The primary sequence of badger myoglobin

• Published in: Biochimica et biophysica acta Vol. 351; no. 2; pp. 317 - 324
• Main Authors: Tetaert, Daniel, Han, Kia-Ki, Plancot, Marie-Therese, Dautrevaux, Michel, Ducastaing, Simone, Hombrados, Isabelle, Neuzil, Eugene
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 07.06.1974
• Subjects: Amino Acid Sequence; Amino Acids - analysis; Animals; Asparagine - analysis; Carnivora; Chromatography, Gel; Chromatography, Paper; Chromatography, Thin Layer; Chymotrypsin; Cyanogen Bromide; Dansyl Compounds; Electrophoresis, Paper; Glutamine - analysis; Myoglobin; Peptide Fragments - analysis; Protein Denaturation; Thermolysin; Trypsin; N-peptide; M-C x; M-Th x; C-peptide; M-peptide
• ISSN: 0005-2795; 0006-3002; 1879-2952
• DOI: 10.1016/0005-2795(74)90194-9

The badger apomyoglobin was first submitted to tryptic digestion. The tryptic hydrolysate of whole protein was fractionated by resin chromatography and each tryptic peptide was sequenced. The apomyoglobin was also cleaved by cyanogen bromide and the resulting fragments were fractionated by gel filtration; three segments were obtained; the N-terminal segment (55 residues), the C-terminal segment (22 residues) and the median segment (76 residues). Each segment was submitted to a variety of enzymatic digestions and the complete amino acid sequence of resulting peptides was established. In addition, the whole protein and the median segment were analyzed by using a sequenator (Edman); the first 31 N-terminal residues of the intact protein and the first 28 N-terminal residues of the median segment of CNBr resulting peptide were confirmed. The complete sequence of the C-terminal segment (22 residues) was also established and confirmed by manual Edman's degradation. Between badger and harbor seal myoglobins, 19 differences out of 153 residues were found. Of these amino acid replacements, one corresponds to the exchange of two bases and 18 to the exchange of one base in the coding triplets.