Biomedical subjects

J R Spies

Publications and source records attributed to J R Spies.

10 recordsLinked to original sources

PubMed1980

Milk hypersensitivity: RAST studies using new antigens generated by pepsin hydrolysis of beta-lactoglobulin.

RAST was performed on sera from 28 patients with a variety of allergic symptoms, giving histories compatible with milk allergy, to investigate the occurrence of IgE antibodies to new antigens (NA) generated by in vitro pepsin hydrolysis. A variety of symptoms were associated with positive RAST scores. A positive correlation was found between the degree of RAST reactivity with undigested milk proteins and reactivity with the NA's. Reactivity to the NA's was always associated with reactivity to at least one of the undigested proteins. These findings suggest that undigested milk proteins are more reactive than digested proteins. Furthermore, antigens derived from pepsin digestion do not elicit a significant antibody response in individuals who do not allow show antibody responses to undigested proteins.

Adolescent↗

PubMed1975

Chemistry of allergens. XXII. Isolation and characterization of three new antigens from the dialysates of six successive pepsin hydrolyses of beta-lactoglobulin.

Twelve new antigens previously have been demonstrated in the pepsin digests of milk proteins. The term "new antigen" is defined as an antigen with a specificity distinct from that of the protein from which it was generated. Three new antigens (alpha-, beta-, and D2i) polypeptides and one nonantigenic gamma-polypeptide have been isolated from the dialysates of six successive pepsin hydrolyses of beta-lactoglobulin. The alpha- and beta-polypeptides were 1/5 and D2i was 1/10-1/20 as potent immunogens as precursor beta-lactoglobulin as determined by the Schultz-Dale technique. The minimum observed amounts of new antigen eliciting maximum response of uterine strips in the Schultz-Dale tests were: alpa-D2, 50 ng; beta-D2, 15 ng; beta-D3; 10 ng; and D2i, 1,000 ng. Except for the alpha-polypeptide, the amino acid contents of the polypeptides differed markedly from that of beta-lactoglobulin. The beta-polypeptide has been tentatively identified as a 33 amino acid fragment of beta-lactoglobulin (3,910 daltons). The gamma-polypeptide has been tentatively identified as a 12 amino acid fragment of beta-lactoglobulin (1,372 daltons).

Amino Acids↗

PubMed1972