1-Anilinonaphthalene-8-sulphonate, a fluorescent conformational probe for glutamate dehydrogenase - PubMed

1-Anilinonaphthalene-8-sulphonate, a fluorescent conformational probe for glutamate dehydrogenase

Doddgh et al. Biochem J. 1969 Sep.

Abstract

1. The interaction of 1-anilinonaphthalene-8-sulphonate with ox liver glutamate dehydrogenase was examined. 2. The fluorescence of the dye is enhanced 100-fold on binding. 3. A further enhancement is observed when NADH and GTP are added to the enzyme. 4. By using this property of the dye to measure conformational equilibria in the enzyme the effects of coenzyme, inhibitors, enzyme concentration, ionic strength and pH on the allosteric transitions were studied. 5. GTP and NADH interact with the enzyme in a heterotropic manner. 6. The rate of the structural transition brought about by GTP and NADH is biphasic with half-lives of 34 and 200msec. 7. The relation of these observations to regulatory mechanisms is discussed.

Similar articles

• Desensitization of glutamate dehydrogenase by reaction of tyrosne residues.

  Price NC, Radda GK. Price NC, et al. Biochem J. 1969 Sep;114(2):419-27. doi: 10.1042/bj1140419. Biochem J. 1969. PMID: 5810106 Free PMC article.

• 8-Anilino naphthalene sulfonate binding as a probe for conformational changes induced in glutamate dehydrogenase by regulatory reagents.

  Thompson W, Yielding KL. Thompson W, et al. Arch Biochem Biophys. 1968 Aug;126(2):399-406. doi: 10.1016/0003-9861(68)90424-4. Arch Biochem Biophys. 1968. PMID: 5691576 No abstract available.

• The mechanism of substrate and coenzyme binding to clostridial glutamate dehydrogenase during reductive amination.

  Basso LA, Engel PC, Walmsley AR. Basso LA, et al. Eur J Biochem. 1995 Dec 1;234(2):603-15. doi: 10.1111/j.1432-1033.1995.603_b.x. Eur J Biochem. 1995. PMID: 8536710

• Conformational changes and the regulation of glutamate-dehydrogenase activity.

  Bayley PM, Radda GK. Bayley PM, et al. Biochem J. 1966 Jan;98(1):105-11. doi: 10.1042/bj0980105. Biochem J. 1966. PMID: 4287181 Free PMC article.

• [Regulation of ox liver glutamate dehydrogenase activity by coenzymes].

  Popova SV, Sugrobova NP. Popova SV, et al. Biokhimiia. 1983 Nov;48(11):1783-7. Biokhimiia. 1983. PMID: 6661450 Russian.

Cited by

• Thiol groups of ribonucleic acid polymerase.

  King AM, Nicholson BH. King AM, et al. Biochem J. 1972 Jul;128(3):90P-91P. Biochem J. 1972. PMID: 4564260 Free PMC article. No abstract available.

• Conformational studies on phospholipase C from Bacillus cereus. The effect of urea on the enzyme.

  Little C. Little C. Biochem J. 1978 Dec 1;175(3):977-86. doi: 10.1042/bj1750977. Biochem J. 1978. PMID: 105729 Free PMC article.

• Interaction of 1-anilino-8-naphthalene sulfonate with yeast glyceraldehyde-3-phosphate dehydrogenase.

  Nagradova NK, Asryants RA, Ivanov MV. Nagradova NK, et al. Experientia. 1971 Oct 15;27(10):1169-70. doi: 10.1007/BF02286905. Experientia. 1971. PMID: 5127865 No abstract available.

• The effects of phospholipids on the activation of glutamate dehydrogenase by L-leucine.

  Couée I, Tipton KF. Couée I, et al. Biochem J. 1989 Aug 1;261(3):921-5. doi: 10.1042/bj2610921. Biochem J. 1989. PMID: 2803251 Free PMC article.

• Multiple conformations in solution of the maize C₄-phosphoenolpyruvate carboxylase isozyme.

  Barreda-Huerta F, Bustos-Jaimes I, Mújica-Jiménez C, Muñoz-Clares RA. Barreda-Huerta F, et al. Heliyon. 2021 Nov 25;7(11):e08464. doi: 10.1016/j.heliyon.2021.e08464. eCollection 2021 Nov. Heliyon. 2021. PMID: 34888425 Free PMC article.

References

MeSH terms

Substances

LinkOut - more resources

• Full Text Sources

  • Europe PubMed Central
  • PubMed Central
  • Silverchair Information Systems