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Biomedical subjects

E Appella

Publications and source records attributed to E Appella.

At least 397 records · Page 22Linked to original sources
PubMed1971

Structural basis of the A14 and A15 allotypic specificities in rabbit immunoglobulin G.

The structural basis for the A14 and A15 allotypic specificities of rabbit immunoglobulin G was investigated with Fe fragments prepared from homozygous rabbits. The presence of threonine in the Cgamma2 region (position 309: Eu numbering) correlates with the A14 allotype; the presence of alanine at this same position correlates with the A15. Now that the sequence of the Cgamma2 region of rabbit IgG has been completely elucidated, a high degree of homology of the constant region domains of rabbit and human gamma chains is apparent (about 60-80%).

Amino Acid Sequence↗
PubMed1970

Serological and immunogenic activity of soluble mouse transplantation antigens controlled by the H-2 locus.

The solubilization and partial purification of mouse transplantation antigens were monitored by (1) an in vitro assay for alloantigenic specificities and (2) an in vivo assay for transplantation antigens controlled by the H-2 histocompatibility locus. Antigens from A/J mice were solubilized by papain and fractionated on a Sephadex G-150 column. The eluate showed a 280 nm absorbance peak (F(1)) in the excluded volume and two peaks (F(2) and F(3)) in the included volume. H-2 specificities 1, 3, 4, 5, 11, 23, and 28 were confined to a single peak in the F(2) fraction. Fractions F(1), F(2), and F(3), were tested for their ability to accelerate skin graft rejection in noncoisogenic strains which differ at both H-2 and non-H-2 loci, and coisogenic strains which differ only at the H-2 locus. All fractions produced significant acceleration of graft rejection in the noncoisogenic strains, but only fraction F(2) produced significant acceleration in the coisogenic strains. These findings indicate that H-2 transplantation antigens detected by our in vivo assay, and H-2 alloantigenic specificities detected by our in vitro assay are solubilized by papain and are eluted in the same peak during Sephadex fractionation.

Alleles↗
PubMed1966

Light chains of mouse myeloma proteins: partial amino acid sequence.

Five kappa chains in the urinary proteins of the BALB/c mouse have the same carboxyl terminal amino acid sequence; this sequence resembles that of kappa light chains in human immunoglobulins. The five chains have amino acid sequence variations at the amino- terminal. The genetic basis for the amino- terminal variations is not understood but could be due either to a mecha nism for differently translating a single genetic message or to the presence of more than one kappa- type structural cistron in the BALB/c genome.

Amino Acid Sequence↗
PubMedDate not supplied

The development of multi-epitope vaccines: epitope identification, vaccine design and clinical evaluation.

We have developed efficient methods for epitope identification and vaccine design. Our process for epitope selection based on the combined use of motif analyses, binding assays and immunogenicity evaluations is described. We also describe how the projected population coverage and vaccine design can be optimized. Finally, it is discussed how vaccine potency is evaluated by immunogenicity and antigenicity assays.

Epitopes↗