Abstract
The annelid extracellular hemoglobins are giant heme containing respiratory proteins (3-4x106 MW) possessing an extraordinary range of physiological function, Their electron microscopic appearance is that of two superimposed hexagons with approximate dimensions of 300 x 200Å by STEM. These unusual proteins are composed of multiple copies of as many as six distinct polypeptides ranging in size from 13 to 37,000 MW as determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). Possessing approximately 150 hemes per molecule, they represent an alternate solution to the demand for increased efficiency of oxygen transport imposed by the evolution of multicellular organisms.The hemoglobin of Lumbricus terrestris dissociates at alkaline pH yielding a broad overlapping distribution of molecular weight species ranging in size from 25 to 300K. Exposure to 0.05M sodium borate buffer, pH 9.0, for 24 hours, followed by gel filtration on a column of Sepharose C1-6B equilibrated in the same buffer, gives the elution profile shown in Fig. 1.
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Schedule a callMore From: Proceedings, annual meeting, Electron Microscopy Society of America
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