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Identification of the intersubunit binding region in rat tyrosine hydroxylase.

Abstract：

:Limited proteolysis converts the 39200 molecular weight catalytic domain of rat tyrosine hydroxylase to a monomer with a molecular weight of 37600. The purified monomer is almost fully active, with minor changes in kinetic parameters at pH 7. Mass spectral analysis and N-terminal sequencing of the proteolytically generated species establish that 20 amino acids have been removed from the carboxyl terminus and five from the amino terminus. Based on these results, the carboxyl terminus is responsible for tetramer formation by tyrosine hydroxylase. The sequence of amino acids which is removed is consistent with a coiled coil structure in the intact tetramer.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Lohse DL,Fitzpatrick PF

doi

10.1006/bbrc.1993.2653

subject

Has Abstract

pub_date

1993-12-30 00:00:00

pages

1543-8

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(83)72653-7

journal_volume

197

pub_type

杂志文章

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