Abstract

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.

Full Text
Paper version not known

Talk to us

Join us for a 30 min session where you can share your feedback and ask us any queries you have

Schedule a call

Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.