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Volumn 20, Issue 9, 2003, Pages 1087-1093

Significance of Affinity and Cooperativity in Oxygen Binding to Hemoglobin of Horse Fetal and Maternal Blood

Author keywords

Cooperativity; Effectiveness of the Bohr effect; Hemoglobin; Horse; O2 Hb equilibrium curve

Indexed keywords

2,3 DIPHOSPHOGLYCERIC ACID; HEMOGLOBIN; OXYGEN;

EID: 0346973882     PISSN: 02890003     EISSN: None     Source Type: Journal    
DOI: 10.2108/zsj.20.1087     Document Type: Article
Times cited : (5)

References (25)
  • 1
    • 0001314221 scopus 로고
    • 2 equilibrium curve of hemoglobin
    • 2 equilibrium curve of hemoglobin. J Biol Chem 63: 529-545
    • (1925) J Biol Chem , vol.63 , pp. 529-545
    • Adair, G.S.1
  • 2
    • 84935023004 scopus 로고
    • Ubereinen in biologischer Beziehung wichtigen Einfluss, den die Kohlensaeurespannung des Blutes auf dessen Sauerstoffbindung ubt
    • Bohr C, Hasselbalch KA, Krogh A (1904) Ubereinen in biologischer Beziehung wichtigen Einfluss, den die Kohlensaeurespannung des Blutes auf dessen Sauerstoffbindung ubt. Skand Arch Physiol 16: 402-412
    • (1904) Skand Arch Physiol , vol.16 , pp. 402-412
    • Bohr, C.1    Hasselbalch, K.A.2    Krogh, A.3
  • 3
    • 0015694442 scopus 로고
    • Hemoglobin function in the horse: The role of 2,3-diphosphoglycerate in modifying the oxygen affinity of maternal and fetal blood
    • Bunn HF, Kitchen H (1973) Hemoglobin function in the horse: The role of 2,3-diphosphoglycerate in modifying the oxygen affinity of maternal and fetal blood. Blood 42: 471-479
    • (1973) Blood , vol.42 , pp. 471-479
    • Bunn, H.F.1    Kitchen, H.2
  • 4
    • 0027135394 scopus 로고
    • Comparative study of the oxy-haemoglobin dissociation curve of four mammals: Man, Dog, Horse and Cattle
    • Clerbaux TH, Gusti P, Detry B, Cao ML, Frans A (1993) Comparative study of the oxy-haemoglobin dissociation curve of four mammals: Man, Dog, Horse and Cattle. Comp Biochem Physiol 106A: 687-694
    • (1993) Comp Biochem Physiol , vol.106 A , pp. 687-694
    • Clerbaux, T.H.1    Gusti, P.2    Detry, B.3    Cao, M.L.4    Frans, A.5
  • 5
    • 0016171242 scopus 로고
    • A comparative study of blood gas tensions, oxygen affinity and red cell 2,3-DPG concentrations in fetal and maternal blood in the mare, cow and sow
    • Comline RS, Silver M (1974) A comparative study of blood gas tensions, oxygen affinity and red cell 2,3-DPG concentrations in fetal and maternal blood in the mare, cow and sow. J Physiol 242: 805-826
    • (1974) J Physiol , vol.242 , pp. 805-826
    • Comline, R.S.1    Silver, M.2
  • 6
    • 84910350698 scopus 로고
    • Placental transfer of blood gases
    • Comline RS, Silver M (1975) Placental transfer of blood gases. Br Med Biull 31: 25-31
    • (1975) Br Med Biull , vol.31 , pp. 25-31
    • Comline, R.S.1    Silver, M.2
  • 7
  • 8
    • 0005656280 scopus 로고
    • A modified method for the determination of 2,3-diphosphoglycerate in erythrocytes
    • Ericson A, Verdier CH (1972) A modified method for the determination of 2,3-diphosphoglycerate in erythrocytes. Scand J Clin Lab Inv 29: 85-90
    • (1972) Scand J Clin Lab Inv , vol.29 , pp. 85-90
    • Ericson, A.1    Verdier, C.H.2
  • 9
    • 0000400174 scopus 로고
    • Micro determination of oxyhemoglobin, methemoglobin, and sulfhemoglobin in a single sample of blood
    • Evelyn KA, Malloy HT (1938) Micro determination of oxyhemoglobin, methemoglobin, and sulfhemoglobin in a single sample of blood. J Biol Chem 126: 655-662
    • (1938) J Biol Chem , vol.126 , pp. 655-662
    • Evelyn, K.A.1    Malloy, H.T.2
  • 10
    • 0034304171 scopus 로고    scopus 로고
    • Determinants of oxygen delivery and hemoglobin saturation during incremental exercise in horses
    • Fenger CK, McKeever KH, Hinchcliff KW, Kohn CW (2000) Determinants of oxygen delivery and hemoglobin saturation during incremental exercise in horses. Am J Vet Res 61: 1325-1332
    • (2000) Am J Vet Res , vol.61 , pp. 1325-1332
    • Fenger, C.K.1    McKeever, K.H.2    Hinchcliff, K.W.3    Kohn, C.W.4
  • 11
    • 0015790339 scopus 로고
    • An enzymatic reduction system for met-myoglobin, and its application to functional studies of oxygen carrier
    • Hayashi A, Suzuki T, Shin M (1973) An enzymatic reduction system for met-myoglobin, and its application to functional studies of oxygen carrier. Biochim Biophys Acta 310: 309-316
    • (1973) Biochim Biophys Acta , vol.310 , pp. 309-316
    • Hayashi, A.1    Suzuki, T.2    Shin, M.3
  • 12
    • 0003043542 scopus 로고
    • The possible effects of aggregation of the molecule on its dissociation curve
    • Hill AV (1910) The possible effects of aggregation of the molecule on its dissociation curve. J Physiol 18: 4-7
    • (1910) J Physiol , vol.18 , pp. 4-7
    • Hill, A.V.1
  • 13
    • 0017577243 scopus 로고
    • The hemoglobin-oxygen equilibrium associated with subunit dissociation. 1. An approach with the Hill scheme
    • Imai K, Yonetani T (1977) The hemoglobin-oxygen equilibrium associated with subunit dissociation. 1. An approach with the Hill scheme. Biochim Biophys Acta 490: 164-170
    • (1977) Biochim Biophys Acta , vol.490 , pp. 164-170
    • Imai, K.1    Yonetani, T.2
  • 14
    • 0019738497 scopus 로고
    • Measurement of accurate oxygen equilibrium curves by an automatic oxygenation apparatus
    • Imai K (1981) Measurement of accurate oxygen equilibrium curves by an automatic oxygenation apparatus. Meth Enzymol 76: 438-449
    • (1981) Meth Enzymol , vol.76 , pp. 438-449
    • Imai, K.1
  • 15
    • 0005768993 scopus 로고
    • Correlations between the Monod Wyman Changeux model parameters and their implications in oxygenation of mammalian haemoglobins
    • (AG Schnek & C Paul, eds.), Brussels Free University, Brussels
    • Imai K (1984) Correlations between the Monod Wyman Changeux model parameters and their implications in oxygenation of mammalian haemoglobins. In Hemoglobin (AG Schnek & C Paul, eds.), Brussels Free University, Brussels, pp 83-102
    • (1984) Hemoglobin , pp. 83-102
    • Imai, K.1
  • 16
    • 0035639316 scopus 로고    scopus 로고
    • A new look on the position of the oxygen equilibrium curve of human adult hemoglobin at rest and during exercise with special reference to the effectiveness of the Bohr shift
    • Itoh R, Sasagawa K, Kimura S, Ishigaki K, Imai K, Kobayashi M (2001) A new look on the position of the oxygen equilibrium curve of human adult hemoglobin at rest and during exercise with special reference to the effectiveness of the Bohr shift. Zool Sci 18: 905-908
    • (2001) Zool Sci , vol.18 , pp. 905-908
    • Itoh, R.1    Sasagawa, K.2    Kimura, S.3    Ishigaki, K.4    Imai, K.5    Kobayashi, M.6
  • 17
    • 0028267930 scopus 로고
    • Shape of the haemoglobin-oxygen equilibrium curve and oxygen transport efficiency
    • Kobayashi M, Ishigaki K, Kobayashi M, Imai K (1994) Shape of the haemoglobin-oxygen equilibrium curve and oxygen transport efficiency. Respir Physiol 95: 321-328
    • (1994) Respir Physiol , vol.95 , pp. 321-328
    • Kobayashi, M.1    Ishigaki, K.2    Kobayashi, M.3    Imai, K.4
  • 19
    • 0348124257 scopus 로고
    • The oxygen affinity of human maternal and fetal hemoglobin
    • MaCarthy EF (1943) The oxygen affinity of human maternal and fetal hemoglobin. J Physiol 102: 55-61
    • (1943) J Physiol , vol.102 , pp. 55-61
    • MaCarthy, E.F.1
  • 20
    • 0031084817 scopus 로고    scopus 로고
    • The hemoglobin polymorphism of the Sardinian wild draft horse and the oxygen binding properties of the four different horse hemoglobins
    • Pellegrini MG, Corda EM, Manga L, Olianas A, Sanna MT, Fais A, Masala B (1996) The hemoglobin polymorphism of the Sardinian wild draft horse and the oxygen binding properties of the four different horse hemoglobins. Ital J Biochem 46: 7-14
    • (1996) Ital J Biochem , vol.46 , pp. 7-14
    • Pellegrini, M.G.1    Corda, E.M.2    Manga, L.3    Olianas, A.4    Sanna, M.T.5    Fais, A.6    Masala, B.7
  • 22
    • 0020083889 scopus 로고
    • 50 of hemoglobin?
    • 50 of hemoglobin? Anesthesia 37: 640-645
    • (1982) Anesthesia , vol.37 , pp. 640-645
    • Sold, M.J.1
  • 25
    • 0038105021 scopus 로고    scopus 로고
    • The cooperativity of human fetal and adult hemoglobins is optimized: A consideration based on the effectiveness of the Bohr shift
    • Zhang Y, Miki M, Sasagawa K, Kobayashi M, Imai K, Kobayashi M (2003) The cooperativity of human fetal and adult hemoglobins is optimized: a consideration based on the effectiveness of the Bohr shift. Zool Sci 20: 23-29
    • (2003) Zool Sci , vol.20 , pp. 23-29
    • Zhang, Y.1    Miki, M.2    Sasagawa, K.3    Kobayashi, M.4    Imai, K.5    Kobayashi, M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.