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The primary structure of porcine complement c 3a anaphylatoxin


, : The primary structure of porcine complement c 3a anaphylatoxin. Journal of Immunology 117(3): 990-995

Porcine C3a [a fragment of the 3rd complement component] was generated in whole porcine serum by inulin activation of enzymes of the alternative complement pathway. The C3a anaphylatoxin was isolated according to procedures previously described. The complete amino acid sequence for porcine C3a was determined utilizing automatic sequencing techniques in addition to manual subtractive Edman degradation and carboxypeptidase A, B or Y digestion of isolated peptides. Porcine C3a is composed of a polypeptide chain containing 77 amino acid residues and has a MW of approximately 9000 daltons. This C3a molecule is devoid of threonine, tryptophan and carbohydrates. The proposed primary structure for porcine C3a is as follows: .**GRAPHIC**. .**GRAPHIC**. .**GRAPHIC**. .**GRAPHIC**. .**GRAPHIC**. Comparisons between the amino acid sequences of human and porcine C3a reveal that the 6 half-cystinyl and 5 aromatic residue positions are conserved. Conservation of these 6 half-cystinyl residue positions suggest that the disulfide arrangement remains identical in both anaphylatoxin molecules. Maintenance of 3 interconnected disulfide linkages helps to explain a near identity between the secondary structures of human and porcine C3a as indicated by circular dichroism measurements. Particular attention was focused on the COOH-terminal region of the anaphylatoxins since an arginyl residue at position 77 is functionally essential in human and porcine C3a. Five residue positions at the carboxy termini were observed in both C3a molecules, and the sequence Leu-Gly-Leu-Ala-Arg probably relates directly to anaphylatoxin activity. A total of 23 residue replacements occur between human and porcine C3a which accounts for a 30% difference in primary structure. Although the C3a molecules exhibit identical biologic activity, this large structural difference readily explains the absence of a detectable immunologic cross-reactivity.

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Related references

Hugli, T.E., 1975: Human anaphylatoxin complement c 3a from the complement c 3 primary structure. Journal of Biological Chemistry 250(21): 8293-8301

Corbin, N.C.; Hugli, T.E., 1976: The primary structure of porcine C3a anaphylatoxin. Porcine C3a was generated in whole porcine serum by inulin activation of enzymes of the alternative complement pathway. The C3a anaphylatoxin was isolated according to the procedures previously described by Hugli. The complete amino acid sequence...

Hugli, T.E., 1975: Human anaphylatoxin (C3a) from the third component of complement. Primary structure. C3a anaphylatoxin is derived from the third component (C3) of the blood complement system. Selective proteolysis of C3 by activated proenzymes indigenous to blood generates the C3a fragment. Human C3a was isolated from inulin-activated serum conta...

Jun, S.Whan.; Kim, T.Hoon.; Lee, H.Man.; Lee, S.Hoon.; Kim, W.Joo.; Park, S.Jin.; Kim, Y.Soo.; Lee, S.Hag., 2008: Overexpression of the anaphylatoxin receptors, complement anaphylatoxin 3a receptor and complement anaphylatoxin 5a receptor, in the nasal mucosa of patients with mild and severe persistent allergic rhinitis. Background: Although the complement anaphylatoxin peptides, complement anaphylatoxin 3a (C3a) and complement anaphylatoxin 5a (C5a), are implicated in the inflammatory process in allergic rhinitis, a direct interaction between allergic mucosa and...

Smith, M.A.; Gerrie, L.M.; Dunbar, B.; Fothergill, J.E., 1982: Primary structure of bovine complement activation fragment C4a, the third anaphylatoxin. Purification and complete amino acid sequence. Purification of C4a from heat-activated bovine plasma by elution from CM-Sephadex C-50 at pH 7.4 and gel filtration on Sephadex G-50 gives a 20% yield of pure C4a. The complete amino acid sequence of bovine C4a has been determined by automatic seq...

Smith M.A.; Gerrie L.M.; Dunbar B.; Fothergill J.E., 1982: Primary structure of bovine complement activation fragment c 4a the 3rd anaphylatoxin purification and complete amino acid sequence. Purification of C4a [complement component 4a] from heat-activated bovine plasma by elution from CM-Sephadex C-50 at pH 7.4 and gel filtration on Sephadex G-50 gives a 20% yield of pure C4a. The complete amino acid sequence of bovine C4a was determ...

Morgan, W.T.; Vallota, E.H.; Müller-Eberhard, H.J., 1974: Circular dichroism of C5a anaphylatoxin of porcine complement. Biochemical and Biophysical Research Communications 57(3): 572-577

Stimler N.P.; Hugli T.E.; Bloor C.M., 1979: Pulmonary injury induced by porcine complement c 5a anaphylatoxin. Federation Proceedings 38(3 PART 1): 1343

Gerard, C.; Hugli, T.E., 1980: Amino acid sequence of the anaphylatoxin from the fifth component of porcine complement. Journal of Biological Chemistry 255(10): 4710-4715

Gerard C.; Hugli T.E., 1979: Anaphylatoxin from porcine complement c 5 purification and partial chemical characterization. A novel procedure for porcine C5a [a fraction of complement component 5] purification is described which yields milligram quantities of anaphylatoxin from 1 l of complement-activated serum. Isolation strategy employs acid precipitation of the acti...