[HTML][HTML] An autocatalytic cleavage in the C terminus of the human MUC2 mucin occurs at the low pH of the late secretory pathway
ME Lidell, MEV Johansson, GC Hansson - Journal of Biological Chemistry, 2003 - ASBMB
During purification of a recombinant MUC2 C terminus expressed in CHO-K1 cells, the
protein was partly cleaved when buffers with a pH of 6.0 were used. When buffers with
higher pH values were used, less cleavage was found. Disulfide bonds held the two
fragments generated together as these were only observed after reduction. Edman
sequencing of the C-terminal 110-kDa fragment revealed that the cleavage had occurred at
an Asp-Pro bond, a site described previously to generate the so-called" link peptide" after …
protein was partly cleaved when buffers with a pH of 6.0 were used. When buffers with
higher pH values were used, less cleavage was found. Disulfide bonds held the two
fragments generated together as these were only observed after reduction. Edman
sequencing of the C-terminal 110-kDa fragment revealed that the cleavage had occurred at
an Asp-Pro bond, a site described previously to generate the so-called" link peptide" after …