Luminescence in Clinical Analysis

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Balharry G. J. E. Nicholas D. J. D. (1971). New assay for ATP Sulphurylase using the luciferinluciferase method. Analytical Biochemistry. 40, 1–17.

Becvar J. E. Baldwin T. O. Nicoli M. Z. Hastings J. W. (1976). The flavin stoichiometry of the bacterial bioluminescence reaction. In Flavins and Flavoproteins, edited by Singer T. P. , pp. 94–100. Elsevier, Amsterdam.

Berne C. (1976). Determination of D-3-hydroxybutyrate dehydrogenase in mouse pancreatic islets with a photokinetic technique using bacterial luciferase, Enzyme, 21, 127–136.

Brolin S. E. Berne C. Isacsson U. (1972). Photokinetic assay of NADH and NADPH in microdissected tissue samples. Analytical Biochemistry, 50, 50–55.

Brolin S. E. Borglund E. Tegner L. Wettermark G. (1971). Photokinetic microassay based on dehydrogenase reactions and bacterial luciferase. Analytical Biochemistry, 42, 124–135.

Brolin S. E. Hjertén S. (1977). Microassay with the NADH-induced light reaction, technique improved by means of purified enzymes from Achromobacter fischeri. Molecular and Cellular Biochemistry. 17, 61–73.

Cantarow W. Stollar B. D. (1976). The use of bacterial luciferase and a liquid scintillation spectrometer to assay the enzymatic synthesis of NAD⁺ . Analytical Biochemistry, 71, 333–340.

Cavari B. Z. Phelps G. (1977). Sensitive enzymatic assay for glucose determination in natural waters. Applied and Environmental Microbiology, 33, 1237–1243.

Chappelle E. W. Levin G. V. (1968). Use of the firefly bioluminescense reaction for rapid detection and counting of bacteria. Biochemical Medicine, 2, 41–52.

Chappelle E. W. Picciolo G. L. Altland R. H. (1967). A sensitive assay for flavin mononucleotide using the bacterial bioluminescence reaction. Biochemical Medicine, 1, 252–260.

Denburg J. L. McElroy W. D. (1970). Anion inhibition of firefly luciferase. Archives of Biochemistry and Biophysics, 141, 668–675.

DeLuca M. (1969). Hydrophobic nature of the active site of firefly luciferase, Biochemistry, 8, 160–166.

DeLuca M. (1976). Firefly luciferase. In Advances in Enzymology, edited by Meister A. , volume 44, pp. 37–68. Interscience Publishers, New York.

Duane W. Hastings J. W. (1975). Flavin mononucleotide reductase of luminous bacteria. Molecular and Cellular Biochemistry, 6, 53–64.

Gibson Q. H. Hastings J. W. (1962). The oxidation of reduced flavin mononucleotide by molecular oxygen. Biochemical Journal, 83, 368–377.

Gilles R. Pequeux A. Saive J. J. Spronck A. C. Thome-Lentz G. (1976). Effect of various ions on ATP determinations using the “luciferine-luciferase” system. Archives Internationales de Physique et de Biochimie, 84, 807–817.

Goto T. Kubota J. Suzuki N. Kishi Y. (1973). In Chemiluminescence and Bioluminescence, edited by Cormier M. J. Hercules D. M. Lee J. , pp. 325–331. Plenum Press, New York.

Gunsalus-Miguel A. Meighen E. A. Nicoli M. Z. Nealson K. H. Hastings J. W. (1972). Purification and properties of bacterial luciferases. Journal of Biological Chemistry, 247, 398–404.

Haggerty C. Jablonski E. Stav L. DeLuca M. (1978). Continuous monitoring of reactions that produce NADH and NADPH using immobilized luciferase and oxidoreductases from Beneckea harveyi Analytical Biochemistry, 88, 162–173.

Hammar H. (1973). NAD and NADP dependent isocitrate dehydrogenase and fumarate hydratase activities in normal human skin and in some maculosquamous diseases of the skin. Archiv für Dermotologische Forschung, 247, 295–308.

Hammar H. Wettermark G. Wladimiroff W. (1975). Bioluminescence assay of enzymes obtained from buccal epithelium by superficial scraping. Scandinavian Journal of Dental Research, 83, 375–381.

Hastings J. W. Nealson K. H. (1977). Bacterial bioluminescence. Annual Review of Microbiology, 31, 549–595.

Hastings J. W. Balny C. Le Peuch C. Doujou P. (1973). Spectral properties of an oxygenated luciferase-flavin intermediate isolated by low-temperature chromatography. Proceedings of the National Academy of Sciences of the United States of America, 70, 3468–3472.

Hastings J. W. Riley W. H. Massa J. (1965). The purification, properties, and chemiluminescent quantum yield of bacterial luciferase. Journal of Biological Chemistry, 240, 1473–1481.

Hastings J. W. Spudich J. Malnic G. (1963). The influence of aldehyde chain length upon the relative quantum yield of the bioluminescent reaction of Achromobacter fischeri Journal of Biological Chemistry, 238, 3100–3105.

Hastings J. W. Weber K. Friedland J. Eberhard A. Mitchell G. W. Gunsalus A. (1969). Structurally distinct bacterial luciferases. Biochemistry, 8, 4681–4689.

Jablonski E. DeLuca M. (1976). Immobilization of bacterial luciferase and FMN reductase on glass rods. Proceedings of the National Academy of Sciences of the United States of America, 73, 3848–3851.

Jablonski E. DeLuca M. (1977). Purification and properties of the NADH and NADPH specific FMN oxidoreductases from Beneckea harveyi Biochemistry, 16, 2932–2936.

Jablonski E. DeLuca M. (1978). Studies of the control of luminescence in Beneckea harveyi: Properties of the NADH and NADPH:FMN oxidoreductases. Biochemistry, 17, 672–678.

Johnson R. A. Hardman J-G. Broadus A. E. Sutherland E. W. (1970). Analysis of adenosine 3′,5′-monophosphate with luciferase luminescence. Analytical Biochemistry, 35, 91–97.

Larsson C. M. Olsson T. (1979). Firefly assay of adenine nucleotides from algae: Comparison of extraction methods. Plant and Cell Physiology, 20, 145–155.

Lee J. (1972). Bacterial bioluminescence. Quantum yields and stoichiometry of the reactants reduced flavin mononucleotide, dodecanal and oxygen, and of a product hydrogen peroxide. Biochemistry, 11, 3350–3359.

Lee Y. Jablonski I. DeLuca M. (1977). Immobilization of firefly luciferase on glass rods: Properties of the immobilized enzyme. Analytical Biochemistry, 80, 496–501.

Lee J. Murphy C. L. Faini G. J. Baucom T. L. (1974). Bacterial bioluminescence and its application to analytical procedures. In Liquid Scintillation Counting, Recent Developments, edited by Stanley P. E. Scoggins B. A. , pp.403–420, Academic Press, New York.

Lemasters J. J. Hackenbrock C. R. (1973). Adenosine triphosphate: Continuous measurement in mitochondrial suspensions by firefly luciferase luminescence. Biochemical and Biophysical Research Communications, 55, 1262–1270.

Lundin A. Rickardsson A. Thore A. (1976). Continuous monitoring of ATP converting reactions by purified firefly luciferase. Analytical Biochemistry, 75, 611–620.

Lundin A. Rickardsson A. Thore A. (1977a). Substrate and enzyme determinations by continuously monitoring the ATP level by a purified luciferase reagent. In Proceedings, 2nd Bi-Annual ATP Methodology Symposium, SAI Technology Company, San Diego.

Lundin A. Styrelius I. (1978). Sensitive assay of creatine kinase isoenzymes in human serum using M subunit inhibiting antibody and firefly luciferase. Clinica Chimica Acta, 87, 199–209.

Lundin A. Thore A. (1975a). Analytical information obtainable by evaluation of the time course of firefly bioluminescence in the assay of ATP. Analytical Biochemistry, 66, 47–63.

Lundin A. Thore A. (1975b). Comparison of methods for extraction of bacterial adenine nucleotides determined by firefly assay. Applied Microbiology, 30, 713–721.

Lundin A. Thore A. Baltscheffsky M. (1977b). Sensitive measurement of flash induced photophosphorylation in bacterial chromatophores by firefly luciferase. FEBS letters, 79, 73–76.

Manandhar M. S. P. Van Dyke K. (1974a). Guanosine triphosphate analysis: PEI thin layer purification and luciferine-luciferase liquid scintillation quantitation. Analytical Biochemistry, 60, 122–129.

Manandhar M. S. P. Van Dyke K. (1974b). Adenosine tetraphosphate analysis: Polyethyleneimine (PEI) thin layer purification and firefly-extract liquid scintillation counting. Analytical Biochemistry, 58, 368–375.

McCapra F. Hysert D. W. (1973). Bacterial bioluminescence—identification of fatty acid as product, its quantum yield and suggested mechanism. Biochemical and Biophysical Research Communications, 52, 298–304.

McCoy G. D. Doeg K. A. (1975). A simplified assay of phosphoenolpyruvate. Analytical Biochemistry, 64, 115–120.

McElroy W. D. (1947). The energy source for bioluminescence in an isolated system. Proceedings of the National Academy of Sciences of the United States of America, 33, 342–345.

McElroy W. D. Seliger H. H. White E. H. (1969). Mechanism of bioluminescence, chemiluminescence and enzyme function in the oxidation of firefly luciferin, Photochemistry and Photobiology, 10, 153–170.

Meighen E. A. Hastings J. W. (1971). Binding site determination data: Reduced flavin mononucleotide binding to bacterial luciferase. Journal of Biological Chemistry, 246, 7666–7674.

Michaliszyn G. A. Wing S. S. Meighen E. A. (1977). Purification and properties of a NAD(P)H: flavin oxidoreductase from the luminous bacterium, Beneckea harveyi. Journal of Biological Chemistry, 252, 7495–7499.

Momsen G. (1977). Determination of 1,3-diphosphoglycerate and other intermediates in the human red blood cells by firefly luciferase method. Analytical Biochemistry, 82, 493–502.

Nicholas D. J. D. Clarke G. R. (1971). Bioluminescent method for determing micro quantities of ammonia in a liquid scintillation spectrometer. Analytical Biochemistry, 42, 560–568.

Nicoli M. Z. Baldwin T. O. Becvar J. E. Hastings J. W. (1976). The interaction of oxidized flavin mononucleotide with bacterial luciferase. In Flavins and Flavoproteins, edited by Singer T. P. , pp. 87–93. Elsevier, Amsterdam.

Nicoli M. Z. Baldwin T. O. Hastings J. W. (1974a). Binding of flavin mononucleotide to bacterial luciferase. Federation Proceedings, 33, 1589.

Nicoli M. Z. Hastings J. W. (1974). Bacterial luciferase: The hydrophobic environment of the reactive sulfhydryl. Journal of Biological Chemistry, 249, 2393–2396.

Nicoli M. Z. Meighen E. A. Hastings J. W. (1974b). Bacterial luciferase: Chemistry of the reactive sulfhydryl. Journal of Biological Chemistry, 249, 2385–2392.

Nielsen R. Rasmussen H. (1968). Fractionation of extracts of firefly tails by gel filtration. Acta Chemica Scandinaviva, 22, 1757–1762.

Nilsson L. Höjer H. Ånséhn S. Thore A. (1977). A rapid, semiautomatic assay of gentamicin based on luciferase assay of bacterial adenosine triphosphate. Scandinavian Journal of Infectious Disease, 9, 232–236.

Njus D. Baldwin T. O. Hastings J. W. (1974). A sensitive assay for proteolytic enzymes using bacterial luciferase as a substrate. Analytical Biochemistry, 61, 280–287.

Olsson T. Thore A. Carlsson H. E. Brunius G. Eriksson G. (1979). Quantitation of immunological reactions by luminescence, In Proceedings from the International Symposium on Analytical Applications of Chemiluminescence and Bioluminescence, edited by Stanley P. E. Schram E. (In press). Brussels.

Pradet A. (1967). Etude des adénosine-5′-mono, di et tri-phosphates dans les tissus végétaux I. Dosage enzymatique. Physiologie Végétaux, 5, 209–221.

Seitz W. R. Neary M. P. (1976). Recent advances in bioluminescence and chemiluminescence assay. In Methods of Biochemical Analysis, edited by Glick D. , volume 23, pp. 161–188, Wiley Interscience Publishers, New York.

Seliger H. H. McElroy W. D. (1960). Spectral emission and quantum yield of firefly bioluminescence. Archives of Biochemistry and Biophysics, 88, 136–145.

Shimomura O. Johnson F. H. Kohama Y. (1972). Reactions involved in bioluminescence systems of limpet (Latia neritoides) and luminous bacteria. Proceedings of the National Academy of Sciences of the United States of America, 69, 2086–2089.

Stanley P. E. (1971). Determination of subpicomole levels of NADH and FMN using bacterial luciferase and the liquid scintillation spectrometer. Analytical Biochemistry, 39, 441–453.

Stanley P. E. (1974a). Use of bioluminescence procedures and liquid scintillation spectrometers for measuring very small amounts of enzymes and metabolites. In Liquid Scintillation Counting, Recent Developments, edited by Stanley P. E. Scoggins B. A. , pp. 421–430. Academic Press, New York and London.

Stanley P. E. (1974b). Analytical bioluminescence assays using the liquid scintillation spectrometer: a review. In Liquid Scintillation Counting, edited by Crook M. A. Johnson P. , vol 3, pp. 253–272, Heyden, London.

Strehler B. L. (1953). Luminescence in cell-free extracts of luminous bacteria and its activation by DPN. Journal of the American Chemical Society, 75, 1264.

Strehler B. L. (1974). Bioluminescence assay: Principles and practice. In Methods of Biochemical Analysis, edited by Glick D. , volume 16, pp.99–181. Interscience Publishers, New York.

Strehler B. L. Cormier M. J. (1953). Factors affecting the luminescence of cell-free extracts of the luminous bacterium, Achromobacter fisheri. Archives of Biochemistry and Biophysics, 47, 16–33.

Strehler B. L. Totter J. R. (1952). Firefly luminescence in the study of energy transfer mechanisms. I. Substrate and enzyme determination. Archives of Biochemistry and Biophysics, 40, 28–41.

Thore A. Ånséhn S. Lundin A. Bergman S. (1975). Detection of bacteriuria by luciferase assay of adenosine triphosphate. Journal of Clinical Microbiology, 1, 1–8.

Travis J. McElroy W. D. (1966). Isolation and sequence of an essential sulfhydryl peptide at the active site of firefly luciferase. Biochemistry, 5, 2170–2176.

Watanabe T. Nakamura T. (1972). Studies on luciferase from Photobacterium phosphoreum II. Substrate specificity and stoichiometry of the reaction in vitro Journal of Biochemistry, 72, 647–653.