The primary structure of the egyptian fruit bat (rousettus aegyptiacus, chiroptera) hemoglobin
Hoppe-Seyler's Zeitschrift fur Physiologische Chemie, ISSN: 1437-4315, Vol: 363, Issue: 2, Page: 1209-1216
1982
- 13Citations
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Metrics Details
- Citations13
- Citation Indexes13
- 13
- CrossRef10
Article Description
Das Hämoglobin des ägyptischen Flughundes (Rousettus aegyptiacus) hat nur eine Komponente. Die Trennung der α-und β-Ketten gelang durch Chromatographie an CM-52-Cellulose. Die vollständige Primärstruktur beider Ketten wurde durch automatischen Edman-Ab-bau an den Ketten und den tryptischen Peptiden bestimmt.Die Zuordnung der Sequenzen erfolgte aufgrund der Homologie zu den Ketten des adulten Humanhämoglobins. Die Zahl der Substitutionen zwischen Flughund- und Humanhämoglobin liegt für die α-Ketten bei 14, für die β-Ketten bei 19 Resten und ist damit für die große phylogenetische Distanz zwischen Primaten und Mega-chiropteren sehr gering. In den für die Funktion wichtigen Positionen wurden in den α-und β-Ketten nur je ein Austausch in der Umgebung des Häms und einer bzw. zwei in den α1 β1 -Bindungsstellen gefunden. Die Sequenzdaten deuten auf eine normale Sauerstoffaffinität des Flughundhämoglobins hin, die auch von Jürgens et al. gefunden wurde. © Copyright 1982 by Walter de Gruyter & Co.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0020198707&origin=inward; http://dx.doi.org/10.1515/bchm2.1982.363.2.1209; https://www.degruyter.com/document/doi/10.1515/bchm2.1982.363.2.1209/html; https://www.degruyter.com/document/doi/10.1515/bchm2.1982.363.2.1209/pdf; https://www.degruyter.com/view/j/bchm2.1982.363.issue-2/bchm2.1982.363.2.1209/bchm2.1982.363.2.1209.xml
Walter de Gruyter GmbH
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