Target size analysis by radiation inactivation: The use of free radical scavengers

Experimental Biology and Medicine

Volumn 230, Issue 7, 2005, Pages 455-463

  Ness, Gene C ^a   Pendleton, Laura C ^a   McCreery, Michael J ^b  

^a UNIVERSITY OF SOUTH FLORIDA   (United States)

^b US ARMY MEDICAL RESEARCH INSTITUTE OF CHEMICAL DEFENSE   (United States)

Author keywords

Free radical scavengers; Functional units of proteins; Glucose 6 phosphate dehydrogenase; Glutamate dehydrogenase; Radiation inactivation analysis; Target size determinations

Indexed keywords

ASCORBIC ACID; BENZOIC ACID; CATALASE; CYSTEINE; DIAMIDE; DITHIOTHREITOL; DODECYL SULFATE SODIUM; FREE RADICAL; GLUCOSE 6 PHOSPHATE DEHYDROGENASE; GLUTAMATE DEHYDROGENASE; GLUTATHIONE; GLUTATHIONE PEROXIDASE; GLYCEROL; HYDROGEN PEROXIDE; HYDROGEN POTASSIUM ADENOSINE TRIPHOSPHATASE; MANNITOL; MERCAPTAMINE; SCAVENGER; SUPEROXIDE DISMUTASE;

ANALYTIC METHOD; ARTICLE; ENZYME ANALYSIS; IMMUNOREACTIVITY; IRRADIATION; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROTEIN ANALYSIS; PROTEIN FUNCTION; PROTEIN TARGETING; RADIATION DOSE; RADIATION EXPOSURE; SAMPLING;

EID: 21544463692     PISSN: 15353702     EISSN: None     Source Type: Journal    
DOI: 10.1177/153537020523000703     Document Type: Article

References (43)

1. Kempner ES, Schlegel W. Size determination of enzymes by radiation inactivation. Anal Biochem 92:2-10, 1979.
2. Kempner ES, Miller JH, McCreery MJ. Radiation target analysis of glycoproteins. Anal Biochem 156:140-146, 1986.
3. Kempner ES, Fleischer S. Radiation inactivation of membrane components and molecular mass determination by target analysis. Methods Enzymol 172:410-439, 1989.
4. Kempner ES. Advances in radiation target analysis. Anal Biochem 276:113-123, 1999.
5. Harmon JT, Nielsen TB, Kempner ES. Molecular weight determinations from radiation inactivation. Methods Enzymol 117:65-94, 1985.
6. Kempner ES. Molecular size determination of enzymes. Adv Enzymol 61:107-147, 1988.
7. Innerarity TL, Kempner ES, Hui DY, Mahley RW. Functional unit of the low density lipoprotein receptor of fibroblasts: a 100,000-dalton structure with multiple binding sites. Proc Natl Acad Sci U S A 78:4378-4382, 1981.
8. Ness GC, McCreery MJ, Sample CE, Smith M, Pendleton LC. Sulfhydryl/disulfide forms of rat liver 3-hydroxy-3-methylglutaryl coenzyme A reductase. J Biol Chem 260:16395-16399, 1985.
9. Edwards PA, Kempner ES, Lan S-F, Erickson SK. Functional size of rat hepatic 3-hydroxy-3-methylglutaryl coenzyme A reductase as determined by radiation inactivation. J Biol Chem 260:10278-10282, 1985.
10. Steer CJ, Kempner ES, Ashwell G. Molecular size of the hepatic receptor for asialoglycoproteins determined in situ by radiation inactivation. J Biol Chem 256:5851-5856, 1981.
11. Schwartz AL, Steer CJ, Kempner ES. Functional size of the human asialoglycoprotein receptor as determined by radiation inactivation. J Biol Chem 259:12025-12029, 1984.
12. Schrijen JJ, Van Groningen-Luyben WA, Nauta H, De Pont JJ, Bonting SL. Studies on (K++H+)-ATPase. Determination on the molecular size by radiation inactivation analysis. Biochim Biophys Acta 731:329-337, 1983.
13. Jensen J, Norby JG. Membrane-bound Na,K-ATPase: target size and radiation inactivation size of some of its enzymatic reactions. J Biol Chem 263:18063-18070, 1988.
14. Harmon JT, Kahn CR, Kempner ES, Johnson ML, Andreani D, De Pirro R, Lauro R, Olejsky J, Roth J, Eds. Current Views on Insulin Receptors, Serono Symposium No. 41, Academic Press, pp 37-44, 1981.
15. Ness GC, Pendleton LC, McCreery MJ. In situ determination of the functional size of hepatic 3-hydroxy-3-methylglutaryl-CoA reductase by radiation inactivation analysis. Biochim Biophys Acta 953:361-364, 1988.
16. Straka JG, Bloomer JR, Kempner ES. The functional size of ferrochelatase determined in situ by radiation inactivation. J Biol Chem 266:24637-24641, 1991.
17. Ness GC, Sukalski KA, Sample CE, Pendleton LC, McCreery MJ, Nordlie RC. Radiation inactivation analysis of rat liver microsomal glucose-6-phosphatase. J Biol Chem 264:7111-7114, 1989.
18. Hill JS, Davis RC, Yang D, Wen J, Philo JS, Poon PH, Phillips ML, Kempner ES, Wong H. Human hepatic lipase subunit structure determination. J Biol Chem 271:22931-22936, 1996.
19. Sluis-Cremer N, Kempner ES, Parniak MA. Structure-activity relationships in HIV-1 reverse transcriptase revealed by radiation target analysis. Prot Sci 12:2081-2086, 2003.
20. Boyer TD, Vessey DA, Kempner ES. Radiation inactivation of microsomal glutathione S-transferase. J Biol Chem 261:16963-16968, 1986.
21. McIntyre JO, Churchill P, Maurer A, Berenski CJ, Jung CY, Fleischer S. Target size of D-β-hydroxybutyrate dehydrogenase. J Biol Chem 258:953-959, 1983.
22. Milner HE, Beliveau R, Jarvis SM. The in situ size of the dopamine transporter is atetramer as estimated by radiation inactivation. Biochim Biophys Acta 1190:185-187, 1994.
23. Kempner ES, Miller JH. Radiation inactivation of glutamate dehydrogenase hexamer: lack of energy transfer between subunits. Science 222:586-589, 1983.
24. Pummill PE, Kempner ES, Deangelis PL. Functional molecular mass of a vertebrate hyaluronan synthase as determined by radiation inactivation analysis. J Biol Chem 276:39832-39835, 2001.
25. Bolger G, Liuzzi M, Krogsrud R, Scouten E, McCollum R, Weichner E, Kempner ES. Radiation inactivation of ribonucleotide reductase, an enzyme with a stable free radical. Biophys J 79:2155-2161, 2000.
26. Eichler DC, Solomonson LP, Barber MJ, McCreery MJ, Ness GC. Radiation inactivation analysis of enzymes. Effect of free radical scavengers on apparent target sizes. J Biol Chem 262:9433-9436, 1987.
27. Solomonson LP, McCreery MJ, Kay CJ, Barber MJ. Radiation inactivation analysis of assimilatory NADH:nitrate reductase. Apparent functional sizes of partial activities associated with intact and proteolytically modified enzyme. J Biol Chem 262:8934-8939, 1987.
28. Kempner ES. Novel predictions from radiation target analysis. Trends Biochem Sci 18:236-239, 1993.
29. Kepner GR, Macey RI. Membrane enzyme systems. Molecular size determinations by radiation inactivation. Biochim Biophys Acta 163:188-203, 1968.
30. Kempner ES, Haigler HT. The influence of low temperature on the radiation sensitivity of enzymes. J Biol Chem 257:13297-13299, 1982.
31. Kempner ES, Miller JH. Effect of environmental conditions on radiation target size analysis. Anal Biochem 216:451-455, 1994.
32. Fisher HF. L-Glutamate dehydrogenase from bovine liver. Methods Enzymol 113:16-27, 1985.
33. Ness GC, Sample CE, Smith M, Pendleton LC, Eichler DC. Characteristics of rat liver microsomal 3-hydroxy-3-methylglutaryl coenzyme A reductase. Biochem J 233:167-172, 1986.
34. Blum E, Alper T. Radiation-target molecular weights of urease and of L-glutamate dehydrogenase, and their relevance to the size of the functional subunits. Biochem J 122:677-680, 1971.
35. Moon K, Smith EL. Sequence of bovine liver glutamate dehydrogenase. VIII. Peptides produced by specific chemical cleavages; the complete sequence of the protein. J Biol Chem 248:3082-3088, 1973.
36. Hucho F, Janda M. Investigation of the quaternary structure of beef liver glutamate dehydrogenase with bifunctional reagents. Biochem Biophys Res Commun 57:1080-1088, 1974.
37. Jenkins RL, Ong RL, Parrish SW, McDaniel HG. Association-dissociation studies of bovine and rat liver glutamate dehydrogenase by high-performance liquid chromatography gel filtration. Arch Biochem Biophys 266:72-82, 1988.
38. Strambini GB, Cioni P, Puntoni A. Relationship between the conformation of glutamate dehydrogenase, the state of association of its subunits, and catalytic function. Biochemistry 28:3808-3814, 1989.
39. Le Maire M, Thauvette L, De Forresta B, Viel A, Beauregard G, Poitier M. Effects of ionizing radiation on proteins. Evidence of non-random fragmentations and a caution in the use of the method for determination of molecular mass. Biochem J 267:431-439, 1990.
40. Lidzey DG, Berovic N, Chittock RS, Beynon TD, Wharton CW, Jackson JB, Parkinson NS. A critical analysis of the use of radiation inactivation to measure the mass of protein. Radiat Res 143:181-186, 1995.
41. Biermann J, Schoonderwoerd K, Hom ML, Luthjens LH, Van den Bosch H. The native molecular size of alkyl-dihydroxyacetonephosphate synthase and dihydroxyacetonephosphate acyltransferase. Biochim Biophys Acta 1393:137-142, 1998.
42. Suarez MD, Ferguson-Miller S. Yeast and horse liver alcohol dehydrogenases: potential problems in target size analysis and evidence for a monomer active unit. Biochemistry 26:3340-3347, 1987.
43. Harman LS, Mottley C, Mason RP. Free radical metabolites of L-cysteine oxidation. J Biol Chem 259:5606-5611, 1984.