Biol. Chem. Hoppe-Seyler Vol. 371, pp. 641-648, July 1990 Primary Structure and Oxygen-Binding Properties of the Hemoglobin from Guanaco (Lama guanacoe, Tylopoda)* Marco PicciNiNi a ,Traute KLEINSCHMIDT", Klaus D. JuRGENS h and Gerhard BRAUNiTZER at ;1 h Max-Planck-Institut für Biochemie, Abteilung Proteinchemie, Martinsried bei München Medizinische Hochschule Hannover, Abteilung Vegetative Physiologie, Hannover (Received 11 April 1990) Summary: The primary structure of the hemoglobin from guanaco (Lama guanacoe, Tylopoda) is presented. It could be separated into the chains by CMcellulose chromatography. The sequences have been determined by automatic Edman degradation with the film technique or gas phase method, using the native chains and the tryptic peptides of the oxidized chains as well as a fragment obtained by acid hydrolysis. Guanaco hemoglobin has identical -chains with alpaca and identical /3-chains with all Lama species with the exception that one guanaco in this study had alanine and serine in the ratio 1:1 in position 135 whereas a second individual had alanine only. Since the data suggest that the domesticated species llama and alpaca originate from the guanaco, it seems likely that /3135Ala is the common form. Guanaco, llama, and alpaca show a comparable high blood oxygen affinity, caused by the substitution
Biological Chemistry Hoppe-Seyler – de Gruyter
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