The Primary Structure of the Hemoglobin from the Australian Ghost Bat (Macroderma Gigas, Microchiroptera)

Singera G.A.M., Kleinschmidt T. and Braunitzera G. (1991) The Primary Structure of the Hemoglobin from the Australian Ghost Bat (Macroderma Gigas, Microchiroptera). Biological Chemistry Hoppe-Seyler, 372 2: 1089-1096. doi:10.1515/bchm3.1991.372.2.1089


Author Singera G.A.M.
Kleinschmidt T.
Braunitzera G.
Title The Primary Structure of the Hemoglobin from the Australian Ghost Bat (Macroderma Gigas, Microchiroptera)
Journal name Biological Chemistry Hoppe-Seyler   Check publisher's open access policy
ISSN 1437-4315
Publication date 1991
Sub-type Article (original research)
DOI 10.1515/bchm3.1991.372.2.1089
Volume 372
Issue 2
Start page 1089
End page 1096
Total pages 8
Subject 1303 Specialist Studies in Education
Abstract The Australian ghost bat (Macroderma gigas, Microchiroptera) has two hemoglobin components in the ratio 3:2. They share identical β-chains and differ by three replacements in the α-chains. The primary structures of all three chains are presented. They could be separated by high-performance liquid chromatography. The sequences were determined by automatic liquid and gas phase Edman degradation of the chains and their tryptic peptides.The two α-chains show 18 and 19 and the β-chains 15 exchanges compared to human α- and β-chains, respectively. The divergent evolution of Macroderma gigas and Megaderma lyra, two representatives of the family Megadermatidae, is discussed. An influence of replacements at functionally important positions on the hemoglobin oxygen affinity seems unlikely.
Keyword Australian ghost bat
hemoglobin
Macroderma gigas
Microchiroptera
primary structure
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
Collection: Scopus Import
 
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