The complete amino acid sequence of the major component myoglobin of Amazon river dolphin (Inia geoffrensis).

Biochemistry
F E DwuletF R Gurd

Abstract

The complete amino acid sequence of the major component myoglobin from Amazon River dolphin, Inia geoffrensis, was determined by specific cleavage of the protein to obtain large peptides which are readily degraded by the automatic sequencer. Three easily separable peptides were obtained by cleaving the protein with cyanogen bromide at the methionine residues and four peptides were obtained by cleaving the methyl-acetimidated protein with trypsin at the arginine residues. From these peptides over 85% of the sequence was completed. The remainder of the sequence was obtained by fragmentation of the large cyanogen bromide peptide with trypsin. This protein differs from that of the common porpoise, Phocoena phocoena, at seven positions, from that of the common dolphin, Delphinus delphis, at 11 positions, and from that of the sperm whale, Physeter catodon, at 15 positions. By comparison of this sequence with the three-dimensional structure of sperm whale myoglobin it appears that those residues close to the heme group are most conserved followed by those in nonhelical regions and lastly by those in the helical segments. All of the substitutions observed in this sequence fit easily into the three-dimensional structure of the sperm wha...Continue Reading

Citations

Jun 8, 1979·Journal of Molecular Evolution·R CoutelleR D Levine
Jul 1, 1980·Journal of Molecular Evolution·R A BogardtF R Gurd
Jan 1, 1981·Journal of Molecular Evolution·J L MeuthF R Gurd
Jan 1, 1977·Comparative Biochemistry and Physiology. B, Comparative Biochemistry·L K Duffy, C T Genaux
Mar 28, 1977·Biochimica Et Biophysica Acta·O CastilloL T Jones
Jan 1, 1981·Archives of Biochemistry and Biophysics·B N Jones, R S Gurd
Feb 1, 1979·International Journal of Peptide and Protein Research·F E Dwulet, F R Gurd
May 27, 1977·Biochimica Et Biophysica Acta·O Castillo, H Lehmann

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