The amino acid sequence of the alpha- and beta-chains of the two hemoglobins of the Antarctic fish Notothenia coriiceps neglecta.

• Published in: FEBS Letters
• Main Authors: R. D'Avino, C. Caruso, B. Rutigliano, M. Romano, L. Camardella, G. Di Prisco, SCHININA', Maria Eugenia, BOSSA, Francesco, BARRA, Donatella
• Other Authors: R., D'Avino, C., Caruso, Schinina', Maria Eugenia, B., Rutigliano, M., Romano, L., Camardella, Bossa, Francesco, Barra, Donatella, G., Di Prisco
• Format: Article in Journal/Newspaper
• Language: English
• Published: Attuale:ELSEVIER SCIENCE INC, 360 PARK AVE SOUTH, NEW YORK, USA, NY, 10010-1710 Academic Press Incorporated:6277 Sea Harbor Drive:Orlando, FL 32887:[phone], [phone], EMAIL: [e-mail], INTERNET: http://www.idealibrary.com, Fax: [phone] 1989
• Subjects: hemoglobin; protein primary structure; Antarctic; The Antarctic; Antarc*
• Online Access: http://hdl.handle.net/11573/78428; https://doi.org/10.1016/0014-5793(89)80683-0; http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=A1989AB76300011&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=0c7ff228ccbaaa74236f48834a34396a

The blood of the Antarctic fish Notothenia coriiceps neglecta contains two hemoglobins, Hb 1 and Hb 2, which have a beta-chain in common. We have elucidated the primary structure of the beta-chain (146 residues) and of the alpha-chains (142 residues) of the two hemoglobins. The two alpha-chains differ from each other by 51 residues; in comparison with globin sequences of temperate fishes, the alpha-chain of Hb 1 is more similar to that of bluefin tuna than to the alpha-chain of Hb 2 of the same species.