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Biomedical subjects

B Cartwright

Publications and source records attributed to B Cartwright.

At least 19 recordsLinked to original sources
PubMed1999

Ethical dilemmas related to counseling clients living with HIV/AIDS.

This study tested an eight-factor model of client actions/decisions in terms of the extent to which professionals counseling persons with HIV/AIDS believed that those actions/decisions presented ethical dilemmas, and the frequency with which they encountered such actions. A confirmatory factor analysis lent initial support for the hypothetical eight-factor ethical-dilemma model for the ratings regarding the extent to which the participants believed those items constituted ethical dilemmas. Similar results were obtained for the frequency ratings, but in this case a second, competing model was equally plausible. Several significant predictors of participant ratings were found and are discussed.

Confidentiality↗
PubMed1983

Comparison of human versus porcine insulin in treatment of diabetes in children.

The blood glucose control obtained when using semi-synthetic monocomponent human insulin (insulin A) was compared with that using standard monocomponent porcine insulin (insulin B) in 14 children in a double blind crossover study. At the start of the study age, duration of diabetes, insulin dose, and daily carbohydrate intake were the same in both groups. After a one month run in period of standard treatment with porcine insulin the children were randomly divided into group 1 (three months of insulin A followed by three months of insulin B) and group 2 (three months of insulin B followed by three months of insulin A). During each treatment period blood glucose control was assessed by clinical symptoms, glycosylated haemoglobin, and home blood glucose monitoring. Although a significant difference in the period after lunch during 24 hour blood glucose profiles suggested a shorter onset time and faster peak action time of human insulin, no significant difference in the overall diabetic control was seen between the two types of insulin. There was a trend towards improved blood glucose control (irrespective of insulin) as the trial progressed. No clinical reactions to human insulin occurred, and there was no significant difference in the daily insulin dose between porcine and human insulin.

Adolescent↗
PubMed1982

Nature of the antibody response to the foot-and-mouth disease virus particle, its 12S protein subunit and the isolated immunizing polypeptide VP1.

Inoculation of inactivated 146S foot-and-mouth disease virus particles into guinea-pigs elicited the formation of neutralizing antibody and the serum had a 10-fold higher titre in radioimmunoassay (RIA) with 146S particles than with the 12S virus subunit. In contrast, a single inoculation of the 12S subunit or the isolated polypeptide VP1 elicited the formation of antibody having a much lower titre in RIA with the 146S particle than with the 12S subunit and low or undetectable neutralizing activity. However, sera from guinea-pigs given two or more inoculations of the 12S subunit or VP1 had neutralizing activity. The level in the anti-VP1 serum was lower than that in the anti-12S serum and both were much lower than that in animals receiving two inoculations of the 146S particle. The neutralizing activity elicited by the three antigens was absorbed by the homologous antigen. In contrast, neither the 12S subunit nor VP1 absorbed the anti-146S neutralizing antibody and VP1 did not absorb the anti-12S subunit neutralizing antibody. However, the 12S subunit partly absorbed the neutralizing activity elicited by VP1. The results are compatible with a model in which the 146S particle elicits a spectrum of neutralizing antibodies which are completely absorbed by the homologous particle but only partially by the 12S subunit or VP1. The results are discussed in relation to the structural features required for the production of neutralizing antibody.

Animals↗
PubMed1982

Stimulation by heterotypic antigens of foot-and-mouth disease virus antibodies in vaccinated cattle.

Immunisation of cattle with foot-and-mouth disease virus failed to raise a level of antibody that provides protection against heterotypic challenge. Further the 12S substructure, produced from the 146S particle, was ineffective in providing protection against challenge by homotypic virus. These findings suggest considerable antigenic differences in the virus serotypes and between the virus and its substructure. Inoculation of homologous 12S and heterologous 1246S and 12S antigens into vaccinated cattle, however, revealed antigenic relationship between different serotypes, and between serotypes and their substructures.

Animals↗
PubMed1980

Serological and immunological relations between the 146S and 12S particles of foot-and-mouth disease virus.

Intact 146S particles of the seven serotypes of foot-and-mouth disease virus (FMDV) produce type-specific precipitating, complement-fixing and neutralizing antibodies in cattle and guinea-pigs. However, the 12S structural subunit, produced from the virus particle by mild acid treatment (pH 6) or by heating at 56 degrees C, although stimulating the production of precipitating and complement-fixing antibodies, produces only low levels of neutralizing antibody. Nevertheless, 12S antibody in guinea-pigs primed with a vaccine prepared from 146S particles. Moreover, heterotypic 12S and 146S particles also boosted the neutralizing antibody response to the first virus. These results point to an antigenic similarity between the 146S particles of each type and to a close antigenic relationship between the 146S and 12S particles.

Animals↗
PubMed1979

Purification and identification of the RNA-dependent RNA polymerase of foot-and-mouth disease virus.

The RNA-dependent RNA polymerase induced in BHK 21 cells by infection with foot-and-mouth disease virus has been isolated from the replication complex. It contains a major, virus-coded protein with mol. wt. 56 000 which appears from serological studies and tryptic peptide mapping to be the same as the virus infection associated (VIA) antigen and the protein P56 found in cells infected with the virus. Other virus coded proteins and a host cell protein were present in the partially purified replication complex but were removed by digestion with ribonuclease T1, leaving only the major virus coded protein. The tryptic peptide maps of the VIA antigen of the seven serotypes of the virus were similar, suggesting a high level of conservation in that region of the genome coding for the RNA polymerase of each type.

Animals↗
PubMed1977

Effect of concanavalin A on vesicular stomatitis virus maturation.

Addition of concanavalin A to BHK cell monolayers infected with vesicular stomatitis virus prevented the formation of mature virus particles. In these cells the virus glycoprotein (G) was inserted into the plasma membrane and the protein that is in close association with the ribonucleic acid, protein N, was found in the cytoplasm. At times when cells infected in the absence of the lectin were liberating virus into the supernatant medium, the M or matrix protein was found in association with the plasma membrane of the lectin-treated cells. The removal of the lectin from the cells with alpha-methyl-D-glucoside 3 h after infection was followed by the immediate release of mature virus particles. The rate of virus release from these cells was the same as that from cells infected in the absence of the lectin. Addition of cycloheximide, and inhibitor of protein synthesis, immediately after alpha-methyl-D-glucoside treatment of the cells did not alter the rate of virus production, suggesting that the proteins required for virus synthesis were available in the lectin-treated cells and that virus assembly took place without further protein synthesis on removal of the lectin.

Cell Line↗
PubMed1977

Role of sialic acid in infection with vesicular stomatitis virus.

The role of sialic acid in the infection of tissue culture cells and mice with vesicular stomatitis virus has been studied. No loss of infectivity of the Indiana serotype of the virus was detected by incubating with neuraminidase although the virus particles had lost sialic acid as judged by their ability to inhibit the agglutination of red blood cells by influenza virus. The results did not depend on the type of cell used for growth and assay of the virus since essentially similar findings were made in BHK cells, L cells or mice. Similar results were obtained with Brazil virus, a subtype of the Indiana serotype and with the New Jersey serotype. We consider that the sialic acid of the virus which is removed by neuraminidase does not play a major role in the infectivity of the virus.

Aedes↗
PubMed1972

Model for vesicular stomatitis virus.

Vesicular stomatitis virus contains single-stranded ribonucleic acid of molecular weight 3.6 x 10(6) and three major proteins with molecular weights of 75 x 10(3), 57 x 10(3), and 32.5 x 10(3). The proteins have been shown to be subunits of the surface projections, ribonucleoprotein, and matrix protein, respectively. From these values and from estimates of the proportions of the individual proteins, it has been calculated that the virus has approximately 500 surface projections, 1,100 protein units on the ribonucleoprotein strand, and 1,600 matrix protein units. Possible models of the virus are proposed in which the proteins are interrelated.

Amino Acids↗