Peptidylglycine alpha amidating

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peptidylglycine alpha amidating-24peptidylglycine alpha amidating-1

With the purified enzyme, we detected an intermediate of the alpha-amidating reaction by high performance liquid chromatography analysis.

The production of the intermediate required copper, oxygen, and ascorbate and increased linearly with incubation time.

Its apparent molecular mass (43 kd), estimated by both SDS-PAGE and molecular sieving, was higher than the value (39 kd) for the ' PAM' (AE-I) purified from frog skin.

N-terminal sequence analysis indicated that cleavage of signal sequence had occurred but the propeptide still remained at the N terminus.

Its apparent molecular mass (43 kd), estimated by both SDS-PAGE and molecular sieving, was higher than the value (39 kd) for the 'PAM' (AE-I) purified from frog skin.

It was shown that the purified enzyme had converted the model peptide to the C-terminal alpha-hydroxyglycine-extended peptide [X-Gly(OH)] instead of the amidated product (X-NH2), indicating that the enzyme widely known as 'PAM' should be called 'peptidylglycine alpha-hydroxylating monooxygenase'.

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It was shown that the purified enzyme had converted the model peptide to the C-terminal alpha-hydroxyglycine-extended peptide [X-Gly(OH)] instead of the amidated product (X-NH2), indicating that the enzyme widely known as ' PAM' should be called 'peptidylglycine alpha-hydroxylating monooxygenase'.

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