Human free secretory component is composed of the first 585 amino acid residues of the polymeric immunoglobulin receptor

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,...

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Bibliographic Details
Published in:FEBS letters 1997-06, Vol.410 (2), p.443-446
Main Authors: Hughes, Graham J, Frutiger, Séverine, Savoy, Luc-Alain, Reason, Andrew J, Morris, Howard R, Jaton, Jean-Claude
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Carboxy-terminal region
Chromatography, High Pressure Liquid
dithiothreitol
DTT
electrospray mass spectrometry
ES-MS
FAB-MS
fast atom bombardment mass spectrometry
Female
Humans
Molecular Sequence Data
peptide-N-glycosidase F
PNGase F
poly-Ig receptor
polymeric Ig receptor
Polymeric immunoglobulin receptor
Receptors, Polymeric Immunoglobulin - chemistry
restriction fragment length polymorphism
RFLP
Secretory component
Secretory Component - chemistry
secretory immunoglobulin A
sIgA
TFA
tosyl-l-phenylalanine chloromethyl ketone
TPCK
trifluoroacetic acid
Trypsin - metabolism
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Summary: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.
ISSN:0014-5793
1873-3468
DOI:10.1016/S0014-5793(97)00629-7