Abstract
AbstractA protein fraction was isolated from rat mast cell granules. Disc gel electrophoresis and peptide mapping showed this fraction to be a mixture of 1 or 2 main components and 2–3 minor components. On ultracentrifugation the protein fraction behaved as an homogeneous material with a molecular weight of 5600. Amino acid analysis showed the presence of all the common amino acids (with the possible exception of tryptophan). High contents of lysine, aspartic acid, glutamic acid, proline, glycine and valine were noted. The content of cysteine was remarkably low. The isoelectric point of the main component(s) was found to be around 9.
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