Characterization of the myoglobin of the lamprey Petromyzon marinus.
Myoglobin has been identified in the myocardium of the lamprey Petromyzon marinus, one of the most primitive of all vertebrates. This protein was isolated by ammonium sulphate fractionation and purified by successive chromatography on Ultrogel AcA 54, DEAE-Sephadex and CM-23 cellulose. The molecule differs substantially from the monomeric hemoglobins found in the lamprey as evidenced by its elution profile on DEAE-Sephadex and the fingerprint pattern of its enzymically-produced peptides. The functional significance of this protein in Agnatha is discussed.
D000595:Amino Acid Sequence; D000645:Ammonium Sulfate; D000818:Animals; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D005399:Fishes / Q000378:metabolism*; D007798:Lampreys / Q000378:metabolism*; D009211:Myoglobin / Q000302:isolation & purification*
D009211:Myoglobin; D000645:Ammonium Sulfate