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S McKneally

Publications and source records attributed to S McKneally.

5 recordsLinked to original sources
PubMed1973

Experimental allergic encephalomyelitis in the rat: response to encephalitogenic proteins and peptides.

Lewis rats were used to determine the encephalitogenic activity of myelin basic protein of different species and of 45-residue fragments of basic protein. Basic protein from guinea pigs was more active than that from rats, and the fragments from the two species showed the same order of activity. Bovine basic protein was the least active of the intact proteins, and the respective fragment was inactive. Studies of serum-binding capacity did not support the hypothesis that blocking antibody played a role in this biological variation, whereas consideration of the amino acid sequences of the three fragments suggested that differences in primary structure, operating either at the sensitization or the effector phase of the immune response, could account for the variation.

Amino Acid Sequence↗
PubMed1971

Biologicl activity and synthesis of an encephalitogenic determinant.

A 45-residue fragment of the basic protein of myelin is encephalitogenic in the rabbit and monkey but relatively inactive in the guinea pig. Synthetic peptides containing the sequence of a tryptic peptide of the fragment Thr-Thr-His-Tyr-Gly-Ser-Leu-Pro-Gln-Lys are moderately encephalitogenic.

Amino Acid Sequence↗
PubMed1969

Encephalitogenic protein: structure.

Amino acid sequences of encephalitogenic proteins from bovine cord and rabbit brain are reported. The bovine protein contains 45 residues. The rabbit protein is identical except for two isopolar substitutions, a dipeptide and amino acid deletion. Analysis of this protein and a 140-residue myelin basic protein indicates that the smaller protein is a portion of the larger encephalitogen. The larger myelin protein contains at least two encephalitogenic sites.

Amino Acid Sequence↗