Literature DB >> 27175

Reversible inactivation of tyrosine aminotransferase from guinea pig liver by thiol and disulfide compounds.

G Federici, D Di Cola, P Sacchetta, C Di Ilio, G Del Boccio, G Polidoro.   

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Year:  1978        PMID： 27175     DOI： 10.1016/0006-291x(78)91585-1

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN： 0006-291X            Impact factor:   3.575


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  6 in total

1.  Enzyme inactivation via disulphide-thiol exchange as catalysed by a rat liver membrane protein.

Authors:  G L Francis; F J Ballard
Journal:  Biochem J       Date:  1980-02-15       Impact factor: 3.857

2.  Tyrosine aminotransferase: biochemical and structural properties and molecular dynamics simulations.

Authors:  Prajwalini Mehere; Qian Han; Justin A Lemkul; Christopher J Vavricka; Howard Robinson; David R Bevan; Jianyong Li
Journal:  Protein Cell       Date:  2010-12-10       Impact factor: 14.870

3.  Effect of physiological reducing compounds on the inactivation of tyrosine aminotransferase from guinea-pig liver.

Authors:  D Di Cola; G Federici
Journal:  Biochem J       Date:  1982-08-01       Impact factor: 3.857

4.  Cysteine-dependent inactivation of hepatic ornithine decarboxylase.

Authors:  Y Murakami; T Kameji; S Hayashi
Journal:  Biochem J       Date:  1984-01-15       Impact factor: 3.857

5.  Quantitative microspectrophotometrical determination of protein thiols and disulfides with 2,2'-dihydroxy-6,6'-dinaphthyldisulfide (DDD). The variety of DDD-staining methods demonstrated on Ehrlich ascites tumor cells.

Authors:  G Nöhammer
Journal:  Histochemistry       Date:  1982

6.  Destabilization of tyrosine aminotransferase by amino acids.

Authors:  J L Hargrove; C Liu
Journal:  Amino Acids       Date:  1994-10       Impact factor: 3.520
  6 in total

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