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Biomedical subjects

R Pink

Publications and source records attributed to R Pink.

9 recordsLinked to original sources
PubMed1995

A comparison of tissue reactions to Ketac-Fil and amalgam.

The objective of this study was to compare the bone tissue reactions of Ketac-Fil to the most commonly used retrograde filling material, amalgam, in a rat model. Forty-eight Harlan rats were divided into three groups: amalgam, Ketac-Fil, and controls. Following anesthesia, the right lower incisor was extracted from each animal. A 3-mm long x 1-mm diameter polyethylene tube filled with amalgam or Ketac-Fil was implanted in the extraction site. The animals were killed at 14, 42, and 90 days; and the mandibles were dissected en block and processed histologically. The inflammatory reaction was assessed by the number of plasma cells, lymphocytes, polymorphonuclear neutrophils, giant cells, and osteoclasts within 100 microns of the implant. Bone formation was determined as either present or absent in the same area. There was no statistically significant bone apposition within 100 microns of the Ketac material, and there was a statistically significant increase in inflammation in the amalgam group. This study indicates that both Ketac-Fil and amalgam are relatively biocompatible, and provides support for clinical usage tests of Ketac-Fil as a retrograde filling material.

Alveolar Process↗
PubMed1989

Effects of interferons on immune response to a synthetic peptide malaria sporozoite vaccine in non-immune adults.

A Plasmodium falciparum sporozoite vaccine, composed of a synthetic dodecapeptide (NANP)3 coupled to tetanus toxoid (TT), was injected, at weeks 0 and 8, into non-immune volunteers in two randomized double-blind placebo-controlled trials. In the first trial, 37 volunteers received the vaccine simultaneously with placebo (group 1), 0.5 x 10(6-) (group 2), or 1.5 x 10(6) U (group 3) of recombinant human interferon-alpha (= IFN-alpha). In the second trial, 35 other volunteers received the vaccine with placebo (group 4), 0.25 x 10(6) (group 5), or 1.0 x 10(6) IU (group 6) of interferon-gamma (= IFN-gamma). Immunizations were well tolerated and resulted in seroconversion rates (greater than or equal to 4-fold increase of antibody titre in immunofluorescence or enzyme-linked immunosorbent assays) of 67-100% of volunteers. IFN-alpha significantly enhanced the IgG antibody titres in ELISA to malaria peptide.

Adjuvants, Immunologic↗
PubMed1988

Major surface antigen p190 of Plasmodium falciparum: detection of common epitopes present in a variety of plasmodia isolates.

Plasmodium falciparum merozoites are covered with polymorphic proteins that are processed from a 190 kd (p190) precursor protein. These are candidates for an antimalarial vaccine. We cloned and expressed a number of DNA fragments, comprising almost the entire p190 gene of the K1 isolate, in Escherichia coli. Pooled human endemic-area sera and rabbit antibodies raised against p190 protein isolated from K1 parasites react with only a limited number of the recombinant proteins. From these studies we could select two antigenic polypeptides containing conserved amino acid stretches of the otherwise highly polymorphic protein. Rabbits and mice injected with the purified recombinant proteins produce antibodies reacting differentially with various isolates of P. falciparum. We obtained antibodies detecting all isolates tested and a monoclonal antibody specific for isolates containing a K1 type allele of the p190 gene.

Amino Acid Sequence↗
PubMed1980

Presence of T 145 on cytolytic T cell lines and their lectin-resistant mutants.

Murine cytolytic T cell lines have been analyzed for the expression of two surface glycoproteins called T145 and T130. T145, known to be expressed by activated cytolytic T cells, is also expressed by such lines, but T130, which has been described by a universal T cell marker, is not. Our results suggest a structural relationship between T145 and T130. Vicia villosa lectin, which binds selectively to T145 of activated T cells and which is cytotoxic for cytolytic T cell lines, has been used to select lectin-resistant mutants from these lines. Five independent lectin-resistant mutants have been obtained. All of them are cytolytically active, bind up to 100-fold less lectin than the parental lines, but still express T145 or a closely related glycoprotein.

Animals↗
PubMed1976

Chemical properties of two antigens controlled by the major histocompatibility complex of the chicken.

The chemistry of antigens controlled by the major histocompatibility complex of the chicken has been investigated. Peripheral blood leukocytes of five chicken strains were radioactively labeled by incorporation of tritiated amino acids, enzymatic iodination, or mild periodate oxidation followed by reduction with tritiated sodium borohydride. Membrane-bound antigens were solubilized with Nonidet P-40 and purified by a two-step immunoprecipitation procedure. The resulting immunoprecipitates were analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis under reducing or nonreducing conditions. The chicken major histocompatibility antigens (B antigens) are composed of polypeptide chains with molecular weights (in the reduced form) of 40,000 to 43,000 and 11,000 to 12,000, as deduced from their mobilities in internally calibrated gels. The larger chains, when isolated from different chicken strains, can have slightly different mobilities in such gels; thus the mobilities of the large polypeptides from strains WA and WB correspond to molecular weights of 40,000 and 43,000, respectively. Gels run under nonreducing conditions give similar results; in particular no dimers or oligomers of the larger chains are detectable, thus ruling out an immunoglobulin-like structure for the B antigens. The large chains are labeled by the periodate oxidation-reduction procedure, suggesting that they are glycoproteins (probably containing sialic acid), while the small polypeptides cannot be labeled by this method. An additional protein or proteins of apparent molecular weight about 30,000 could be precipitated from 3H-amino-acid-labeled leukocyte lysates by one particular anti-B serum. This protein(s), named B-L, differs from the B major histocompatibility antigens in that it is not associated with the small chain of molecular weight 11,000 to 12,000 and does not occur on erythrocytes. Thus, at least two protein chains are coded for (or have their synthesis controlled by) genes in the chicken major histocompatibility complex.

Animals↗