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Amino acid sequence of a globin from the sea cucumber Caudina (Molpadia) arenicola.

Biochimica et Biophysica Acta

Amino Acid Sequence, Animals, Globins, chemistry, Humans, Invertebrates, Molecular Sequence Data, Phylogeny, Sea Cucumbers, analysis, Sequence Homology, Nucleic Acid, Vertebrates

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      Coelomic cells from the sea cucumber Caudina (Molpadia) arenicola contain four major globins, A, B, C and D. The hemoglobins from this organism show unusual ligand-linked dissociation properties. The complete amino acid sequence of the D globin has been established. It is N-acetylated, consists of 158 residues and has a 10 amino acid N-terminal extension similar to that found in some other invertebrate globins. The C. arenicola D globin has an equal sequence identity (28%) with both alpha and beta human globins and as anticipated, is more closely related to these vertebrate proteins than are molluscan globins. The C. arenicola D globin shows a 59% identity with the globin I from the sea cucumber Paracaudina chilensis. The availability of the C. arenicola D globin sequence will aid the X-ray analysis of this protein and facilitate an understanding of the changes in subunit interactions that occur with cooperative ligand binding.

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