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At least 19 recordsLinked to original sources
PubMed1979

Accuracy sensitivity to carboxyhemoglobin, and speed of response of the Hewlett-Packard 47201A ear oximeter.

We have shown that the Hewlett-Packard 47201A ear oximeter measures arterial O2 saturation within 95 per cent confidence limits of +/- 4 per cent when arterial blood saturation is more than 65 per cent, but at lower saturations the oximeter consistently provides a reading that is too low. The oximeter is sensitive to carboxyhemoglobin, progressively overestimating arterial saturation as carboxyhemoglobin concentration increases from 0 to 18 per cent. The time response is exponential, with a normal time constant of 3 sec, but this is halved in the fast mode or operation.

Carboxyhemoglobin↗
PubMed1976

Dissociation of CO from carboxyhemoglobin.

The reaction between carboxyhemoglobin and reduced microperoxidase (MP): Hb4(CO)4 + 4MP=Hb4 + 4MPCO, recently reported by us, has been further studied. By generating species Hb4(CO), Hb4(CO)2, and Hb(CO)3 in the stopped flow cuvette by the reaction of dithionite with the species of the general formula Hb4(O2)x(CO)y(x + y=4) in the presence of microperoxidase it has been possible to determine the stepwise CO dissociation rate constants l4, l3, l2, and l1. The overall CO dissociation rate constant l, which is the same in this system as l4, is not affected by 2,3-diphosphoglyceric acid. The activation energy of the reaction is 21,400 cal in 15-25 degrees range. The ratio deltal/deltapH is approximately 3 in 6.5 to 7.5 pH range. The kinetic data indicate that, compared to HbO2, the contribution to the cooperativity of the dissociation rate constants of carboxyhemoglobin is greatly reduced. The ligand-dependent differences in the reactions of Hb with CO, O2, and NO suggest that in the combination reactions the ligand plays an active role in the rate-limiting step.

Carbon Monoxide↗
PubMed1975

Lack of relationship of red cell enzyme activity to bilirubin and carboxyhemoglobin levels in healthy term infants.

A total of 32 term infants were studied in an attempt to confirm and extend the recent observation of Petrich & associates (14) that minor degrees of transient deficiences of the red cell enzymes glucose phosphate isomerase and glyceraldehyde-3-phosphate dehydrogenase were related to hyperbilirubinemia in otherwise healthy term infants. No relationships could be observed between the activity of these enzymes and the bilirubin level on day three. In addition, no correlation was present between bilirubin values and carboxyhemoglobin levels on day three, suggesting that in the healthy term infant excessive hemolysis is not usually responsible for the variations observed in bilirubin levels.

Bilirubin↗
PubMedDate not supplied

[Relationship of the content of carboxyhemoglobin in the blood and of carbon monoxide in the expired air of test subjects to the CO concentration in the air of a hermetic chamber].

Four manned experiments (4 test subjects participating in each) were carried out in a chamber of 24 m3. The effect of CO at a concentration of 10 to 45 mg/m3 on the content of carboxyhemoglobin in the blood, nonhemoglobin iron in the plasma, CO in the breathing air, catalase and peroxidase activity was studied. A correlation was found between these parameters and CO concentration in the atmosphere and exposure time. It was demonstrated that a continuous exposure (up to 90 days) to CO at a concentration of 10 mg/m3 under favorable microclimatic conditions produced no significant effect on the above mentioned biochemical paramters.

Atmosphere Exposure Chambers↗
PubMed1976

Quaternary conformational changes in human hemoglobin studied by laser photolysis of carboxyhemoglobin.

These experiments indicate that absorbance changes observed at the 425 nm isosbestic point of the Hb and HbCO following laser photolysis of HbCO provide a direct measure of the rates of quaternary conformational changes between rapidly reacting Hb (the immediate product of full photolysis) and slowly reacting normal deoxyhemoglobin. Hb, first observed by Gibson (Gibson, Q.H. (1959) Biochem. J. 71, 293-303), Has been interpreted as deoxyhemoglobin remaining in the liganded quaternary conformation following rapid removal of ligand by a light pulse. In borate buffers between pH 8.4 and 9.6 particularly simple pH-independent results were obtained which allowed the use of a Monod. Wyman, and Changeux model (Monod, J., Wyman, J., and Changeux, J (1965) J. Mol. Biol. 12, 88-118) to fit the data. In this case Hb is taken to be R state deoxyhemoglobin. Partial photolysis experiments at 425 nm show that the rate of the R - T conformational change at 20 degrees decreases by about a factor of 2 for each additional bound ligand. The rate of the ligand-free conformational change is found to be 920 +/- 60s(-1), 6400 +/- 600s(-1), and 15,700 +/- 700(-1) respectively at 3 degrees, 20 degrees, and 30 degrees. The previously uninterpreted effects of flash length and partial photolysis on the CO recombination kinetics can be explained in terms of the present model. Kinetic results obtained below pH 8 are found to be inconsistent with a two-state model. It appears that binding of inositol hexaphosphate produces a new rapidly reacting quaternary conformation of HbCO.

Binding Sites↗
PubMed1979

[Hemoglobin oxygen combining capacity power. Reproducibility, variability; the effect of carboxyhemoglobin (author's transl)].

Hemoglobin oxygen combining power (HOCP) was measured in blood samples of 41 non smoking subjects and 36 smokers. The reproductibility and the varibility of this value were established (maximal variability was 2,5% in individual measurement). When the oxygen carrying capacity is reported to total hemoglobin (Hbt.), these two groups are not significantly different (1,344 +/- 0,004 ml O2 g-1 Hbt--n = 77-). However, when oxygen carrying capacity is reported to functional hemoglobin (Hbf = Hbt -- HbCO) there is a significative difference between smokers and non smokers (Student's t test 2 p less than 0,001) (1,404 +/- 0,005 ml O2 Hbf -- n = 77-).

Carboxyhemoglobin↗
PubMed1979

Dependence of the quantum efficiency for photolysis of carboxyhemoglobin on the degree of ligation.

A combined stopped flow-laser photolysis apparatus was used to measure the quantum efficiency for removal of carbon monoxide bound to human hemoglobin as a function of fractional CO saturation. This flow-flash technique allows the properties of partially liganded hemoglobin molecules, which are sparsely populated under equilibrium conditions, to be conveniently studied. Experiments performed at pH 7 and 20 degrees C both in the presence and absence of phosphates gave a similar dependence of quantum efficiency on fractional saturation. The observed quantum efficiency was 0.90 +/- 0.06 at 10% saturation and decreased to 0.47 +/- 0.02 as full saturation was approached. An allosteric model in which Hb(CO)1 has a quantum efficiency of 0.99 while other liganded species have quantum efficiencies of 0.47 was used to produce a good simulation of the results.

Carbon Monoxide↗
PubMed1979

Conformation-specific antibodies to the alpha chain COOH terminus of hemoglobin A0.

An anti-hemoglobin antiserum obtained from a sheep immunized with human carboxyhemoglobin A0 demonstrated little difference in its reactivity with deoxy- or carboxyhemoglobin A0. However, a subpopulation of this antiserum isolated by synthetic peptide affinity chromatography clearly distinguished between these two hemoglobin species. This subpopulation, designated alpha(129-141) anti-hemoglobin antibodies, represents less than 1% of the total anti-hemoglobin antibodies. They are nonprecipitating by Ouchterlony analysis, and fluorescence-quenching studies demonstrate the interaction of a single antibody binding site per hemoglobin dimer. These antibodies bind preferentially to carboxyhemoglobin with a median affinity constant of 5 X 10(8) M-1 compared to binding to deoxyhemoglobin with a binding affinity of less than 1 X 10(8) M-1. Furthermore, the presence of these antibodies in stoichiometric amounts increases the oxygen affinity of hemoglobin, and thus antibody and oxygen binding to hemoglobin can be considered as a linked function.

Antibodies↗
PubMed1975

Determination of the pK values for the alpha-amino groups of human hemoglobin.

The rate of reaction between alpha-amino groups and cyanic acid was followed at 26 degrees and ionic strength 0.2 M as a function of pH of human hemoglobin Ao solutions to determine the pK and the pH-independent second order rate constant, kappa, for these groups in the alpha and beta chains. At a given point in time, the extent of the reaction was determined by employing the Beckmann Sequencer as a quantitative tool in which the yields of leucine and histidine in the second Edman degradation cycle were used to define the rates of reaction of the alpha and beta chains, respectively. From these results, the individual were evaluated (Garner, M.H., Garner, W.H., and Gurd, F. R.N. (1973) J. Biol. Chem. 248, 5451-5455). Values for pK for the alpha and beta chains were, respectively, 6.74 and 6.93 for cyanoferrihemoglobin, 6.95 and 7.05 for carboxyhemoglobin, and 7.79 and 6.84 for deoxyhemoglobin. Values for kappa, M- minus 1 S-minus 1, for the alpha and beta chains were, respectively, 12.5 and 17 for cyanoferrihemoglobin, 12 and 18 for carboxyhemoglobin, and 91 and 24 for deoxyhemoglobin. Limits of significance were estimated for both variables in each case. The pK results for valine 1alpha agree well with the value obtained by Hill and Davis (1967) J. Biol. Chem. 242, 2005-2012) for carboxyhemoglobin and with that of Kilmartin and Rossi-Bernardi ((1971) Biochem. J. 124, 31-45) for deoxyhemoglobin. Values obtained for sperm whale myoglobin were 7.77 for pK and 7.4 for kappa. The results are useful for the interpretation of the allosteric interactions of hemoglobin with hydrogen ions, with CO2, and with phosphate.

Amines↗