Amino-acid Sequences and Functional Differentiation of Hemoglobins A and D from Swift(Apus apus,Apodiformes)
- 1 January 1989
- journal article
- research article
- Published by Walter de Gruyter GmbH in Biological Chemistry Hoppe-Seyler
- Vol. 370 (2) , 1197-1208
- https://doi.org/10.1515/bchm3.1989.370.2.1197
Abstract
The blood of the adult swift contains one major (HbA = .alpha.2A.beta.2) and two minor components (HbD = .alpha.2D.beta.2 and HbD''). The components were separated by FPLC with a TSK SP-5 PW-column in phosphate buffers, and were eluted with a linear NaCl gradient. HbD'' could be detected only in freshly prepared hemolysates with the sensitive FPLC separation method. The globin chains were separated on a cation exchanger (CM-cellulose), the tryptic peptides by HPLC with a RP-2 LiChrosorb column. Their amino-acid sequences were determined by automatic Edman degradation with the film- or gasphase method. For the .alpha.A-, .alpha.D- and .beta.-chains, peptide alignment was achieved by homologous comparison with the corresponding chains of the greylag goose (Anser anser). The structural significance of the substitutions was examined with the aid of molecular graphics. The oxygen-binding properties of the stripped hemolysate and of HbA HbD and their dependence on pH, temperature and inositol polyphosphate are presented and discussed with reference to molecular structures and hypothermy that occurs during torpidity.This publication has 31 references indexed in Scilit:
- High-Altitude Respiration of Birds. The Primary Structures of the αD-Chains of the Bar-headed Goose(Anser indicus),the Greylag Goose(Anser anser)and the Canada Goose(Branta canadensis)Biological Chemistry Hoppe-Seyler, 1986
- Die Hämoglobine des Feldsperlings(Passer montanus,Passeriformes). Die Sequenz der Haupt- (Hb A) und Nebenkomponente (Hb D)Biological Chemistry Hoppe-Seyler, 1985
- The crystal structure of human deoxyhaemoglobin at 1.74 Å resolutionJournal of Molecular Biology, 1984
- Hämoglobine vom Gemeinen Star(Sturnus vulgaris,Passeriformes). Die Primärstrukturen der αA, αD- und β-KettenHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1984
- Die Primärstruktur der α- und β-Ketten der Hauptkomponenten der Hämoglobine des Straußes(Struthio camelus)und des Nandus(Rhea americana) (Struthioformes).Aspekte zur Atmungsphysiologie und SystematikHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1983
- Hämoglobine, XLII. Untersuchungen am Hämoglobin der Graugans(Anser anser).Die Primärstruktur derα-und β-Ketten der HauptkomponenteHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1981
- Präparative Auftrennung des tryptischen Hydrolysats eines Proteins mit Hilfe der Hochdruck-Flüssigkeitschromatographie. Die Primärstruktur einer monoklonalen L-Kette vom K-Typ, Subgruppe I (Bence-Jones-Protein Wes)Hoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1980
- The protein data bank: A computer-based archival file for macromolecular structuresJournal of Molecular Biology, 1977
- Abnormal human haemoglobins: Separation and characterization of the α and β chains by chromatography, and the determination of two new variants, Hb chesapeake and Hb J (Bangkok)Journal of Molecular Biology, 1966
- Studies on the structure of hemoglobin I. Physicochemical properties of human globinBiochimica et Biophysica Acta, 1958