TY - JOUR
T1 - Major intrinsic polypeptide (MIP26K) from lens membrane
T2 - Reconstitution into vesicles and inhibition of channel forming activity by peptide antiserum
AU - Gooden, M.
AU - Rintoul, D.
AU - Takehana, M.
AU - Takemoto, L.
PY - 1985/4/30
Y1 - 1985/4/30
N2 - Bovine and human lens membrane, when reconstituted into lipid vesicles containing oxidized cytochrome C, will mediate the transmembrane passage of ascorbate into the vesicles, where the reduction of cytochrome C is measured spectrophotometrically. This channel forming activity is specifically inhibited by antiserum made against a synthetic octapeptide near the C-terminus of MIP26K. Together, these studies describe a direct and more sensitive assay system for measurement of channel-forming activity of MIP26K, and suggest that the C-terminus of this molecule may be particularly important in the regulation of channel formation.
AB - Bovine and human lens membrane, when reconstituted into lipid vesicles containing oxidized cytochrome C, will mediate the transmembrane passage of ascorbate into the vesicles, where the reduction of cytochrome C is measured spectrophotometrically. This channel forming activity is specifically inhibited by antiserum made against a synthetic octapeptide near the C-terminus of MIP26K. Together, these studies describe a direct and more sensitive assay system for measurement of channel-forming activity of MIP26K, and suggest that the C-terminus of this molecule may be particularly important in the regulation of channel formation.
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U2 - 10.1016/0006-291X(85)90145-7
DO - 10.1016/0006-291X(85)90145-7
M3 - Article
C2 - 2581574
AN - SCOPUS:0021789405
SN - 0006-291X
VL - 128
SP - 993
EP - 999
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 2
ER -