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The amino acid sequence of hemoglobin I from Parasponia andersonii , a nonleguminous plant
Author(s) -
Kortt Alexander A.,
Burns John E.,
Trinick Michael J.,
Appleby Cyril A.
Publication year - 1985
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(85)80229-5
Subject(s) - hemoglobin , homology (biology) , biology , amino acid , peptide sequence , biochemistry , helix (gastropod) , amino acid residue , botany , genetics , gene , paleontology , snail
The complete amino acid sequence of the hemoglobin I from nitrogen‐fixing root nodules of the nonleguminous plant, Parasponia andersonii , has been determined. This dimeric protein consists of two identical polypeptide chains of 155 amino acids and shows extensive sequence homology with other hemoglobins. Homology between the hemoglobin I of P. andersonii and the leghemoglobins of lupin and soybean nodules is 41 and 39%, respectively. The predicted secondary structure of P. andersonii hemoglobin I has a high content of α‐helix; except for the E‐helix, similar helices were predicted as those in the leghemoglobins. The close homology of the sequences provides evidence that this nonleguminous hemoglobin shares the same genetic origin as the legume and animal hemoglobins.