Alternative splicing and endoproteolytic processing generate tissue-specific forms of pituitary peptidylglycine alpha-amidating monooxygenase (PAM).
BA Eipper, CB Green, TA Campbell, DA Stoffers… - Journal of Biological …, 1992 - jbc.org
The pituitary is a rich source of peptidylglycine alpha-amidating monooxygenase (PAM).
This bifunctional protein contains peptidylglycine alpha-hydroxylating monooxygenase
(PHM) and peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL) catalytic domains
necessary for the two-step formation of alpha-amidated peptides from their peptidylglycine
precursors. In addition to the four forms of PAM mRNA identified previously, three novel
forms of PAM mRNA were identified by examining anterior and neurointermediate pituitary …
This bifunctional protein contains peptidylglycine alpha-hydroxylating monooxygenase
(PHM) and peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL) catalytic domains
necessary for the two-step formation of alpha-amidated peptides from their peptidylglycine
precursors. In addition to the four forms of PAM mRNA identified previously, three novel
forms of PAM mRNA were identified by examining anterior and neurointermediate pituitary …
