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http://purl.uniprot.org/citations/6479896http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/6479896http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/6479896http://www.w3.org/2000/01/rdf-schema#comment"The primary structure of the haemoglobin of the African Elephant (Loxodonta africana) is reported. The sequence was determined by means of a sequenator. The haemoglobin differs in 26 amino acids in the alpha-chains and in 27 in the beta-chains from that of adult human haemoglobin. The haemoglobin of the African Elephant, like that of the Indian Elephant and Ilama, has only 5 binding sites for polyphosphate. This finding explains the low p(O2)50 value in whole blood as a result of the lower 2,3-bisphosphoglycerate-haemoglobin interaction. This is discussed in relation to aspects of respiratory physiology; some points are also of interest with regard to the Second Punic War and Hannibal's crossing of the Alps."xsd:string
http://purl.uniprot.org/citations/6479896http://purl.org/dc/terms/identifier"doi:10.1515/bchm2.1984.365.2.743"xsd:string
http://purl.uniprot.org/citations/6479896http://purl.org/dc/terms/identifier"doi:10.1515/bchm2.1984.365.2.743"xsd:string
http://purl.uniprot.org/citations/6479896http://purl.uniprot.org/core/author"Braunitzer G."xsd:string
http://purl.uniprot.org/citations/6479896http://purl.uniprot.org/core/author"Braunitzer G."xsd:string
http://purl.uniprot.org/citations/6479896http://purl.uniprot.org/core/author"Schrank B."xsd:string
http://purl.uniprot.org/citations/6479896http://purl.uniprot.org/core/author"Schrank B."xsd:string
http://purl.uniprot.org/citations/6479896http://purl.uniprot.org/core/author"Wiesner H."xsd:string
http://purl.uniprot.org/citations/6479896http://purl.uniprot.org/core/author"Wiesner H."xsd:string
http://purl.uniprot.org/citations/6479896http://purl.uniprot.org/core/author"Krombach C."xsd:string
http://purl.uniprot.org/citations/6479896http://purl.uniprot.org/core/author"Krombach C."xsd:string
http://purl.uniprot.org/citations/6479896http://purl.uniprot.org/core/author"Stangl A."xsd:string
http://purl.uniprot.org/citations/6479896http://purl.uniprot.org/core/author"Stangl A."xsd:string
http://purl.uniprot.org/citations/6479896http://purl.uniprot.org/core/date"1984"xsd:gYear
http://purl.uniprot.org/citations/6479896http://purl.uniprot.org/core/date"1984"xsd:gYear
http://purl.uniprot.org/citations/6479896http://purl.uniprot.org/core/name"Hoppe-Seyler's Z. Physiol. Chem."xsd:string
http://purl.uniprot.org/citations/6479896http://purl.uniprot.org/core/name"Hoppe-Seyler's Z. Physiol. Chem."xsd:string
http://purl.uniprot.org/citations/6479896http://purl.uniprot.org/core/pages"743-749"xsd:string
http://purl.uniprot.org/citations/6479896http://purl.uniprot.org/core/pages"743-749"xsd:string
http://purl.uniprot.org/citations/6479896http://purl.uniprot.org/core/title"Phosphate-haemoglobin interaction. The primary structure of the haemoglobin of the African elephant (Loxodonta africana, Proboscidea): asparagine in position 2 of the beta-chain."xsd:string
http://purl.uniprot.org/citations/6479896http://purl.uniprot.org/core/title"Phosphate-haemoglobin interaction. The primary structure of the haemoglobin of the African elephant (Loxodonta africana, Proboscidea): asparagine in position 2 of the beta-chain."xsd:string
http://purl.uniprot.org/citations/6479896http://purl.uniprot.org/core/volume"365"xsd:string
http://purl.uniprot.org/citations/6479896http://purl.uniprot.org/core/volume"365"xsd:string