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(Received for publication, November 18, 1996, and in revised form, January 24, 1997)
From The Wellcome Trust Centre for Cell-Matrix Research, University
of Manchester, 2.205, Stopford Building, Manchester M139PT, United
Kingdom
It has been demonstrated previously that
respiratory secretions contain three oligomeric, gel-forming mucins;
one of these was identified as the product of the MUC5AC
gene (1). Here we demonstrate that the other two mucins are glycoforms
of the MUC5B gene product. This was accomplished by trypsin treatment
of the purified reduced mucin subunit populations and N-terminal
sequencing of the liberated peptides. The products of trypsin digestion
were separated by gel filtration into high molecular weight mucin
glycopeptides and low molecular weight tryptic peptides. The latter
were fractionated by reverse phase chromatography, and four of the
major peptides were sequenced. Three of these peptides were identical
to and contiguous within a 51-amino acid sequence deduced from a
cDNA clone (JER57) encoding a portion of the MUC5B mucin. The other peptide is also present within this sequence but showed identity in
only 9 of its 10 residues. A polyclonal antiserum raised against one of
these peptides was reactive with the two putative MUC5B glycoforms.
Analysis of the high molecular weight glycopeptides indicated that the
MUC5B subunit contained different types and lengths of glycosylated
domains; one domain of Mr 7.3 × 105, two domains of Mr 5.2 × 105, and a third domain of Mr
2.0 × 105. The amino acid composition of the larger
two glycopeptides was similar in serine, threonine, and proline content
but distinct from that of the smallest glycopeptide. Each of these
domains in the mucin subunit is separated by a trypsin-sensitive
region, and the relative abundance of the major peptides derived by
proteolysis of these regions and their occurrence in a contiguous
sequence suggest that they contain a common cysteine-rich motif.
Volume 272, Number 14,
Issue of April 4, 1997
pp. 9561-9566
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
EVIDENCE FOR A CYSTEINE-RICH SEQUENCE REPEATED WITHIN THE
MOLECULE
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