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. 1972 Oct;129(5):1131–1138. doi: 10.1042/bj1291131

Inactivation of tyrosine aminotransferase in neutral homogenates and rat liver slices

F Auricchio 1, L Mollica 1, A Liguori 1
PMCID: PMC1174272  PMID: 4144232

Abstract

Inactivation of tyrosine aminotransferase induced in vivo by triamcinolone was studied in a homogenate incubated at neutral pH values. The integrity and the presence of subcellular particles together with a compartment of acidic pH are necessary for inactivation of tyrosine aminotransferase. It is suggested that tyrosine aminotransferase is inactivated inside lysosomes. The system responsible for inactivation of tyrosine aminotransferase was partially purified and identified with lysosomal cathepsins B and B1. Inactivation of tyrosine aminotransferase in liver slices is controlled by the amino acid concentration and strongly stimulated by cysteine. 3,3′,5-Tri-iodo-l-thyronine reversibly and strongly decreases the rate of inactivation of tyrosine aminotransferase. The effect is not due to an increased rate of tyrosine aminotransferase synthesis.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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