tailieunhanh - Báo cáo khoa học: Native and subunit molecular mass and quarternary structure of the hemoglobin from the primitive branchiopod crustacean Triops cancriformis

Many branchiopod crustaceans are endowed with extracellular, high-molecular-weight hemoglobins whose exact structural characteristics have remained a matter of conjecture. By using a broad spectrum of techniques, we provide precise and coherent information on the hemoglobin of one of the phylogenetically ‘oldest’ extant branchiopods, the tadpole shrimp Triops cancriformis. | ỊFEBS Journal Native and subunit molecular mass and quarternary structure of the hemoglobin from the primitive branchiopod crustacean Triops cancriformis Morgane Rousselot1 Elmar Jaenicke2 Tobias Lamkemeyer3 J. Robin Harris4 and Ralph Pirow5 1 Equipe Ecophysiologie Adaptation et Evolutions Moleculaires Station Biologique Roscoff France 2 Institute of Molecular Biophysics Johannes Gutenberg University of Mainz Germany 3 Proteome Centre Tubingen Eberhard-Karls University of Tubingen Germany 4 Institute of Zoology Johannes Gutenberg University of Mainz Germany 5 Institute of Zoophysiology University of Munster Germany Keywords Crustacea hemoglobin structure-function relationship Correspondence R. Pirow Institute of Zoophysiology Hindenburgplatz 55 University of Munster D-48143 Munster Germany Fax 49 251 8323876 Tel 49 251 8323858 E-mail pirow@ Received 12 May 2006 revised 23 June 2006 accepted 6 July 2006 doi Many branchiopod crustaceans are endowed with extracellular high-molecular-weight hemoglobins whose exact structural characteristics have remained a matter of conjecture. By using a broad spectrum of techniques we provide precise and coherent information on the hemoglobin of one of the phylogenetically oldest extant branchiopods the tadpole shrimp Triops cancriformis. The hemoglobin dissociated under reducing conditions into two subunits designated TcHbA and TcHbB with masses of 35 775 4 and 36 055 4 Da respectively determined by ESI-MS. Nonreducing conditions showed only two disulfide-bridged dimers a homodimer of TcHbA designated D1 71 548 5 Da and the heterodimer D2 71 828 5 Da . Carbamidomethylation of free SH groups revealed the presence of three cysteines per subunit and indicated one intrasubunit and one intersubunit disulfide bridge. Ultracentrifugation and light-scattering experiments under nondenaturating conditions yielded mass estimates that suggested an uneven number of 17 subunits forming the native .

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