Structure and oxygen equilibrium of the three coelomic cell hemoglobins of the echiuran worm Thalassema mellita (Conn).

Journal Article (Journal Article)

1. The three coelomic cell hemoglobins from Thalassema mellita have been isolated to purity; the two major components have dimeric structure while the third minor component has monomeric structure. 2. Acid-urea Triton gel electrophoresis of the isolated hemoglobins identified three polypeptides among the three hemoglobins, one of the dimeric hemoglobins is a heterodimer (pI = 4.9) with one polypeptide sharing identity with the monomeric hemoglobin (pI = 6.3), while the other dimer is a homodimer (pI = 4.5) consisting of the third polypeptide. 3. SDS gel electrophoresis suggests that the two dimeric hemoglobins have interpolypeptide disulfide bonds. 4. Coelomic cell suspensions and lysed coelomic cells have PO2 at half saturation (P50) of 2.5-3.0 mmHg and cooperativity values (n) of 1.5-1.93. 5. All three isolated hemoglobins have higher oxygen affinities and lower cooperativity values (P50 = 1-2 mmHg, n = 1-1.3) than lysed coelomic cells suggesting some heterotrophic and homotrophic interactions.

Full Text

Duke Authors

Cited Authors

  • Vinson, CR; Bonaventura, J

Published Date

  • January 1987

Published In

Volume / Issue

  • 87 / 2

Start / End Page

  • 361 - 366

PubMed ID

  • 3621904

International Standard Serial Number (ISSN)

  • 0305-0491

Digital Object Identifier (DOI)

  • 10.1016/0305-0491(87)90153-2


  • eng