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Journal articles on the topic 'Clinical enzymology'

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Published: 4 June 2021
Last updated: 26 July 2024

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1

Werner, Mario. "Hellenic Society for Clinical Enzymology." Enzyme 46, no. 4-5 (1992): 272. http://dx.doi.org/10.1159/000468799.

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2

Scheindlin, S. "CLINICAL ENZYMOLOGY: Enzymes As Medicine." Molecular Interventions 7, no. 1 (February 1, 2007): 4–8. http://dx.doi.org/10.1124/mi.7.1.1.

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3

Goldberg, David M. "Clinical enzymology: An autobiographical history." Clinica Chimica Acta 357, no. 2 (July 2005): 93–112. http://dx.doi.org/10.1016/j.cccn.2005.03.016.

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4

Goldberg, David M. "reso8th International Congress of Clinical Enzymology." Enzyme 45, no. 1-2 (1991): 92–96. http://dx.doi.org/10.1159/000468871.

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5

Rosalki, S. "Clinical Enzymology. A Case-Oriented Approach." Journal of Clinical Pathology 41, no. 1 (January 1, 1988): 119. http://dx.doi.org/10.1136/jcp.41.1.119-d.

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6

Dennis, P. M. "Clinical Enzymology — A Case Oriented Approach." Pathology 19, no. 4 (1987): 435. http://dx.doi.org/10.3109/00313028709103899.

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7

Tipton, K. F. "Enzymology of monoamine oxidase." Cell Biochemistry and Function 4, no. 2 (April 1986): 79–87. http://dx.doi.org/10.1002/cbf.290040202.

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8

Moss, Donald W. "The place of reference materials in clinical enzymology." Clinica Chimica Acta 173, no. 1 (March 1988): 1–7. http://dx.doi.org/10.1016/0009-8981(88)90351-8.

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9

Goldberg, David M., and Lauro Galzigna. "Newsletters of the international society for clinical enzymology." Clinica Chimica Acta 175, no. 1 (June 1988): S1—S9. http://dx.doi.org/10.1016/0009-8981(88)90048-4.

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10

Goldberg, David M. "The enzymology of intestinal disease." Clinical Biochemistry 20, no. 2 (April 1987): 63–72. http://dx.doi.org/10.1016/s0009-9120(87)80101-7.

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11

Davies, Dai T. "Enzymology in Preclinical Safety Evaluation." Toxicologic Pathology 20, no. 3-2 (May 1992): 501–5. http://dx.doi.org/10.1177/0192623392020003207.

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This short paper will briefly discuss the merits of determining plasma enzyme activities in pre-clinical safety evaluation. Emphasis is placed on the value of selecting the appropriate enzymes and collecting blood samples at the appropriate times during the study, so as to gain the maximum amount of diagnostic information. Examples of actual results will be cited to illustrate some of the points. These examples are drawn from the 2 commonly used toxicology species—the laboratory white rat and the beagle—and serve to demonstrate the importance of enzymology in monitoring the progress or resolution of an adverse drug effect.
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12

Cerny, Matthew A. "SC2.3 - Enzymology and clinical importance of reductases and hydrolases." Drug Metabolism and Pharmacokinetics 35, no. 1 (2020): S2. http://dx.doi.org/10.1016/j.dmpk.2020.04.275.

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13

Rothman, J. E. "Enzymology of intracellular membrane fusion." Klinische Wochenschrift 69, no. 3 (February 1991): 98–104. http://dx.doi.org/10.1007/bf01795952.

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14

Xie, Sunney. "Single-Molecule Approach to Enzymology." Single Molecules 2, no. 4 (December 2001): 229–36. http://dx.doi.org/10.1002/1438-5171(200112)2:4<229::aid-simo229>3.0.co;2-9.

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15

Stansbie, D. "Book Review: A Practical Guide to Enzymology." Annals of Clinical Biochemistry: International Journal of Laboratory Medicine 25, no. 3 (May 1988): 332. http://dx.doi.org/10.1177/000456328802500326.

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16

Martinek, Karel, Iliya V. Berezin, Yurii L. Khmelnitski, Natalya L. Klyachko, and Andrei V. Levashov. "Micellar enzymology: Potentialities in applied areas (biotechnology)." Collection of Czechoslovak Chemical Communications 52, no. 10 (1987): 2589–602. http://dx.doi.org/10.1135/cccc19872589.

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Micellar enzymology, a new trend in molecular biology, studies the catalysis by enzymes entrapped into hydrated reversed micelles of surfactants (detergents, phospholipids) in organic solvents. The effect of solubilization on enzymatic properties is briefly considered. Applications of such biocatalytic systems in fine organic syntheses, in clinical and chemical analyses, and in medicine, as well as probable future trends in biotechnology are discussed.
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17

Theodorsen, L. "Dry Reagent Technology. Kodak Ektachem 700 XR in Clinical Enzymology." Scandinavian Journal of Clinical and Laboratory Investigation 53, sup215 (January 1993): 101–11. http://dx.doi.org/10.3109/00365519309090702.

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18

Braun, J. P., M. Aktas, H. Lefebvre, A. G. Rico, and P. L. Toutain. "Clinical enzymology for the assessment of organ damage: Interspecific differences." Comparative Haematology International 3, no. 1 (March 1993): 27–32. http://dx.doi.org/10.1007/bf00394924.

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19

Alvarez-Gonzalez, Rafael, Gustavo Pacheco-Rodriguez, and Hilda Mendoza-Alvarez. "Enzymology of ADP-ribose polymer synthesis." Molecular and Cellular Biochemistry 138, no. 1-2 (1994): 33–37. http://dx.doi.org/10.1007/bf00928440.

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20

Tang, Wei. "The Metabolism of Diclofenac - Enzymology and Toxicology Perspectives." Current Drug Metabolism 4, no. 4 (August 1, 2003): 319–29. http://dx.doi.org/10.2174/1389200033489398.

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21

Ramsay, Rona R., and Alen Albreht. "Questions in the Chemical Enzymology of MAO." Chemistry 3, no. 3 (August 31, 2021): 959–78. http://dx.doi.org/10.3390/chemistry3030069.

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We have structure, a wealth of kinetic data, thousands of chemical ligands and clinical information for the effects of a range of drugs on monoamine oxidase activity in vivo. We have comparative information from various species and mutations on kinetics and effects of inhibition. Nevertheless, there are what seem like simple questions still to be answered. This article presents a brief summary of existing experimental evidence the background and poses questions that remain intriguing for chemists and biochemists researching the chemical enzymology of and drug design for monoamine oxidases (FAD-containing EC 4.1.3.4).
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22

Kabil, Omer, and Ruma Banerjee. "Enzymology of H2S Biogenesis, Decay and Signaling." Antioxidants & Redox Signaling 20, no. 5 (February 10, 2014): 770–82. http://dx.doi.org/10.1089/ars.2013.5339.

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23

Kuenzle, Clive C. "Enzymology of DNA replication and repair in the brain." Brain Research Reviews 10, no. 3 (December 1985): 231–45. http://dx.doi.org/10.1016/0165-0173(85)90026-8.

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24

Goldberg, David M. "International Society for Enzymology (ISE) Newsletter, August 2006." Clinica Chimica Acta 375, no. 1-2 (January 2007): 175–78. http://dx.doi.org/10.1016/j.cca.2006.08.015.

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25

Goldberg, David. "International Society for Enzymology (ISE), Newsletter, December 2006." Clinica Chimica Acta 379, no. 1-2 (April 2007): 176–78. http://dx.doi.org/10.1016/j.cca.2006.12.030.

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26

Goldberg, David M. "International Society for Enzymology (ISE), Newsletter, August 2005." Clinica Chimica Acta 362, no. 1-2 (December 2005): S15—S22. http://dx.doi.org/10.1016/j.cccn.2005.07.012.

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27

Moss, D. W. "Enzyme reference materials: Their place in diagnostic enzymology." Clinica Chimica Acta 225, no. 1 (February 1994): S5—S11. http://dx.doi.org/10.1016/0009-8981(94)90033-7.

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28

Goldberg, David M. "International Society for Enzymology (ISE), Newsletter, February 2005." Clinica Chimica Acta 357, no. 1 (July 2005): S1—S10. http://dx.doi.org/10.1016/j.cccn.2005.02.005.

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29

Kim, Keun IL, Sung Hee Baek, and Chin Ha Chung. "Versatile protein tag, SUMO: Its enzymology and biological function." Journal of Cellular Physiology 191, no. 3 (May 9, 2002): 257–68. http://dx.doi.org/10.1002/jcp.10100.

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30

Nishonov, Abdumalik A., Xiaohui Ma, and Vasu Nair. "Azadideoxyadenosine: Synthesis, enzymology, and anti-HIV activity." Bioorganic & Medicinal Chemistry Letters 16, no. 15 (August 2006): 4099–101. http://dx.doi.org/10.1016/j.bmcl.2006.04.085.

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31

Hermann, Lucas, Christopher-Nils Mais, Laura Czech, Sander H. J. Smits, Gert Bange, and Erhard Bremer. "The ups and downs of ectoine: structural enzymology of a major microbial stress protectant and versatile nutrient." Biological Chemistry 401, no. 12 (November 26, 2020): 1443–68. http://dx.doi.org/10.1515/hsz-2020-0223.

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AbstractEctoine and its derivative 5-hydroxyectoine are compatible solutes and chemical chaperones widely synthesized by Bacteria and some Archaea as cytoprotectants during osmotic stress and high- or low-growth temperature extremes. The function-preserving attributes of ectoines led to numerous biotechnological and biomedical applications and fostered the development of an industrial scale production process. Synthesis of ectoines requires the expenditure of considerable energetic and biosynthetic resources. Hence, microorganisms have developed ways to exploit ectoines as nutrients when they are no longer needed as stress protectants. Here, we summarize our current knowledge on the phylogenomic distribution of ectoine producing and consuming microorganisms. We emphasize the structural enzymology of the pathways underlying ectoine biosynthesis and consumption, an understanding that has been achieved only recently. The synthesis and degradation pathways critically differ in the isomeric form of the key metabolite N-acetyldiaminobutyric acid (ADABA). γ-ADABA serves as preferred substrate for the ectoine synthase, while the α-ADABA isomer is produced by the ectoine hydrolase as an intermediate in catabolism. It can serve as internal inducer for the genetic control of ectoine catabolic genes via the GabR/MocR-type regulator EnuR. Our review highlights the importance of structural enzymology to inspire the mechanistic understanding of metabolic networks at the biological scale.
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32

Xu, Shu, and Dengshun Tao. "Leptin Alleviates Inflammatory Response in Myocardial Ischemia Reperfusion Injury." Disease Markers 2022 (March 9, 2022): 1–6. http://dx.doi.org/10.1155/2022/8707061.

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Objective. To investigate the role of leptin in regulating cell inflammation and protecting myocardium after myocardial ischemia-reperfusion injury in rats through signaling pathway at tissue and molecular protein levels. Methods. Healthy female SD rats were randomly divided into 4 groups, which were sham, I/R group, leptin low-dose intervention group, and high-dose intervention group (40 μg/kg and 80 μg/kg, respectively). Cardiac hemodynamics, myocardial enzymology, inflammatory indices, and pathological changes were observed. Western blot was used to observe the expression of PI3K, AKT, and NFκB protein by leptin. Results. Leptin can improve the hemodynamics of cardiac ischemia-reperfusion rats, improve the expression of myocardial enzymology, reduce the release of cardiac and serum inflammatory factors, increased PI3k, AKT, and NFκB expression, and reduce the occurrence of inflammation from the perspective of gross pathology, thus protecting the body. Conclusion. Leptin pretreatment can reduce MIRI injury, and the protective mechanism may be that leptin upregulates PI3K-AKT-NFκB expression in myocardial tissue to reduce inflammation and promote repair of I/R injury.
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33

Wolf, Paul L. "History of diagnostic enzymology: A review of significant investigations." Clinica Chimica Acta 369, no. 2 (July 2006): 144–47. http://dx.doi.org/10.1016/j.cca.2006.02.043.

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34

Ulusu, Nuriye Nuray. "Curious Cases of the Enzymes / Neobiča Istorija Enzima." Journal of Medical Biochemistry 34, no. 3 (July 1, 2015): 271–81. http://dx.doi.org/10.2478/jomb-2014-0045.

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SummaryLife as we know it heavily relies on biological catalysis, in fact, in a very nonromantic version of it, life could be considered as a series of chemical reactions, regulated by the guarding principles of thermodynamics. In ancient times, a beating heart was a good sign of vitality, however, to me, it is actually the presence of active enzymes that counts… Though we do not usually pay attention, the history of enzymology is as old as humanity itself, and dates back to the ancient times. This paper is dedicated to these early moments of this remarkable science that touched our lives in the past and will make life a lot more efficient for humanity in the future. There was almost always a delicate, fundamentally essential relationship between mankind and the enzymes. Challenged by a very alien and hostile Nature full of predators, prehistoric men soon discovered the medicinal properties of the plants, through trial and error. In fact, they accidently discovered the enzyme inhibitors and thus, in crude terms, kindled a sparkling area of research. These plant-derivatives that acted as enzyme inhibitors helped prehistoric men in their pursuit of survival and protection from predators; in hunting and fishing… Later in history, while the underlying purposes of survival and increasing the quality of life stayed intact, the ways and means of enzymology experienced a massive transformation, as the ‘trial and error’ methodology of the ancients is now replaced with rational scientific theories.
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35

Khan, Wahab A., Rachael E. Barney, and Gregory J. Tsongalis. "CRISPR-cas13 enzymology rapidly detects SARS-CoV-2 fragments in a clinical setting." Journal of Clinical Virology 145 (December 2021): 105019. http://dx.doi.org/10.1016/j.jcv.2021.105019.

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36

James, D. R. "Book Review: Plasma Isoenzymes: The Current Status. Advances in Clinical Enzymology, Volume 3." Annals of Clinical Biochemistry: International Journal of Laboratory Medicine 24, no. 3 (May 1987): 325. http://dx.doi.org/10.1177/000456328702400316.

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37

Vetting, M., S. L. Roderick, S. Hegde, S. Magnet, and J. S. Blanchard. "What can structure tell us about in vivo function? The case of aminoglycoside-resistance genes." Biochemical Society Transactions 31, no. 3 (June 1, 2003): 520–22. http://dx.doi.org/10.1042/bst0310520.

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Resistance to antibiotics used in the treatment of bacterial infections is an expanding clinical problem. Aminoglycosides, one of the oldest classes of natural product antibiotics, exert their bactericidal effect as the result of inhibiting bacterial protein synthesis by binding to the acceptor site of the 30 S ribosomal subunit. The most common mechanism of clinical resistance to aminoglycosides results from the expression of enzymes that covalently modify the aminoglycoside. We will discuss the enzymology and structure of two representative chromosomally encoded aminoglycoside N-acetyltransferases, Mycobacterium tuberculosis AAC(2´)-Ic and Salmonella enterica AAC(6´)-Iy, and speculate about their possible physiological function and substrates.
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38

Povsic, Thomas, Mauricio Cohen, Christopher Rusconi, Bruce Sullenger, and Richard Becker. "Nucleic acid aptamers as antithrombotic agents: Opportunities in extracellular therapeutics." Thrombosis and Haemostasis 103, no. 03 (2010): 586–95. http://dx.doi.org/10.1160/th09-10-0716.

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SummaryAntithrombotic therapy for the acute management of thrombotic disorders has been stimulated and guided actively by our current understanding of platelet biology, coagulation proteases, and vascular science. A translatable platform for coagulation, based soundly on biochemistry, enzymology and cellular events on platelets and tissue factor-baring cells, introduces fundamental constructs, mechanistic clarity, and an unparalleled opportunity for accelerating the development and clinical investigation of both disease- and patient-specific therapies. In the current review, we build upon and expand substantially our observations surrounding nucleic acids as antithrombotic agents.
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39

Gerhardt, W. "Will implementation of ICES delay method standardization in clinical enzymology? Scandinavian Committee on Enzymes." Clinical Chemistry 31, no. 2 (February 1, 1985): 342–44. http://dx.doi.org/10.1093/clinchem/31.2.342.

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40

Férard, Georges, John Edwards, Takashi Kanno, Jean-Marc Lessinger, Donald W. Moss, Françoise Schiele, Norbert W. Tietz, and Anne Vassault. "Interassay calibration as a major contribution to the comparability of results in clinical enzymology." Clinical Biochemistry 31, no. 6 (August 1998): 489–94. http://dx.doi.org/10.1016/s0009-9120(98)00038-1.

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41

Bowers, G. N., and R. B. McComb. "In Reply: Will Implementation of ICES Delay Method Standardization in Clnical Enzymology?" Clinical Chemistry 31, no. 2 (February 1, 1985): 344–45. http://dx.doi.org/10.1093/clinchem/31.2.344.

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42

Diamandis, Eleftherios P., Andreas Scorilas, Ioannis Prassas, and Mario Plebani. "The International Society for Enzymology: a glorious history, a golden legacy." Clinical Chemistry and Laboratory Medicine (CCLM) 56, no. 11 (October 25, 2018): 275–76. http://dx.doi.org/10.1515/cclm-2018-0766.

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43

Bain, M. D., J. Till, M. G. Jones, G. T. N. Besley, P. Lee, D. Oliveira, and R. A. Chalmers. "Methylmalonic aciduria: Follow-up and enzymology on the original case after 36 years." Journal of Inherited Metabolic Disease 28, no. 6 (December 2005): 1179–80. http://dx.doi.org/10.1007/s10545-005-0244-1.

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44

Ferry, James G. "Enzymology of the fermentation of acetate to methane by Methanosarcina thermophila." BioFactors 6, no. 1 (1997): 25–35. http://dx.doi.org/10.1002/biof.5520060104.

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45

Wigle, Tim J., Laurel M. Provencher, Jacqueline L. Norris, Jian Jin, Peter J. Brown, Stephen V. Frye, and William P. Janzen. "Accessing Protein Methyltransferase and Demethylase Enzymology Using Microfluidic Capillary Electrophoresis." Chemistry & Biology 17, no. 7 (July 2010): 695–704. http://dx.doi.org/10.1016/j.chembiol.2010.04.014.

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46

Bagshaw, Clive R., and Paul B. Conibear. "Single-Molecule Enzymology: Critical Aspects Exemplified by Myosin ATPase Activity." Single Molecules 1, no. 4 (December 2000): 271–77. http://dx.doi.org/10.1002/1438-5171(200012)1:4<271::aid-simo271>3.0.co;2-n.

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47

Wrigglesworth, John M. "Methods in enzymology vols. 226 and 227 metallobiochemistry parts C and D." Cell Biochemistry and Function 12, no. 3 (September 1994): 228. http://dx.doi.org/10.1002/cbf.290120314.

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48

Craig, Douglas B., Gundars Reinfelds, and Anna Henderson. "12-Channel Peltier array temperature control unit for single molecule enzymology studies using capillary electrophoresis." ELECTROPHORESIS 35, no. 16 (March 25, 2014): 2408–11. http://dx.doi.org/10.1002/elps.201300526.

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49

Moss, D. W., F. Schiele, G. Siest, and E. Colinet. "Reference materials for clinical enzymology: the work of the Community Bureau of Reference of the European Community." Clinical Chemistry 32, no. 3 (March 1, 1986): 556–58. http://dx.doi.org/10.1093/clinchem/32.3.556.

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50

Colinet, E., G. Siest, and D. W. Moss. "Reference Materials for Clinical Enzymology: The Work of the Community Bureau of Reference of the European Community." Annals of Clinical Biochemistry: International Journal of Laboratory Medicine 23, no. 4 (July 1986): 361–63. http://dx.doi.org/10.1177/000456328602300401.

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