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Biomedical subjects

I Tyuma

Publications and source records attributed to I Tyuma.

At least 37 records · Page 2Linked to original sources
PubMed1981

Functional abnormalities of hemoglobin Toyoake (142 (H20)beta, Ala leads to Pro).

Oxygen equilibrium of Hb Toyoake (142 (H20)beta, Ala leads to Pro) is characterized by an oxygen affinity 6-times higher than that of Hb A, a slightly decreased alkaline Bohr effect, diminished cooperativity, with Hill's coefficient decreased by 1.2, and reduced response to 2,3-diphosphoglycerate and inositol hexaphosphate. These properties are in qualitative agreement with those shown previously from oxygen equilibrium data for hemolysate containing Hb Toyoake. The heat of oxygenation was -13.5 kcal/mol for Hb Toyoake and -12.9 kcal/mol for Hb A at pH 7.4 in 0.1 M Cl- and they became equal when corrected for the heat of oxygen-linked proton and Cl- release. OxyHb Toyoake autooxidized faster than oxyHb A. The visible absorption spectrum and electron paramagnetic resonance spectrum of oxidized Hb Toyake indicated that oxidation of this hemoglobin, either by autooxidation or by K3Fe(CN)6, is followed by gradual conversion into hemichrome derivatives. The soret peak of deoxyHb Toyoake was lowered compared to that of deoxyHb A and the magnitude of narrow-banded oxy-minus-deoxy difference spectrum around 290 nm was smaller for Hb Toyoake than for Hb A, indicating that the former remains predominantly in the R state upon deoxygenation. The functional abnormalities, including tendency to lose heme groups previously reported, were interpreted in terms of structural disturbance by proline at 142beta of 141 leucine, 143 histidine, 145 tyrosine, and 146 histidine residues of the same beta chain.

Diphosphoglyceric Acids↗
PubMed1981

Prediction of the carbonmonoxyhemoglobin levels during and after carbon monoxide exposures in various animal species.

The equation derived by Coburn, Forster, and Kane (1965) for the absorption and elimination processes of carbon monoxide was solved analytically with less-restrictive assumptions. The solution can predict the COHb levels during and after exposures of 50 to 500 ppm CO not only in human subjects but also in rats and mice with reasonable accuracy, except for the CO elimination by breathing hyperbaric oxygen. Physiological parameters required for the prediction are only body mass and hemoglobin concentration. It has been shown that the rate of both processes is inversely proportional to B0.24 in mammals, where B is the body mass: the smaller the animal, the faster the rate of both absorption and elimination.

Absorption↗
PubMed1980

Further studies on the functional properties of hemoglobin M Hyde Park.

The oxygen binding properties of Hb M Hyde Park (92 beta, histidine leads to tyrosine) were reinvestigated directing special care to testing the wave length-dependence of the oxygen equilibrium curve and to stabilizing hemoglobin samples using a methemoglobin reductase system. There was no indication that the Hb M Hyde Park fraction separated on a DEAE Sephadex column contained an unknown hemoglobin derivative which appeared in earlier studies. Contrary to earlier observations, there was no significant wave length-dependence of the equilibrium curve of Hb M Hyde Park, verifying the spectrophotometric determination of oxygen saturation. The reductase system satisfactorily reduced the normal alpha chain met hemes without reducing the abnormal beta chain met hemes. The oxygen binding property of Hb M Hyde Park is characterized by 3 to 4 times higher oxygen affinity than that for normal hemoglobin, complete loss of cooperativity, and substantially preserved Bohr effect. These results are consistent in part but not entirely with those observed by earlier investigators. The oxygen affinity of Hb M Hyde Park is between the affinity of the oxy structure and the deoxy structure of normal hemoglobin. Oxygen equilibrium curve of red cell suspension and whole hemolysate containing Hb M Hyde Park were biphasic, indicating that Hb M Hyde Park also exhibited the high oxygen affinity in those samples.

Cytochrome-B(5) Reductase↗
PubMed1979

Influence of steric factors on oxygen binding. I. Studies on 2,4-diisopropyldeuteroheme-myoglobin.

Sperm whale apomyoglobin was recombined with 2,4-diisopropyldeuterohemin to form 2,4-diisopropyldeuteroheme-myoglobin and its various physico-chemical properties were investigated to get an insight into the structural and functional role of the peripheral vinyl groups. 2,4-Diisopropyldeuteroheme-myoglobin showed a four times lower oxygen affinity at 25 degrees C and larger enthalpy and entropy changes of oxygenation than the corresponding values of native myoglobin. 2,4-Diisopropyldeuteroheme-metmyoglobin shows a pKa value of 9.68 which is higher than those of native metmyoglobin and mesoheme-metmyoglobin. The rate of autooxidation of oxy-form was about seven times larger in 2,4-diisopropyldeuteroheme-myoglobin than in native myoglobin. The electron-donating effect of isopropyl groups does not give straightforward explanation for these anomalous properties of 2,4-diisopropyldeuteroheme-myoglobin. It is proposed that site and stereospecific van der Waals' interaction between the polypeptide side chains and the peripheral 2,4-diisopropyl groups may weaken the interaction between the bound oxygen molecule and the distal His, resulting in the decrease in the stability of oxyform.

Animals↗
PubMed1979

Stoichiometry of the reaction of oxyhemoglobin with nitrite.

During the reaction of oxyhemoglobin (HbO2) with nitrite, the concentration of residual nitrite, nitrate, oxygen, and methemoglobin (Hb+) was determined successively. The results obtained at various pH values indicate the following stoichiometry for the overall reaction: 4HbO2 + 4NO2- 4H+ leads to 4Hb+ + 4NO3- + O2 + 2H2 O (Hb denotes hemoglobin monomer). NO2- binds with methemoglobin noncooperatively with a binding constant of 340 M-1 at pH 7.4 and 25 degrees C. Thus, the major part of Hb+ produced is aquomethemoglobin, not methemoglobin nitrite, when less than 2 equivalents of nitrite is used for the oxidation.

Hemoglobin A↗
PubMed1979

The linkage between the four-step binding of oxygen and the binding of heterotropic anionic ligands in hemoglobin.

The linkage between the four-step binding of oxygen and the binding of heterotropic anionic ligands in hemoglobin was investigated by accurately measuring and analyzing the oxygen equilibrium curves of human adult hemoglobin in the presence and absence of various concentrations of one or two of the following materials: chloride (Cl-), 2,3-diphosphoglycerate (DPG), and inositol hexaphosphate (IHP). Each equilibrium curve was analyzed according to the Adair equation to evaluate the four-step oxygen equilibrium constants (Adair constants) and the median oxygen pressure. The binding constants of the anions for the molecular species of hemoglobin carrying j oxygen molecules, Hb(O2)j(j=0,1,...,4), were evaluated from the dependences of the Adair constants and the median oxygen pressure on the anion concentration by introducing a model which takes the competitive binding of Cl- and DPG or IHP into account. Assumptions made in the model are: (a) the hemoglobin molecule has two oxygen-linked binding sites for Cl- which are equivalent and independent and (b) no Cl- can be bound to hemoglobin to which DPG or IHP is already bound and vice versa. Thus, we could obtain values for the intrinsic binding constants of Cl- and DPG, i.e., the constants in the absence of other competitive anions. For IHP, only the binding constants and apparent binding constants for Hb and Hb(O2)2 were obtained. Values of the Cl- binding constants and apparent binding constants for DPG and IHP, i.e., the binding constants in the presence of Cl- for Hb and Hb(O2)4, were in reasonable agreement with literature values. From the binding constants we calculated anion binding curves for Hb(O2)j(J=0,1,...,4), the number of anions bound to Hb(O2)J, And the relationship between fractional anion saturation of hemoglobin and fractional oxygen saturation. The numbers of released anions are not uniform with respect to oxygenation step. This non-uniformity is the reason for the changes in the shape of the oxygen equilibrium curve with anion concentration changes and for the non-uniform dependences of the Adair constants on anion concentration, and also results in non-linear relations between anion saturation and oxygen saturation. The anion binding constants and various binding properties of the anions derived from those constants are consistent with those observed by other investigators using different techniques, indicating that the present model describes the oxygen-linked competitive anion binding well.

Adult↗
PubMed1978

On the validity of the spectrophotometric determination of oxygen saturation of hemoglobin. The wavelength dependence of observed oxygen equilibrium parameter values.

Spectral changes of oxyhemoglobin induced by such anions as 2,3-diphosphoglycerate, inositol hexaphosphate, and Cl- may affect the validity of the spectrophotometric determination of oxygen saturation of hemoglobin. Therefore, the anion-induced difference spectra were extensively measured under a variety of conditions and accurate oxygen equilibrium curves were determined under representative conditions with detection at different wavelengths selected from peaks, troughs, and zero difference points of the difference spectra in the visible and Soret regions. Oxygen equilibrium parameters including the four Adair constants (i.e., equilibrium constants for four steps of oxygenation) estimated from the equilibrium curves did not show any dependence on wavelength within the limits of experimental error. These results indicate that anion-induced spectral changes do not invalidate the spectrophotometric determination of oxygen saturation and confirm the validity of the previous conclusions drawn in our series of studies on the effects of anions, pH and temperature on oxygen equilibrium parameters.

Diphosphoglyceric Acids↗
PubMed1977

Evaluation of severinghaus' equation and its modification for 2, 3-dpg.

Severinghaus' equation can safely be used for the indirect estimation of oxygen half saturation pressure (P50) on the basis of blood gas parameters in normal subjects. However, 139 blood samples from 65 patients with severe injuries, the estimated P50 values differed significantly from directly measured values. The difference is highly correlated to the molar ratio of 2, 3-diphosphoglycerate to hemoglobin tetramer (2, 3-DPG ratio, [DPG]). Using this correlation, a modified Severinghaus' equation, including 2, 3-DPG molar ratio, was derived: i.e.,deltalog Po2 equals +0.48 (7.4-pH)+0.024 (T-37), +0.0013BE+0.135[DPG]-0.116 where deltalog Po2 is the shift from the standard oxygen dissociation curve, pH is plasma pH, and T and BE refer to temperature and base excess of blood, respectively. The modified equation enables one to indirectly estimate Po2 and oxygen saturation with an accuracy of plus or minus 2.5 mmHg and plus or minus 5 percent, respectively, based on blood gas parameters and 2, 3-DPG molar ratio in most clinical cases. The limitations of the equation was discussed.

Diphosphoglyceric Acids↗
PubMed1976

Effect of carbon monoxide on equilibrium between oxygen and hemoglobin.

Oxygen dissociation curves of partially CO-saturated human whole blood drawn freshly or preserved more than 3 wk were studied. With increasing CO-hemoglobin concentrations, oxygen affinity of the blood increased and the Hill coefficient, n, fell and gradually approached unity. The changes induced by CO-hemoglobin showed practically no difference in the presence or absence of 2,3-diphosphoglycerate. The Bohr coefficient, deltalog P50/deltapH, was determined as a function of oxygen saturation for various concentrations of CO-hemoglobin. The coefficient remained essentially unchanged in the presence of CO-hemoglobin. In the presence of less than 50% CO-hemoglobin, a good agreement was observed between the observed oxygen dissociation curves and the curves calculated according to Roughton and Darling (Am. J. Physiol. 141: 17-31, 1944). Based on these results, physiological implications of carboxyhemoglobinemia are discussed quantitatively in comparison with methemoglobinemia.

Carboxyhemoglobin↗