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Inositol hexaphosphate hemoglobin

Difference spectroscopy A Hemoglobin vs hemoglobin B Hemoglobin vs hemoglobin + inositol hexaphosphate... [Pg.157]

The observation by Chanutin and collaborators (CIO, S64) and by Benesch and Benesch (B25, B26) that 2,3-DPG (and also ATP and inositol hexaphosphate, or IHP) binds to hemoglobin resulting in a shift to the right of the oxygen dissociation curve has led to numerous reports which describe topics related to biochemical and medical aspects of the... [Pg.159]

Inositol (hexahydroxycyclohexane) occurs in several isomeric forms. Myo-inositol (or meso-inositol) is an important constituent of phospholipids and is the only isomer with biological activity. Inositol hexaphosphate (phytic acid) is found in avian erythrocytes, where it binds to hemoglobin, thereby regulating the oxygen capacity of the blood. It is also important as an intracellular messenger in a number of pathways. [Pg.927]

Inositol hexaphosphate is a component of the blood of birds that favors the release of oxygen from hemoglobin by a mechanism similar to that of 2,3-bisphosphoglycerate in other animals. [Pg.1303]

Fig. 18. Resonance Raman spectra of the (left) and (right) subunits of valency hybrid hemoglobins excited at 441.6 nm. (a) Isolated chain (pH 6.5) (b) stripped /nei-cyanide hybrid at pH 9.0 (c) mei-cyanide hybrid with inositol hexaphosphate (IHP) at pH 6.5 (d) stripped deoxyHb M Milwaukee at pH 6.5 (left) and stripped deoxyHb M Boston at pH 6.5 (right). All samples were in 50 mAf Bis-Tris/50 mAf Tris buffer. (From Nagai and Kitagawa. )... Fig. 18. Resonance Raman spectra of the (left) and (right) subunits of valency hybrid hemoglobins excited at 441.6 nm. (a) Isolated chain (pH 6.5) (b) stripped /nei-cyanide hybrid at pH 9.0 (c) mei-cyanide hybrid with inositol hexaphosphate (IHP) at pH 6.5 (d) stripped deoxyHb M Milwaukee at pH 6.5 (left) and stripped deoxyHb M Boston at pH 6.5 (right). All samples were in 50 mAf Bis-Tris/50 mAf Tris buffer. (From Nagai and Kitagawa. )...
Maxwell, J.C. Caughey, W.S. An infrared study of NO bonding to heme B and hemoglobin A. Evidence for inositol hexaphosphate induced cleavage of proximal histidine to iron bonds. Biochemistry 1976, 15, 388-396. Paoli, M. Dodson. G. Liddington, R.C. Wilkinson. A.J. Tension in haemoglobin revealed by Fe-His(F8) bond mpture in the fully liganded T-state. J. Mol. Biol. 1997, 271. 161-167. [Pg.643]

Gray RD, Gibson QH (1971) The effect of inositol hexaphosphate on the kinetics of CO and O2 binding by human hemoglobin. J Biol Chem 246 7168-7174... [Pg.108]

Nelson, D. P., Miller, W. D., and Kiesow, L. A., 1974, Calorimetric studies of hemoglobin function, the binding of 2,3-diphosphoglycerate and inositol hexaphosphate to human hemoglobin A, J. Biol. Chem. 249 4770. [Pg.57]

See other pages where Inositol hexaphosphate hemoglobin is mentioned: [Pg.166]    [Pg.491]    [Pg.228]    [Pg.166]    [Pg.156]    [Pg.157]    [Pg.156]    [Pg.688]    [Pg.126]    [Pg.164]    [Pg.1880]    [Pg.98]    [Pg.81]    [Pg.688]    [Pg.652]    [Pg.24]    [Pg.1879]    [Pg.164]    [Pg.6833]    [Pg.55]    [Pg.174]    [Pg.305]    [Pg.302]    [Pg.432]    [Pg.112]    [Pg.1585]    [Pg.7]    [Pg.1132]    [Pg.219]    [Pg.198]   
See also in sourсe #XX -- [ Pg.312 ]



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