Raymond Shapira

TL;DR: High molecular weight homologues of gp91phox, the superoxide-generating subunit of phagocyte nicotinamide adenine dinucleotide phosphate (NADPH)-oxidase, have been identified in human and Caenorhabditis elegans and shown to catalyze the cross-linking of tyrosine residues involved in the stabilization of cuticular extracellular matrix.

TL;DR: Heterogeneity of human myeloperoxidase is accompanied by differences in cellular compartmentalization, enzymatic activity, and subunit structure, as well as charge heterogeneity observed on CM-cellulose.

TL;DR: Lewis rats were used to determine the encephalitogenic activity of myelin basic protein of different species and of 45-residue fragments of basic protein, and 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.

TL;DR: In the Lewis rat, fragment 43–88 of the highly encephalitogenic guinea‐pig basic protein has been previously shown to retain the full activity of the parent protein, and was subjected to controlled chymotryptic digestion so that cleavage occurred only at tyrosine 67, generating two peptides.

TL;DR: A 45-residue fragment of the basic protein of myelin is encephalitogenic in the rabbit and monkey but relatively inactive in the guinea pig.