View Item 

Show simple item record

The Interaction Of Acrylamide With Glyceraldehyde‐3‐Phosphate Dehydrogenase. Structural Modifications In The Enzyme Studied By Fluorescence Techniques

dc.contributor.authorÖrstan, Aydin
dc.contributor.authorGafni, Ari
dc.date.accessioned2018-03-07T18:25:28Z
dc.date.available2018-03-07T18:25:28Z
dc.date.issued1990-06
dc.identifier.citationÖrstan, Aydin ; Gafni, Ari (1990). "The Interaction Of Acrylamide With Glyceraldehyde‐3‐Phosphate Dehydrogenase. Structural Modifications In The Enzyme Studied By Fluorescence Techniques." Photochemistry and Photobiology 51(6): 725-731.
dc.identifier.issn0031-8655
dc.identifier.issn1751-1097
dc.identifier.urihttps://hdl.handle.net/2027.42/142516
dc.publisherWiley
dc.titleThe Interaction Of Acrylamide With Glyceraldehyde‐3‐Phosphate Dehydrogenase. Structural Modifications In The Enzyme Studied By Fluorescence Techniques
dc.typeArticleen_US
dc.rights.robotsIndexNoFollow
dc.subject.hlbsecondlevelChemistry
dc.subject.hlbtoplevelScience
dc.description.peerreviewedPeer Reviewed
dc.contributor.affiliationumDepartment of Biological Chemistry, The University of Michigan 300 N. Ingalls, Ann Arbor, MI 48109-2007, USA
dc.contributor.affiliationumInstitute of Gerontology, The University of Michigan 300 N. Ingalls, Ann Arbor, MI 48109-2007, USA
dc.description.bitstreamurlhttps://deepblue.lib.umich.edu/bitstream/2027.42/142516/1/php1990516725.pdf
dc.identifier.doi10.1111/php.1990.51.6.725
dc.identifier.sourcePhotochemistry and Photobiology
dc.identifier.citedreferenceParker, C. A. ( 1968 ) Photoluminescence of Solutions, pp. 19 â 20. Elsevier, New York.
dc.identifier.citedreferenceHarris, J. I. and M. Waters ( 1976 ) Glyceraldehyde-3-phosphate dehydrogenase. In The Enzymes (Edited by P. D. Boyer ). Vol. 8, part C, pp. 1 â 49. Academic Press, New York.
dc.identifier.citedreferenceHarrison, R. A. P. ( 1974 ) The detection of hexokinase, glucosephosphate isomerase and phosphoglucomutase activities in polyacrylamide gels after electrophoresis: a novel method using immobilized glucose 6-phosphate dehydrogenase. Anal. Biochem. 61, 500 â 507.
dc.identifier.citedreferenceHenis, Y. I., A. Levitzki and A. Gafni ( 1979 ) Evidence for ligand-induced conformational changes in rabbit muscle glyceraldehyde-3-phosphate dehydrogenase. Eur. J. Biochem. 97, 519 â 528.
dc.identifier.citedreferenceHowland, R. D., I. L. Vyas, H. E. Lowndes and T. M. Argentieri ( 1980 ) The etiology of toxic peripheral neuropathies: in vitro effects of acrylamide and 2.5-hexanedione on brain enolase and other glycolytic enzymes. Brain Res. 202, 131 â 142.
dc.identifier.citedreferenceHumphreys, L., S. Reid and C. Masters ( 1986 ) Studies on the topographical localization of the binding sites for substrate and for actin on the enzymes, glyceraldehyde-3-phosphate dehydrogenase and phosphofructokinase. Int. J. Biochem. 18, 445 â 451.
dc.identifier.citedreferenceLakowicz, J. R. ( 1983 ) Principles of Fluorescence Spectroscopy, pp. 111 â 131. Plenum Press, New York.
dc.identifier.citedreferenceMiller, M. S. and P. S. Spencer ( 1985 ) The mechanisms of acrylamide axonopathy. Ann. Rev. Pharmacol. Toxicol. 25, 643 â 666.
dc.identifier.citedreferenceMuronetz, V. I., T. O. Golovina and N. K. Nagradova ( 1976 ) Rat skeletal muscle glyceraldehyde-3-phosphate dehydrogenase: adenine nucleotide-induced inactivation. Arch. Biochem. Biophys. 177, 16 â 23.
dc.identifier.citedreferenceNgo, T. T. ( 1976 ) Properties of water-insoluble solid supported electric eel acetylcholinesterase. Int. J. Biochem. 7, 193 â 198.
dc.identifier.citedreferenceSabri, M. I. ( 1983 ) In vitro and in vivo inhibition of glycolytic enzymes by acrylamide. Neurochem. Pathol. 1, 179 â 191.
dc.identifier.citedreferenceScheek, R. M., J. A. Berden, R. Hooghiemstra and E. C. Slater ( 1979 ) Subunit interactions in rabbit muscle glyceraldehyde-3-phosphate dehydrogenase, as measured by NAD and NADH binding. Biochim. Biophys. Acta 569, 124 â 134.
dc.identifier.citedreferenceScheek, R. M. and E. C. Slater ( 1982 ) Glyceraldehyde-3-phosphate dehydrogenase from rabbit muscle. Meth. Enzymol. 89, 305 â 309.
dc.identifier.citedreferenceSignorini, M., F. Dallocchio and C. M. Bergamini ( 1988 ) Inhibition of activity and quenching of intrinsic fluorescence of transglutaminase by acrylamide are independent events. Biochim. Biophys. Acta 957, 168 â 171.
dc.identifier.citedreferenceVelick, S. F. ( 1958 ) Fluorescence spectra and polarization of glyceraldehyde-3-phosphate and lactic dehydrogenase coenzyme complexes. J. Biol. Chem. 233, 1455 â 1467.
dc.identifier.citedreferenceWoronick, C. L. ( 1961 ) Inhibition of liver alcohol dehydrogenase by amides. Acta Chem. Scand. 15, 2062 â 2064.
dc.identifier.citedreferenceAustin, J. C., C. W. Wharton and R. E. Hester ( 1989 ). An ultraviolet resonance raman study of dehydrogenase enzymes and their interactions with coenzymes and substrates. Biochemistry 28, 1533 â 1538.
dc.identifier.citedreferenceBlatt, E., A. Husain and W. H. Sawyer ( 1986 ) The association of acrylamide with proteins. The interpretation of fluorescence quenching experiments. Biochim. Biophys. Acta 871, 6 â 13.
dc.identifier.citedreferenceEckert, B. S. ( 1985 ) Alteration of intermediate filament distribution in PtK 1 cells by acrylamide. Eur. J. Cell Biol. 37, 169 â 174.
dc.identifier.citedreferenceEftink, M. R. and C. A. Ghiron ( 1981 ) Fluorescence quenching studies with proteins. Anal. Biochem. 114, 199 â 227.
dc.identifier.citedreferenceEftink, M. R. and C. A. Ghiron ( 1987 ) Does the fluorescence quencher acrylamide bind to proteins? Biochim. Biophys. Acta 916, 343 â 349.
dc.identifier.citedreferenceEftink, M. R., T. J. Selva and Z. Wasylewski ( 1987 ) Studies of the effficiency and mechanism of fluorescence quenching reactions using acrylamide and succinimide as quenchers. Photochem. Photobiol. 46, 23 â 30.
dc.identifier.citedreferenceEftink, M. R. and L. A. Selvidge ( 1982 ) Fluorescence quenching of liver alcohol dehydrogenase by acrylamide. Biochemistry 21, 117 â 125.
dc.identifier.citedreferenceEllman, G. L. ( 1959 ) Tissue sulfhydryl groups. Arch. Biochem. Biophys. 82, 70 â 77.
dc.identifier.citedreferenceFox, J. B. and W. B. Dandliker ( 1956 ) The coenzyme content of rabbit muscle glyceraldehyde-3-phosphate dehydrogenase. J. Biol. Chem. 221, 1005 â 1017.
dc.identifier.citedreferenceFrost, A. A. and R. G. Pearson ( 1961 ) Kinetics and Mechanism, p. 186. Wiley, New York.
dc.owningcollnameInterdisciplinary and Peer-Reviewed


Files in this item

Name:
php1990516725.pdf
Size:
1.123MB
Format:
PDF
View/Open

Show simple item record

Remediation of Harmful Language

The University of Michigan Library aims to describe library materials in a way that respects the people and communities who create, use, and are represented in our collections. Report harmful or offensive language in catalog records, finding aids, or elsewhere in our collections anonymously through our metadata feedback form. More information at Remediation of Harmful Language.

Accessibility

If you are unable to use this file in its current format, please select the Contact Us link and we can modify it to make it more accessible to you.