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Biomedical subjects

E D Day

Publications and source records attributed to E D Day.

At least 55 records · Page 3Linked to original sources
PubMed1981

Goblet cell glycoprotein: an organ-specific antigen for gut. Isolation, tissue localization and immune response.

We report, for the first time, immune responses within two lines of inbred rats to a purified Lewis rat glycoprotein antigen which is organ-specific for intestine. The antigen was prepared by solubilization of gut epithelial cell-associated macromolecules, fractionation in ethanol, and molecular sieve chromatography over Sepharose 2B. Homogeneity of the end product (RGCG-PK1) was supported by results of both double diffusion in agar and SDS polyacrylamide gel electrophoresis. Amino acid analysis and specific sugar determination proved that RGCG-PK1 was not a classical mucin because of its comparatively high tyrosine and low galactosamine + glucosamine content, and the absence of glycosidic linkages to serine and threonine. Organ-specificity was shown by the ability of RGCG (but not liver homogenate) to inhibit precipitation and haemagglutination by heterologous specific sera. Organ-specificity was confirmed by the demonstration of RGCG-PK1-specific immunofluorescence staining of rat small and large intestine, but not esophagus, stomach or liver. RGCG-PK1 determinants within rat and human small bowel were found to be confined to goblet cells and intestinal glycocalyx. Anti-RCGC-PK1 serum showed no reactivity with highly purified xenogeneic mucins nor with syngeneic small bowel mucin. Specific antibody (as well as antibody-dependent cellular cytotoxicity) to RGCG was elicited and detected for up to 10 days in two lines of inbred rats, including the one (Lewis) from which the antigen was isolated. The duration and peak of the humoral immune response were abbreviated compared with that of a xenogeneic control glycoprotein studied in parallel, probably due to immunoregulatory mechanisms operative for self antigens.

Amino Acids↗
PubMed1981

The major heat stable allergen of shrimp.

Serum from a patient who had experienced several episodes of anaphylaxis after eating shrimp was used to monitor the isolation of a major allergen from shrimp, which was then tested with sera from 10 other shrimp-reactive patients. The allergen was isolated from a fresh extract of boiled shrimp by gel filtration and from raw shrimp by gel filtration and agarose electrophoresis. The purity of the allergen was established by crossed immunoelectrophoresis against rabbit and guinea pig antisera; it gave only a single peak in each case. The native allergen was excluded on Sephadex G-200 but showed a single band at 38000d in SDS-PAGE with or without reduction. The isoelectric point was about 4.5. The allergen contained about 4% carbohydrate and only 7 Tyr and 9 Phe out of 341 amino acid residues. Using the RAST with 11 allergic sera, the allergen gave a correlation coefficient of 0.98 with whole cooked shrimp extract and of 0.66 with raw shrimp extract. The allergen was a potent inhibitor of RAST to both cooked and raw shrimp. A second, weaker allergen of 21000d chain size was isolated from raw shrimp in highly purified form.

Allergens↗
PubMed1978

Myelin basic protein serum factor. An endogenous neuroantigen influencing development of experimental allergic encephalomyelitis in Lewis rats.

Age-related concentrations of myelin basic protein serum factor (MBP-SF), an endogenous neuroantigen detected and quantitated by inhibition of binding of rat myelin basic protein (RMBP) antibody with 125I-RMBP reagent antigen and immunochemically indistinguishable from native RMBP in this respect, reach peak levels as high as 21 ng/microliter among 2-3-wk-old normal suckling Lewis rats. Levels then progressively decline to low, usually undetectable levels of less than or equal to 0.6 ng/microliter MBP-equivalents in adult animals by 7 wk of age. MBP-SF levels are inversely related to the age-related increasing capacity of maturing Lewis rats to develop experimental allergic encephalomyelitis (EAE) after sensitization to MBP of syngeneic, but not xenogeneic, origin. MBP-SF appears to be an endogenous neuroimmunoregulatory product of potential importance for immunologic tolerance to autologous RMBP in Lewis rats.

Animals↗