysis; D010944:Plants; D013045:Species Specificity; D013050:Spectrometry, Fluorescence; D013879:Thioredoxins / Q000302:isolation & purification*
chemical_list: D001426:Bacterial Proteins; D010446:Peptide Fragments; D013879:Thioredoxins