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Biomedical subjects

M L Pearson

Publications and source records attributed to M L Pearson.

11 recordsLinked to original sources
PubMed1992

Differences in quality of care for hospitalized elderly men and women.

OBJECTIVE: To analyze whether important gender differences exist in the quality of hospital care provided to patients with four major medical conditions. DESIGN: Bivariate and multivariate comparisons of clinically detailed sickness at admission, quality, utilization, and outcome measures. SETTING: Acute care hospitals located in five states. PATIENTS OR OTHER PARTICIPANTS: A total of 11,242 patients 65 years or older who were hospitalized with one of four diseases: congestive heart failure, acute myocardial infarction, pneumonia, and cerebrovascular accident. We derived our data from the nationally representative sample used to study the quality of hospital care for Medicare patients before and after the implementation of the prospective payment system. A hierarchical (nested) cluster sampling design was used to draw disease-specific samples of patients hospitalized in 1981, 1982, 1985, or 1986 in one of 297 hospitals located in 30 areas within five states. INTERVENTIONS: This was an observational study. MAIN OUTCOME MEASURES: Sickness at admission, process, use rates, length of stay, discharge status, discharge destination, and mortality. RESULTS: Sex differences in sickness at admission varied by disease. There was some evidence that women received worse process of care, but the difference was very small. We found many similarities in the process and outcomes of care for male and female patients. CONCLUSIONS: After controlling for sickness at admission, age, and other important covariates, the in-hospital experiences of elderly men and women showed greater similarities than differences. The concern that sex bias enters into clinical decision making during hospitalization is eased, although not entirely eliminated.

Aged↗
PubMed1992

Nosocomial transmission of multidrug-resistant Mycobacterium tuberculosis. A risk to patients and health care workers.

OBJECTIVE: To determine the factors associated with the development of multidrug-resistant tuberculosis among patients at a New York City Hospital and to investigate possible nosocomial transmission. DESIGN: A retrospective case-control study and tuberculin skin test survey. PATIENTS: Twenty-three patients with tuberculosis whose isolates were resistant to at least isoniazid and rifampin (case patients) were compared with patients with tuberculosis whose isolates were susceptible to all agents tested (controls). Tuberculin skin test conversion rates were compared among health care workers assigned to wards where patients with tuberculosis were frequently or rarely admitted. SETTING: A large, teaching hospital in New York City. MEASUREMENTS: Mycobacterium tuberculosis isolates from case patients and controls were typed by restriction fragment length polymorphism analysis. RESULTS: Case patients were younger (median age, 34 compared with 42 years; P = 0.006), more likely to be seropositive for HIV (21 of 23 compared with 11 of 23 patients; odds ratio, 11.5; 95% CI, 1.9 to 117), and more likely to have had a previous hospital admission within 7 months before the onset of tuberculosis (19 of 23 compared with 5 of 23 patients; odds ratio, 17.1; CI, 3.3 to 97), particularly on one ward (12 of 23 compared with 0 of 23 patients; odds ratio, undefined; P = 0.002). Health care workers assigned to wards housing case patients were more likely to have tuberculin skin test conversions than were health care workers assigned to other wards (11 of 32 compared with 1 of 47 health care workers; P less than 0.001). Few (6 of 23) case patients were placed in acid-fast bacilli isolation, and no rooms tested had negative pressure. Of 16 available multidrug-resistant isolates obtained from case patients, 14 had identical banding patterns by restriction fragment length polymorphism analysis. In contrast, M. tuberculosis isolates from controls with drug-susceptible tuberculosis had patterns distinct from each other and from those of case patients. CONCLUSIONS: These data suggest nosocomial transmission of multidrug-resistant tuberculosis occurred from patient to patient and from patient to health care worker and underscore the need for effective acid-fast bacilli isolation facilities and adherence to published infection control guidelines in health care institutions.

Adult↗
PubMed1978

Identification of the N gene protein of bacteriophage lambda.

The N gene protein, pN, of bacteriophage lambda stimulates early gene transcription by allowing mRNA chain elongation to proceed into genes distal to transcription termination sites normally recognized by the Escherichia coli transcription termination protein rho. pN has previously eluded detection on sodium dodecyl sulfate/polyacrylamide gels because of its small size, its instability, and the difficulty of distinguishing pN itself both from host proteins and from other early lambda proteins whose synthesis depends on pN action. These problems have now been overcome and we find that the major form of pN present in crude cell extracts of infected cells has an apparent molecular weight of 13,500. lambdabio256, a deletion-substitution mutant terminating in N, codes for a shorter pN of molecular weight 12,500. A nonsense fragment of 10,500 molecular weight coded by lambdaN(am7) has also been identified. These conclusions are based on examination of the electrophoretic profiles of the proteins synthesized after infection of UV-irradiated E. coli by various lambdaN(-) temperature-sensitive, nonsense, and deletion-substitution mutants. It has also been possible to distinguish pN itself from other early lambda polypeptides by infecting ron(-) cells with either lambdaN(mar) phage allowing pN synthesis but not pN action or lambdaN(am) phage defective in pN synthesis and pN action. Our results together with previous data are discussed with respect to the possible existence of multiple molecular weight forms of pN and the location of the coding sequences in the N gene region.

Coliphages↗
PubMed1978

Mass fragmentographic determination of pentachlorophenol in rainbow trout.

Pentachlorophenol (PCP) is extracted from selected tissues of rainbow trout and converted to pentachloroanisole (PCA) by means of alkylation in the presence of potassium carbonate as a condensing agent. Pentachlorophenetole (PPT) is used as an internal standard. The electron impact mass fragmentography is carried out by monitoring m/e 280 (PCA), 294 (PPT), and 237. A plot of peak height vs. concentration is linear from 0.03 to 4.0 ng. Accuracy and precision of the method is +/-2% (N - 36). The results are accurate enough to warrant the use of this method for determining PCP in fish, as well as for monitoring PCP from various environmental sources. In addition, this technique provides a simple and rapid method by which a mixture of PCA and PCP can be determined simultaneously.

Animals↗
PubMed1975

Isolation and characterization of an alpha-amanitin-resistant rat myoblast mutant cell line possessing alpha-amanitin-resistant RNA polymerase II.

Cultures of the rat skeletal muscle myoblast cell line, L6, were treated with the mutagen ethylmethanesulfonate and grown in the presence of alpha-amanitin, an inhibitor of RNA polymerase II in vitro. One clonal cell line, Ama102, resistant tc the cytotoxic action of 2 mu-g/ml of alpha-amanitin was isolated and extensively characterized. Ama102 cells were about 30-fold more resistant to alpha-amanitin than their Ama+ parent cells based on a comparison of the concentration of alpha-amanitin required to reduce their plating efficiencies to similar extents. The RNA polymerase activities from Ama+ and Ama102 cells were solubilized and separated by DEAE-Sephadex chromatography. Whereas all of the Ama+ RNA polymerase II activity was inhibited by 0.1 mu-g/ml of alpha-amanitin, about 30% of the activity in the Ama102 RNA polymerase II peak was resistant to this concentration of alpha-amanitin and was inhibited only by much higher concentrations (25 mu-g/ml) of alpha-amanitin. This alpha-amanitin-resistant activity in Ama102 cells was identified as a bona fide RNA polymerase II by its chromatographic behavior on DEAE-Sephadex, salt optimum, preference for denatured DNA as template, insensitivity to inhibition by potassium phosphate, thermal inactivation kinetics, and inactivation by anti-RNA polymerase II antiserum. Both RNA polymerase IIa and IIb from Ama102 cells exhibited the partial alpha-amanitin resistance, as did this activity when purified further on phosphocellusose. Unlike the parental Ama+ cells, Ama102 cells neither fused at confluence nor showed an increase in the specific activity of creatine kinase. The altered sensitivity of the Ama102 RNA polymerase II to alpha-amanitin appears to account for the drug-resistant phenotype of these cells.

Amanitins↗
PubMed1975

Repression and autogenous stimulation in vitro by bacteriophage lambda repressor.

Purified lambda repressor protein is shown to reduce the lambda DNA-directed synthesis of proteins in vitro as determined both by net amino-acid incorporation and by analysis of specific lambda-coded proteins resolved by sodium dodecyl sulfate/polyacrylamide slab gel electrophoresis. By means of different lambda DNA templates carrying deletion and point mutations in the operators o-L or o-R, it has been possible to demonstrate repression of the synthesis of two classes of lambda proteins. The synthesis of one, class c, appears to be controlled from the operator o-L and is more efficiently repressed at low concentrations of the repressor than that of the other class of repressible lambda proteins, class d, which is controlled from the operator o-R. Several other proteins synthesized in vitro are not repressible. Some of these are coded by the J-att region. In addition, the repressor appears to have another activity, that of stimulating the synthesis of a protein identified as the repressor itself. Lambda repressor appears to stimulate its own synthesis by acting at prm, a site defined by the cis-acting mutation prm 116.

Chromosome Mapping↗