TY - JOUR
T1 - Tissue distribution and characterization of peptide C-terminal α-amidating activity in rat
AU - Sakata, Junichiro
AU - Mizuno, Kensaku
AU - Matsuo, Hisayuki
PY - 1986/10/15
Y1 - 1986/10/15
N2 - The C-terminal α-amide formation of peptides is one of the most important events in prohormone processing. Recently, we developed a simple and sensitive assay for detecting α-amidating activity in tissues by using (125I)-Ac-Tyr-Phe-Gly as a substrate. Using this assay method, we have determined the tissue distribution of α-amidating enzyme activity in adult male rat. High concentrations of α-amidating activity were found in pituitary, brain, thyoid, gastrointestinal tract, pancreas, heart, submaxillary glands and parotid glands. Alpha-amidating enzyme activities in all tissues examined exhibit very similar copper and ascorbate requirements, pH dependence, and behavior on gel-filtration.
AB - The C-terminal α-amide formation of peptides is one of the most important events in prohormone processing. Recently, we developed a simple and sensitive assay for detecting α-amidating activity in tissues by using (125I)-Ac-Tyr-Phe-Gly as a substrate. Using this assay method, we have determined the tissue distribution of α-amidating enzyme activity in adult male rat. High concentrations of α-amidating activity were found in pituitary, brain, thyoid, gastrointestinal tract, pancreas, heart, submaxillary glands and parotid glands. Alpha-amidating enzyme activities in all tissues examined exhibit very similar copper and ascorbate requirements, pH dependence, and behavior on gel-filtration.
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U2 - 10.1016/0006-291X(86)91080-6
DO - 10.1016/0006-291X(86)91080-6
M3 - Article
C2 - 3778444
AN - SCOPUS:0023036383
SN - 0006-291X
VL - 140
SP - 230
EP - 236
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 1
ER -