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Regulation of N-terminus-deleted human tyrosine hydroxylase type 1 by end products of catecholamine biosynthetic pathway

โœ Scribed by A. Ota; S. Yoshida; T. Nagatsu


Book ID
105140539
Publisher
Springer
Year
1996
Tongue
English
Weight
989 KB
Volume
103
Category
Article
ISSN
1435-1463

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Deletion of N-terminus of human tyrosine
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Wildtype human tyrosine hydroxylase (TH) type 1 and 4 mutants (del-52, a form with the first 52 amino acid residues deleted; del-157, one with the first 157 amino acid residues deleted; RR-EE, one in which Arg 37 -Arg 38 was replaced by Glu 37 -Glu 38 ; and S40D, one in which Ser 40 was replaced by