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Human free secretory component is composed of the first 585 amino acid residues of the polymeric immunoglobulin receptor
Author(s) -
Hughes Graham J,
Frutiger Séverine,
Savoy Luc-Alain,
Reason Andrew J,
Morris Howard R,
Jaton Jean-Claude
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)00629-7
Subject(s) - secretory component , residue (chemistry) , chemistry , peptide sequence , arginine , polymeric immunoglobulin receptor , complementary dna , antibody , biochemistry , amino acid , amino acid residue , receptor , stereochemistry , biology , gene , genetics
The main objective of this work was to unequivocally determine the C‐terminal sequence of human milk free secretory component (SC). It was found to end at arginine‐585, i.e. 33 amino acids downstream from the major heterogeneous C‐terminal residue previously identified for colostrum SC. In contrast, our data showed that the C‐terminal end of SC was found to be homogeneous. Conflicting assignments, Asp/Gln, a missing Asn‐211, Asp/Asn, Glu/Gln were corrected and found to agree with the cDNA sequence. An Ala/Val substitution at position 562 (domain VI) was identified. Its genetic significance is uncertain at present.