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Biomedical subjects

C E Castro

Publications and source records attributed to C E Castro.

15 recordsLinked to original sources
PubMed1991

Primary health services in Ecuador: comparative costs, quality, and equity of care in Ministry of Health and rural social security facilities.

This study of costs, quality and financial equity of primary health services in Ecuador, based on 1985 data, examines three assumptions, common in international health, concerning Ministry of Health (MOH) and Social Security (SS) programs. The assumptions are that MOH services are less costly than SS services, that they are of lower quality than SS services, and that MOH programs are more equitable in terms of the distribution of funds available for PHC among different population groups. Full costs of a range of primary health services were estimated by standard accounting techniques for 15 typical health care establishments, 8 operated by the MOH and 7 by the rural SS program (RSSP), serving rural and peri-urban populations in the two major geographical regions of Ecuador. Consistent with the conventional premise, MOH average costs were much lower than RSSP costs for several important types of services, especially those provided by physicians. Little difference was found for dental care. The lower MOH physician service costs appeared to be attributable primarily to lower personnel compensation (only partially offset by lesser productivity) and to greater economies of scope. Several measures of the quality of care were applied, with varying results. Based on staff differences and patterns of expenditures on resource inputs, notably drugs, RSSP quality appeared higher, as assumed. However, contrary to expectation, a questionnaire assessment of staff knowledge and procedures favored the MOH for quality. Program equity was judged in terms of per capita budgeted expenditures (additional measures, such as the likelihood of receiving necessary care, would have required household survey data beyond the scope of this program-based study). The results support the assumption of greater MOH financial equity, as its program reveals less variation in budgeted expenditures between different population groups covered. Additional evidence of equity, using other indicators, would be helpful in future research. The paper's findings have policy implications not only for Ecuador's health sector but also for policy-makers in other countries at similar levels of socioeconomic development. These implications are spelled out in order to guide officials wrestling with issues of efficiency, quality, and equity as they search for the best use of scarce resources to promote health.

Costs and Cost Analysis↗
PubMed1991

[Primary health care in Ecuador: services provided by the Ministry of Health and Rural Social security Services].

The present study will examine three common premises in the field of international public health: that the primary care services offered by agencies of the Ministries of Health (MH) are less costly than those offered by Social Security institutions, that the former services are inferior to the latter, and that funds are distributed more equitably by the MH centers among their various recipient populations. The 1986 study compared the costs, quality, and equity of the services in 15 primary care centers in Ecuador--eight Ministry of Health centers and seven rural Social Security (RSS) centers--examining budgetary data from 1985 and obtaining information through a questionnaire and interviews with the personnel at those centers. Average costs were calculated by standardized accounting techniques, and it was confirmed that for several important services, especially medical consultations, these costs were much lower in the Ministry centers than in the Social Security centers. However, no differences in the cost of dental care were detected. The evaluation of quality, based on an analysis of the production structure and process, did not yield uniform results. On the one hand, the distribution of personnel and the allocation of funds for drugs and other supplies indicated that the RSS agencies provided better quality services. On the other hand, a questionnaire revealed that the MH health workers' knowledge of various principles of primary care was superior to that of the RSS workers. Upon comparing the per capita budget of the two types of entities, it was confirmed that the Ministry of Health had more equitable per capita coverage than rural Social Security. The implications of these findings for Ecuador and other developing countries are discussed and several recommendations made.

Costs and Cost Analysis↗
PubMed1978

Oxidation of heme proteins by alkyl halides: a probe for axial inner sphere redox capacity in solution and in whole cells.

Iron(II) porphyrins in homogeneous solution, in heme proteins, and in intact human erythrocytes and lysed cells are oxidized by certain alkyl halides to the corresponding iron(III) complexes at room temperature. The mechanism established for the oxidation of hemes in homogeneous solution operates at all levels of biological integrity. It is an axial inner sphere process. Deoxyhemoglobin has about the same reactivity within and without cells. The speed of the reaction with the proteins is primarily governed by the steric accessibility to iron. The reactivity of an array of iron(II) proteins accords well with theoretical prediction. In contrast the reactivity of cytochrome b5 does not. An examination of the oxidation and reduction of this protein was additional mechanistically defined reagents (trinitrobenzene and hydroquinone) shows it to be in the G rather than C conformation. The unusual redox characteristics of this protein can be rationalized on this basis.

Animals↗
PubMed1978

Oxidation of low-spin iron(II) porphyrins by molecular oxygen. An outer sphere mechanism.

Hexacoordinate low-spin iron(II) porphyrins are oxidized by molecular oxygen in amine solvents at room temperature by a process that is acid dependent. The visible and NMR spectra of solutions of the iron complexes and the influence of axial ligands upon the rate of oxidation are consistent with an outer sphere mechanism that entails the dissociation of a protonated 1:1 iron porphyrin-oxygen pi complex as the rate-limiting step.

Chemical Phenomena↗
PubMed1978

Conversion of oxyhemoglobin to methemoglobin by organic and inorganic reductants.

Human oxyhemoglobin is converted to methemoglobin by a wide array of organic and inorganic reductants. Depending upon the concentration and nature of the reductant, varying amounts of deoxyhemoglobin are produced. The general overall sequence is: FeO2 leads to (1) FeIII leads to (2) FeII. The intermediacy of methemoglobin can be demonstrated by direct spectral observation and by cyanide trapping. For organic reductants, the second-order rate constants for (1) vary from greater than 300 (phenylhydroxylamine) to 1.4 X 10(-4) M-1 s-1 (malononitrile). Generally the rates parallel the ease of hydrogen abstraction by iron-bound oxygen from the substrate, and simply hydrocarbons are reactive. Rates for these processes have been ascertained with recrystallized protein, lysed cells, and intact human erythrocytes. At room temperature oxyhemoglobin quantitatively converts benzaldehyde to benzoic acid and hydroquinone to benzoquinone. Rates for inorganic species (process 1) range from greater than 7 X 10(3) (chromous ion) to 0.015 M-1 s-1 (ferrocyanide). Ferrous ion rapidly deoxygenates oxyhemoglobin by direct attack on the oxy complex but methemoglobin is not an intermediate with this reagent. Taken together the results support the theoretical prediction that reductants should oxidize oxyhemoglobin, and they demonstrate at least some degree of radical character to the oxy complex.

Anions↗
PubMed1977

Biodehalogenation.

Haloorganic biocides are widely employed as soil fumigants to combat the destructive action of plant parasitic nematodes and fungi. These substances are dehalogenated by soil organisms, principally species of Pseudomonas and Flavobacteria, to nontoxic metabolities. The paths of metabolism of a vareity of simply alkyl halides are described with emphasis upon the biodehalogenation step.

1-Propanol↗
PubMed1975

Conformational isomerism and effective redox geometry in the oxidation of heme proteins by alkyl halides, cytochrome c, and cytochrome oxidase.

In contrast to its lethargy at physiological pH, horse heart cytochrome c can be oxidized at room temperature by the axial inner sphere oxidant bromomalononitrile (BMN) at higher acidities. The following stoichiometry obtains: 2Fe11 c + BrCH(CN2) + H+ leads to 2FeIII c + CH2(CN)2 + Br-, and the rate law is given by: rate = k2(FeIIc)(BMN). At an ionic strength of 1.0 (KCl), second-order rate constants vary from 300 l. per mol per sec (pH 2-3) to 0(pH 9). Below pH 6 there is a noticeable increase in rate with ionic strength while there is no specific salt effect for the process. At pH 7.4 there is no influence of added salt (0.01-1.0 M) upon the slow rate of reaction. The vast changes in rate occur over a pH region (3-6) in which only very minor changes in the visible spectrum of the cytochrome are manifest. The results are interpreted in terms of a conformational isomerism of cytochrome c in which the effective redox geometry alters from a predominantly "short C" form (in which an axial position is available for substitution) at lower pH's to a predominantly "C" form (axial positions encumbered) in the physiological region. At 5 degrees, pH 7.4, both hemes of beef heart cytochrome oxidase are oxidized by the addition of BMN (k2 = 29 plus or minus 3 l. per mol per sec). However, the reaction is inhibited by potassium cyanide and the protein containing iron(II) cyt alpha along with the cyano adduct of iron(II) or iron(III) cyt alpha3 is inert. The results demonstrate cytochrome alpha3 as the site of reaction and that alpha reduces alpha3 in the process. Cytochrome oxidase does catalyze the oxidation of cytochrome c with BMN as substrate. Taken together the results provide additional support for a recent theory and they demonstrate BMN to be an efficient probe for the effective redox geometry of a hemoprotein in solution.

Animals↗