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Hemoglobin binding

Hemoglobins bind four molecules of Oj per tetramer, one per heme. A molecule of Oj binds to a hemoglobin tetramer more readily if other Oj molecules are already bound (Figure 6-4). Termed cooperative binding, this phenomenon permits hemoglobin to maximize both the quantity of O2 loaded at the PO2 of the lungs and the quantity of O2 released at the PO2 of the peripheral tissues. Gooperative interactions, an exclusive property of multimeric proteins, are critically important to aerobic life. [Pg.42]

Fetal hemoglobin binds oxygen more tightly than HbA, and it has a decreased propensity to sickling. HbA2 also possesses this characteristic but to a lesser extent. RBCs that contain HbF sickle less readily than cells without. ISCs are found to have low HbF concentrations. In some patients, higher HbF may ameliorate the disease. [Pg.1006]

L3. Lathem, W., and Jensen, W., Plasma hemoglobin-binding capacity in sickle cell disease. Blood 14, 1047 (1959). [Pg.184]

N6. Nyman, M., On plasma proteins with heme or hemoglobin binding capacity. Scand. J. Clin, ir Lab. Invest. 12, 121 (1960). [Pg.185]

Tl. Tombs, M. P., Hemoglobin-binding -globulin in human serum. Nature 186, 1055 (1960). [Pg.186]

Bimer G, Albrecht W, Neumann H-G. 1990. Biomonitoring of aromatic amines III. Hemoglobin binding of benzidine and some benzidine congeners. Arch Toxicol 64(2) 97-102. [Pg.152]

Mehanna, A.S. Abraham, D.J. Comparison of crystal and solution hemoglobin binding of selected antigelling agents and allosteric modifiers. Biochemistry 1990, 29, 3944-3952. [Pg.482]

Hemoglobin binds Oj at the high PO2 (100 mm Hg) of the lung capillary beds and transports it to the peripheral tissues, where Poj is lower (-30 mm Hg) and O2 dissociates from hemoglobin. [Pg.15]

Bimer, G Neumatm, H.-G (1988) Biomonitoring of aromatic amines. II Hemoglobin binding of some monocyclic aromatic amines. Arch. Toxicol., 62, 110-115 Bollag, J.-M., Blattmann, P. Laanio, T. (1978) Adsorption and transformation of four substituted anilines in soil. J. Am. Food Chem., 26, 1302-1306 Bull, D.L. (1973) Metabolism of chlordimefon in cotton plants. Environ. EntomoL, 2, 869-871 Chemical Information Services (1999) Directory of World Chemical Producers (Version 99.1.0) [CD-ROM], Dallas, TX... [Pg.336]

Hemoglobin binds oxygen with increasing affinity. [Pg.29]

Figure 7.17 Gel electrophoresis of haptoglobins. Haptoglobin 1-1 moves as a single component, whereas the other two types show genetically derived polymorphisms. Hemoglobin-binding activity is identical in the three types. Figure 7.17 Gel electrophoresis of haptoglobins. Haptoglobin 1-1 moves as a single component, whereas the other two types show genetically derived polymorphisms. Hemoglobin-binding activity is identical in the three types.

See other pages where Hemoglobin binding is mentioned: [Pg.1148]    [Pg.40]    [Pg.1148]    [Pg.484]    [Pg.584]    [Pg.1481]    [Pg.1483]    [Pg.164]    [Pg.150]    [Pg.151]    [Pg.153]    [Pg.277]    [Pg.228]    [Pg.346]    [Pg.32]    [Pg.112]    [Pg.334]    [Pg.512]    [Pg.305]    [Pg.348]    [Pg.164]    [Pg.170]    [Pg.171]    [Pg.172]    [Pg.174]    [Pg.42]    [Pg.463]    [Pg.1757]    [Pg.1155]    [Pg.156]    [Pg.270]    [Pg.200]    [Pg.171]    [Pg.217]    [Pg.221]    [Pg.153]    [Pg.157]    [Pg.118]    [Pg.147]    [Pg.269]   
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See also in sourсe #XX -- [ Pg.2 , Pg.2 , Pg.2 , Pg.3 , Pg.6 , Pg.8 ]

See also in sourсe #XX -- [ Pg.278 ]




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Binding of oxygen to myoglobin and hemoglobin

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Carbon monoxide binding to hemoglobin

Carbon monoxide binding to hemoglobin and myoglobin

Dioxygen binding to hemoglobin

Equilibrium constants hemoglobin tetramers, oxygen binding

Hemoglobin 2,3-bisphosphoglycerate binding

Hemoglobin Adair binding model

Hemoglobin Aic binding, folate

Hemoglobin Is an Allosteric Oxygen-Binding Protein

Hemoglobin Oxygen binding

Hemoglobin and oxygen binding

Hemoglobin binding reactions

Hemoglobin carbon monoxide binding

Hemoglobin cooperative oxygen binding

Hemoglobin dioxygen binding

Hemoglobin myoglobin oxygen binding

Hemoglobin oxygen binding cooperativity

Hemoglobin oxygen binding curve

Hemoglobin sigmoidal binding curve

Hemoglobin, iron binding

Nitric oxide binding to hemoglobin

Oxygen binding by hemoglobin

Oxygen binding to hemoglobin

Oxygen binding, hemoglobin, calculations

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