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E L McCandless

Publications and source records attributed to E L McCandless.

15 recordsLinked to original sources
PubMed1982

Carrageenan stimulates the release of dialyzable helper factors.

We found that 1 mg of carrageenan (CGN) could enhance the primary antibody response of BALB/c spleen cells to sheep erythrocytes (SRBC). This enhancement was dependent on the strain of mouse injected as well as the type of CGN administered. In vitro experiments with spleen cells from mice treated with CGN in vivo showed that these cells release low molecular weight factor(s) which enhanced the in vitro antibody response to SRBC. Thy 1+ cells were clearly involved in the production of this factor since depletion of these cells eliminated the helper effect of CGN-treated spleen cells. Our results suggest one possible mechanism by which CGN can modulate the immune response.

Adjuvants, Immunologic↗
PubMed1979

Incorporation of [S]Sulfate and [C]Bicarbonate into Karyotype-specific Polysaccharides of Chondrus crispus.

Gametophytic and sporophytic tissues of Chondrus crispus (Stackhouse) cultured in vitro were labeled with (35)S and (14)C. The major sulfated polysccharides isolated from the two karyotypes were characterized by KCI fractionation, immunoprecipitation, and infrared spectroscopy. Reproducibility of data has been demonstrated by an experiment using gametophytic T(4) strain with five replicates per time point. The rate of sulfate uptake was similar in haploid and diploid plants from a given area cultured for a similar time. Cultures from different sources cultured for different times showed different uptake and incorporation levels. Although sulfate uptake did not appear to be karyotype-related, the pattern of incorporation of (35)S and (14)C into polysaccharides was ploidy-specific.

Journal Article↗
PubMed1978

Anti-carrageenans.

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Antibody Formation↗
PubMed1978

The chemistry and immunochemistry of carrageenans from Eucheuma and related algal species.

Carrageenans from several species of Eucheuma have been fractionated into KC1-soluble and KC1-insoluble fractions and analyzed by the usual chemical procedures. An anti-kappa-carrageenan, the reactivity of which is directed to kappa-structures (i.e., 3-linked galactose 4-sulphate, and 4-linked 3,6-anhydrogalactose) was used to analyze these carrageenans immunochemically. The antibody preparation shows only a small amount of cross-reactivity with iota-type carrageenans and thus could be used to distinguish kappa- and iota-type carrageenans, the latter having an index of homology of less than 0.2. A comparison of chemical and immunochemical data yielded further information as to the nature of the carrageenan-anti-carrageenan interaction, as well as elucidating the finer structure of carrageenans.

Carrageenan↗
PubMed1978

The immunochemistry of lambda-type carrageenans from certain red algae.

An antibody preparation directed against a structural feature associated with 6-sulphate groups was used to probe structural relations among certain lambda-type carrageenans. Immunochemical and chemical differences are described between the KC1-soluble carrageenans from tetrasporic algal plants of Gigartina corymbifera, Gigartina sp. from San Francisco Bay, Petrocelis middendorfii, Iridaea cordata, Rhodoglossum californicum, and Chondrus crispus. The differences in immunochemical reactivity of the Gigartina and Petrocelis carrageenans relative to the homologous antigen (Chondrus crispus lambda-carrageenan) are attributed to the lower content of 6-sulphate groups on the 4-linked residues in the former carrageenans. Both the immunochemical and chemical data suggest that the Gigartina and Petrocelis carrageenans are largely xi-like in structure but do contain lambda-like features. The i.r. spectrum of the Petrocelis carrageenan differs from that of the Gigartina carrageenans. The carrageenans from I. cordata and R. californicum differ to a lesser degree from Chondrus crispus lambda-type carrageenan. These differences cannot be accounted for by differences in the levels of 6-sulphate groups. Some other structural feature, as yet unidentified, is responsible for the discrepancy in the immunochemical reactivity of these carrageenans to the anti-lambda-carrageenan.

Animals↗
PubMed1977

Agarose medium turbidimetric assay for cross reacting antigens.

Appropriate concentrations of carrageenan and antibody to carrageenan were mixed in a medium consisting of 0.1% agarose in 0.01 M phosphate-buffered saline pH 7.4 at 37 degrees C. The kinetics of precipitation were followed by turbidimetric analysis with a double beam Unicam spectrophotometer set at 420 nm. Addition of agarose enhanced the antigen--antibody reaction as judged by turbidity and served as a stabilizing medium permitting extended periods of continuous monitoring. The initial rate of precipitation was found to vary linearly with the concentration of antigen in the antibody excess zone. Both the critical rate of precipitation and final optical density were characteristic of the specific antigen-antibody reaction. These two parameters are used to quantitate the extent of a cross-reaction and to calculate an index of homology for the cross-reacting antigen to the homologous antigen.

Animals↗