The Human C3a des Arg molecule is one of three activation fragments formed from the activation of the complement cascade. C3a des Arg is formed from C3a via carboxypeptidase cleavage of the C-terminal arginine group. The structure of Human C3a des Arg was first reported in 1975 by Hugli. Human C3a des Arg contains 77 amino acids with 6 cysteines involved in disulfide bridges between residues 22-49, 23-56 and 36-57. The C terminal end of C3a des Arg in Human, porcine, rat, mouse and guinea pig is identical. C3a des Arg is a highly cationic molecule containing no carbohydrate. X-ray crystal data shows the N and C terminal residues to have highly flexible helical structures. C3a is one of the most potent constrictors of smooth muscle cells, and guinea pig airways are hyperresponsive to C3a when pretreated with histamine. The long term study of liver and other transplant recipients for both C3a des Arg and C4a des Arg may be useful in assessing a number of pathological conditions. The use of potent protease inhibitors, such as Futhan, in conjunction with EDTA, may allow complement activation factors to be quantitated specifically via inhibition of non-specific protease formation of C3a des Arg.

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