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Experimental Phenylketonuria: Replacement of Carboxyl Terminal Tyrosine by Phenylalanine in Infant Rat Brain Tubulin

J.A. Virseda Rodríguez, Gary G. Borisy

Open publisher page 23 citations

Abstract

In the brains of newborn rats, about half of the tubulin molecules are modified posttranslationally by the addition of an aromatic amino acid at the carboxyl terminus of the alpha chain. Of the added residues, 96 percent are tyrosine and 4 percent are phenylalanine. After induction of hyperphenylalaninemia, the proportion of tubulin molecules containing carboxyl terminal phenylalanine increases up to eightfold and the pool of tyrosine-containing molecules decreases by an equivalent amount.

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What this paper is about

In the brains of newborn rats, about half of the tubulin molecules are modified posttranslationally by the addition of an aromatic amino acid at the carboxyl terminus of the alpha chain. Of the added residues, 96 percent are tyrosine and 4 percent are phenylalanine. After induction of hyperphenylalaninemia, the proportion of tubulin molecules containing carboxyl terminal phenylalanine increases up to eightfold and the pool of tyrosine-containing molecules decreases by an equivalent amount.

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Available abstract

In the brains of newborn rats, about half of the tubulin molecules are modified posttranslationally by the addition of an aromatic amino acid at the carboxyl terminus of the alpha chain. Of the added residues, 96 percent are tyrosine and 4 percent are phenylalanine. After induction of hyperphenylalaninemia, the proportion of tubulin molecules containing carboxyl terminal phenylalanine increases up to eightfold and the pool of tyrosine-containing molecules decreases by an equivalent amount.

Key concepts: Phenylalanine, Tyrosine, Hyperphenylalaninemia, Tubulin, Amino acid, Biochemistry, Chemistry, Stereochemistry

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Experimental Phenylketonuria: Replacement of Carboxyl Terminal Tyrosine by Phenylalanine in Infant Rat Brain Tubulin — Research Paper | ScholarLens