Summary
Oxygen affinity and number of -SH groups of hemoglobins have rather constant values for hens belonging to Leghorn, Whiterock, Rhode Island Red, Sussex and Cornish breeds, and for hybrids between Rhode Island Red and Leghorn, irrespective of the breed. Number of -SH groups in red cell hemolysates amounts to 8 per mole Hb (7,88 – 8,48) , logp50=1,04–0,94; value of “n” for Leghorns is 1,70, for Whiterocks 2,80.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
Literature
Antonini, E.; Brunori, M.: Hemoglobin and myoglobin in their reactions with ligands. Amsterdam-London: Ac. Press 1971
Asakura, T.; Kawai, Y.; Yoneyama, Y.; Yoshikawa, H.: Use of sodium b lorophydride in determination of oxygen dissocation curves of hemoglobin. Anal. Biochemistry 7, 393–400 (1964)
Benesch, R.; Benesch, R.E.; Chi, Ing Ku: Reciprocal binding of oxygen and diphosphoglycerate by human hemoglobin. Proc. Natl. Acad. Sci. USA 59, 526–532 (1968)
Boyer, P.D.: Spectrophotometric study of the reaction of protein sulfhydryl groups with organic mercurials. J. Amer. Chem. Soc. 76, 4331–4337 (1954)
D'Amelio, V.: The globins of adult and embryonic chick hemoglobin. Biochim. Biophys. Acta 127, 59–65 (1966)
D'Amelio, V.; Salvo, A.M.: The serological specifity of chicken hemoglobin fractions. Z. Naturforschg. 14b, 455–457 (1959)
Dunlap, J.S.; Johnson, V.L.; Farner, D.S.: Multiple hemoglobins in birds. Experientia 12, 352–353 (1956)
Gondko, R.: Połączenie hemoglobina — polifosforan i jego rola w organiźmie. Post. Biochemii 18, 323–336 (1972)
Huisman, T.H.J.; Schillhorn Veen, J.M.; Dozy, A.M.; Nechtman, C.M.: Studies of animal hemoglobins. II. The influence of inorganic phosphate on the physico — chemical and physiological properties of the hemoglobin of the adult chicken. Biochem. Biophys. Acta 88, 352–366 (1964)
Kołątaj, A.: Electrophoretic investigations of haemoglobin in chickens in connection with heterosis. Acta Physiol. Polonica 14, 1, 115–120 (1963)
Matsuda, G.; Maita, T.; Nakajima, H.: The N-terminal residues of chicken hemoglobin. J. Biochem. 56, 490–491 (1964)
Muller, C.J.: A comparative study on the structure of mammalian and avian haemoglobin. Groningen 1961
Ochai, T.; Gotoh, T.; Shikama, K.: Effect of intracellular organic phosphates on the oxygen equilibrium curve of chickens hemoglobin. Arch. Biochem. Biophys. 149, 316–322 (1972)
Oshima, M.; Taylor, T.G.; Williams, A.W.: Variations in the concentration of phytic acid in the blood of the domestic fowl. Biochem. J. 92, 42–46 (1964)
Riggs, A.: The nature and significance of the Bohr effect in mammalian hemoglobin. J. Gen. Phys. 43, 737–752 (1969)
Saha, A.: Comparative studies on chick hemoglobins. Biochem. Biophys. Acta 93, 573–584 (1964)
Schall, H.; Turba, F.: Trennung und Identifizierung von Hemoglobin aus Hühner — Reticulocyten. Biochem. Z. 339, 219–223 (1963)
Schnek, A.G.; Paul, C.; Monier, C.; Leonis, J.: Molecular variation in avian haemoglobins. VI. Internationales Berliner Symposium über Struktur und Funktion der Erythrozyten, Berlin (1972)
Van der Helm, H.J.; Huisman, T.H.J.: The two hemoglobin components of the chicken. Science 127, 762–768 (1958)
Wierzbicki, R.: Fizyko — chemiczne i funkcjonalne właściwości hemoglobiny jader erytrocytówptaków. Uniwersytet Łódzki, Łódź (1974)
Author information
Authors and Affiliations
Additional information
Communicated by S. Barbacki
This work was performed within the project 09.3.1 of Polish Academy of Sciences.
Rights and permissions
About this article
Cite this article
Gondko, R., Kołątaj, A. & Rózga, B. Oxygen affinity of red cells hemolysates of different hen breeds. Theoret. Appl. Genetics 48, 285–287 (1976). https://doi.org/10.1007/BF00264960
Received:
Issue Date:
DOI: https://doi.org/10.1007/BF00264960