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After reduction by dithiothreitol and removal of the reductant by molecular sieve chromatography, the four interchain disulfide bonds of the human IgGlk protein Fro reoxidize in the presence of oxygen and trace metal ions. The six molecular components of the reoxidation--L (light chain), H (heavy chain), HL, H2, H2L, H2L2--are quantitatively determined from polyacrylamide gels containing sodium dodecyl sulfate and the time-dependent sulfhydryl titer is measured with 5,5'-dithiobis-(2-nitrobenzoic acid). The rates of H2L2 covalent assembly depend on pH in an unexpected way: If the reduced protein is chromatographed at pH 3.2 and then adjusted to pH 7.5 (25 degrees, ionic strength equals 0.14), H2L2 formation proceeds rapidly, with half-times ranging between 20 and 40 min. In contrast, if chromatography is carried out at pH 5.5 before adjusting to the same final conditions, the half-times for H2L2 formation are considerably longer (120-180 min). The half-times in the former case approach the somewhat faster rates of H2L2 assembly observed in pulse-chase experiments with various types of mouse, IgG-producing cells [Baumal, et al. (1971) J. Exp. Med. 134, 1316-1334]. To facilitate comparison of experiments and models, we plot the concentrations of the six components against the corresponding number of sulfhydryl equivalents per mole of Fro. The respective plots for the pH 3.2 leads to 7.5 and 5.5 leads to 7.5 experiments are very similar despite the rate differences. Moreover, these plots differ significantly from the calculated plot for a hypothetical random reoxidation in which the intrinsic probability for formation of each correct HL and H2 disulfide bond is assumed equal and independent. It is concluded that the in vitro reoxidation of Fro (i) is other than random; (ii) involved a pathway of pathways with HL, H2, and H2L precursors; and (iii) involves at least some kinetic cooperativity in bond formation, since no model bases solely on independent bond formation adequately accounts for the results. The models were used also to examine the cellular assembly pathways of mouse IgG proteins.
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PMID:A kinetic study in vitro of the reoxidation of interchain disulfide bonds in a human immunoglobulin IgGLk. Correlation between sulfhydryl disappearance and intermediates in covalent assembly of H2L2. 23 27

Two unrelated Senegalese patients, both native of the Matam province, were found to have the same deficient G6PD variant. One has no hematological history, the other had several induced acute hemolytic episodes. The deficiency was almost complete in red blood cells and 20-30 percent of the normal level in leukocytes and platelets; in leukocytes the deficiency was due to a decrease in the molecular specific activity of the enzyme to which a molecular instability was added, explaining the greater deficiency in red blood cells. The electrophoretic mobility was slightly fast in leukocytes and platelets but normal in red blood cells. This pattern was confirmed by electrofocusing in ampholine-acrylamide gel. From a kinetic point of view, these enzymes were characterized by a lowered Km (G6P) (13 to 20 muM) a normal Km (NADP+), a Ki (NADPH) increased about twice, a thermal instability, a biphasic pH curve and an increased activation energy (15 kcal/mole). The polymorphonuclear cells were functionally strictly normal: engulfment, nitroblue tetrazolium (NBT) reduction test, induced iodination, and oxygen consumption were normal. The authors discuss the importance of post-synthetic modifications of the muted enzymes and their repercussions on the enzyme characteristics.
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PMID:Gd(minus)Matam, an African glucose-6-phosphate dehydrogenase variant with enzyme deficiency. Biochemical and immunological properties in various hemopoietic tissues. 23 89

In contrast to amphibians belonging to the orders Urodela and Anura, virtually no data exist on the respiratory physiology of the more primitive Apoda. This study concerns oxygen uptake and hemoglobin function in the caecilan Boulengerula taitanus, an apodan with fossorial habits. The oxygen uptake rate resembles that of other amphibians of similar size. The blood was high O2 capacity (14 vol%) and the erythrocytes are smaller, and the red cell count is greater than in other amphibians. The oxygen affinity of whole blood is high compared to other amphibians (P50 = 28 mm Hg at 25 degrees C and pH 7.6). The oxygen equilibrium curve is sigmoid (n = 1.79) and the Bohr factor is small (deltalog P50/deltapH = - 0.21). In 'stripped' hemoglobin solutions oxygen affinity increases strongly (P50 = 3.3 mm Hg at 25 degrees C and pH 7.6) and the temperature sensitivity is high (apparent deltaH=-19.4 kcal/mole), but the ATP and pH influences are too low to account for the difference in P50 compared to whole blood. The high oxygen capacity and oxygen affinity and the low Bohr factor may have adaptive significance to this fossorial amphibian.
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PMID:Oxygen uptake and blood respiratory properties of the caecilian Boulengerula taitanus. 24 53

Physical quantities and equations are used to define the laws of natural and engineering sciences. Clarity has been brought in equal measure into the the theory of physical quantities and the SI-system of units due to the basic work of Wallot and that of national and international institutions. For practical use in this paper, the most important rules and definitions for the formulation of physical equations are treated in an elementary form and the ease of their use is demonstrated in the following examples: speed of a car, capacitance of a plate capacitor, thermal emission of the cathode of an x-ray tube, oxygen uptake in cardiology, mole concentration and mass concentration of a substance in a solution. In addition, some important quantities and units of cardiology were summarized in a table.
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PMID:Notation of physical equations no longer a problem. 26 80

The pathway of anaerobic reduction of nitrite to nitrogen gas (N2) by cell suspensions of the denitrifier, Pseudomonas aeruginosa, was studied using the techniques of gas chromatography and mass spectrometry. While release of nitrous oxide (N2O) is not normally detected during the reduction of nitrite to N2 by this organism, 15N from [15N]nitrite nevertheless can be trapped quantitatively as 15N2O in a pool of added N2O. In such experiments the abundance of 15N in N2O always exceeds that in product N2, consistent with the absence of a major reductive route from nitrite to N2 which by-passes N2O. During the reduction of a mixture of [15N]nitrite and nitric oxide (NO), 15NO produced at most only in trace amounts. The final products are chiefly 15N2 and 14N2 with only a small fraction of the scrambled product, 14N15N. Much of the 14N15N can be accounted for as an artifact caused by traces of molecular oxygen, which promote the conversion of NO to nitrite by autooxidation and thereby degrade slightly the isotopic purity of [15N]nitrite. Nitrous oxide shows all the properties of a free obligatory intermediate during the denitrification of nitrite to N2 by P. aeruginosa, whereas NO does not. The inability to trap 15NO in a pool of NO indicates that NO is not a free obligatory intermediate in the reduction of nitrite. The small mole fractions of 14N15N produced from a mixture of [15N]nitrite and NO require that the main reductive pathways for these nitrogen oxides cannot share any freely diffusible mono-nitrogen intermediate in common. The simplest interpretation is that nitrite and NO are denitrified by separate pathways, at least prior to the formation of the first bi-nitrogen compound.
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PMID:Nitrogen 15 tracer studies on the pathway of denitrification in Pseudomonas aeruginosa. 40 9

Measurements of electrical current and oxygen consumption were carried out concurrently under voltage clamp conditions in 11 toad hemibladders. Inhibition of active transport with amiloride then permitted evaluation of the passive conductance and the rate of basal oxygen consumption Jbr, allowing the simultaneous determination of the rates of active sodium transport JaNa and suprabasal oxygen consumption Jsbr-JaNa and Jabr were linear functions of the electrical potential difference over a range of +/- 80 mV. This allowed the comprehensive application of a linear nonequilibrium thermodynamic formalism, leading to the evaluation of the affinity A (negative free energy) of the metabolic reaction driving transport, all phenomenological coefficients, and the degree of coupling q relating transport to metabolism. Values of A determined by two techniques were A1=56.0 +/- 5.8 and A2=58.2 +/- 6.5 kcal per mole. Values of q determined by two techniques agreed well and were less than 1, indicating incompleteness of coupling, and hence lack of fixed stoichiometry between Na transort and O2 consumption. The affinity and the electromotive force of sodium transport ENa are not closely correlated, reflecting the fact that ENa comprises both kinetic and energetic factors.
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PMID:Thermodynamic analysis of active sodium transport and oxidative metabolism in toad urinary bladder. 40 77

1. The oxygen consumption and the movements of labelled phosphate were measured in garfish olfactory nerve at rest and during activity.2. In solutions with 2.5 mM-K and 0.2 mM-phosphate the resting oxygen consumption was 0.206 m-mole/kg.min; activity at 2 sec(-1) produced an extra oxygen consumption of 2.46 mumole/kg.impulse. The extra oxygen consumption declined exponentially with a time constant of 2.62 min at 22-26 degrees C.3. The phosphate efflux, measured simultaneously, had a resting efflux rate constant of 1.24 x 10(-3) min(-1); activity at 2 sec(-1) produced an extra fractional loss of 9.38 x 10(-6) impulse(-1). The increase in phosphate efflux followed almost the same time course as the increase in oxygen consumption.4. Increasing the frequency of stimulation from 2 sec(-1) to 3 or 5 sec(-1) decreased both the extra oxygen consumption and the extra fractional loss of phosphate. When the frequency was decreased to 0.5 or 1 sec(-1) the extra oxygen consumption per impulse increased, while the extra phosphate liberation was lowered.5. Changing the phosphate concentration did not much affect the extra oxygen consumption; on the other hand, lowering or increasing the phosphate from the standard 0.2 mM decreased both the resting and the stimulated phosphate efflux.6. Lowering the K from the standard 2.5 mM did not affect the extra oxygen consumption, but increased both the resting and the extra loss of phosphate. At higher K concentrations the extra oxygen consumption and the extra fractional loss of phosphate decreased without much change in the resting phosphate efflux.7. Application of 1-20 muM-strophanthidin produced a transient decrease in the resting phosphate efflux without much change in resting oxygen consumption. With 10 or 20 muM-strophanthidin the extra fractional loss of phosphate and the extra oxygen consumption were both lowered in approximately the same proportions.8. The findings are consistent with the hypothesis that the increase in intracellular inorganic phosphate that results from increased break-down of ATP after activity, is the main cause for the increased phosphate efflux. A fraction of the increase in intracellular phosphate only appears to be liberated to the outside, the value of the fraction depending on the resting phosphate efflux before activity.9. The initial increase in intracellular inorganic phosphate after an impulse, estimated from the oxygen consumption or the phosphate fluxes, appears to be about 12-19 mumole/kg nerve, remarkably close to the value known from chemical analysis.
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PMID:Phosphate efflux and oxygen consumption in small non-myelinated nerve fibres at rest and during activity. 43 Apr 13

Using the technique of affinity chromatography on a myo-inositol-substituted Sepharose, the myo-inositol oxygenase from rat kidneys was purified to homogeneity. The active enzyme contains iron, most probably in its divalent form. Electrophoresis on polyacrylamide gel containing sodium dodecylsulphate causes the cleavage of the enzyme protein into apparently identical subunits with a molecular weight of approximately 17,000. The smallest active unit consists of 4 subunits, and is in a pH-dependent equilibium with species consisting of 8, 12, and 16 subunits, respectively, which all show the same specific enzyme activity. In the presence of oxygen the enzyme is highly unstable; at the early stages of inactivation it can be reactivated by reducing agents like NaBH4. Under anaerobic conditions or under the influence of Fe2-chelating agents, the enzyme is also inactivated; this inactivation is caused by the loss of iron and concomitant cleavage into the subunits. It can be reversed by incubation with FeSO4 in the presence of air. If myo-inositol and FeSO4 are present, the reactivation involves an oligomerization to the species with 16 subunits with the uptake of 8 gram-atoms of iron per mole of this species. The enzyme reaction follows Michaelis-Menten kinetics; the Michaelis constants are 4.5 x 10(-2)M for myo-inositol and 9.5 x 10(-6)M for oxygen.
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PMID:myo-Inositol oxygenase from rat kidneys. I: Purification by affinity chromatography; physical and catalytic properties. 43

Myoglobin (Mb) was isolated from canine skeletal muscle by a novel heat denaturation-gel filtration-ion exchange chromatography procedure. The purified major Mb was homogeneous by gel electrophoretic and ultracentrifugal analysis, and the sedimentation coefficient at infinite dilution (S degrees 20, w) was 1.9 S. The molecular weight by sedimentation equilibrium was 1.72 X 10(4) and was essentially identical with the values by the iron analysis (1.80 X 10(4) and the amino acid composition (1.78 X 10(4). The spectroscopic properties of deoxy-, oxy-, carbonmonoxy- and met-derivatives of the Mb were determined in ultraviolet, Soret and visible regions. The pK' of acid-alkaline transition of the met-Mb was estimated as 8.80+/-0.04 (25 degrees) from the pH-dependent spectral change. The oxygen equilibrium studies revealed complete absence of such allosteric properties as heme-heme interaction, anion effect and the Bohr effect which were always present in normal mammalian hemoglobins. Oxygen tension for the half-oxygenation was 0.48 mmHg (20 degrees) and its temperature-dependent change gave the delta H degrees of -15.7 Kcal/mole.
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PMID:[A study on the physiological basis of training effect--with special reference to myoglobin. I. Isolation and properties of myoglobin from dog skeletal muscle (author's transl)]. 54 71

A reduction in myocardial oxygen supply during ischemia, not only leads to reduced aerobic ATP production but does not stimulate glycolytic ATP synthesis. The residual aerobically synthesized ATP comes primarily from continued inefficient (i.e., compared to glucose in terms of moles of ATP produced per mole of O2 consumed) oxidation of fatty acids. This leads to elevated tissue levels of long chain fatty acyl-CoA and fatty acyl-carnitine. Both are potentially cell damaging metabolic intermediates. Restriction of glycolysis is due to inhibition of glyceraldehyde-3-phosphate dehydrogenase by accumulated metabolites, such as H+, lactate and NADH. The reduced production of ATP leads to decreased levels of high energy phosphate stores which in turn may impair myocardial mechanical function.
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PMID:Energy metabolism in the ischemic heart. 55 21


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