Relevant bibliographies by topics / Clinical enzymology

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  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters

Academic literature on the topic 'Clinical enzymology'

Author: Grafiati
Published: 4 June 2021
Last updated: 26 July 2024

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Journal articles on the topic "Clinical enzymology"

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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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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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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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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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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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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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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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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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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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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Dissertations / Theses on the topic "Clinical enzymology"

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Bradburne, James Andrew. "Regulation of nif gene expression in bradyrhizobium japonicum." Diss., Georgia Institute of Technology, 1992. http://hdl.handle.net/1853/25742.

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Husain, Philip Anwar. "Investigative enzymology of selected monooxygenases and development of (S)-N-Succinimidyl-a-Methoxyphenylacetate as a novel tool for assignment of absolute configuration." Diss., Georgia Institute of Technology, 1992. http://hdl.handle.net/1853/27579.

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Gerber, Scott Anthony. "Direct profiling of multiple enzymes in human cell lysates by affinity chromatography/electrospray ionization mass spectrometry : application to clinical enzymology /." Thesis, Connect to this title online; UW restricted, 2001. http://hdl.handle.net/1773/8490.

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Marschke, Ronald James. "Milk enzymes as diagnostic indicators of milk secretory disorders." Thesis, Queensland University of Technology, 1987. https://eprints.qut.edu.au/36796/1/36796_Marschke_1987.pdf.

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Studies were carried out on two enzymes of bovine milk, N-acetyl-8-D-glucosaminidase (NAGase) and lactate dehydrogenase (LDH), which are indicators of the udder disease mastitis. The main objective of this study was to determine the origins of NAGase and LDH in milk. The approach used was to examine the differences in multiple forms of the enzymes in mammary gland, blood leucocytes and blood plasma by various separation procedures. The molecular weight forms of NAGase in mammary gland and polymorphonuclear leucocytes showed pH-dependent association-dissociation behaviour on gel filtration, but this property was not apparent for blood plasma NAGase. Improved differentiation of NAGases was achieved by ion exchange chromatography at pH 7.0. This method was used to estimate the contributions from the individual sources t6 the total NAGase activity in milk. Mammary gland was the major source of NAGase in normal and mastitic milk. There was a significant contribution from leucocytes in mastitic milk but the contribution from blood plasma was low. The distributions of LDH isoenzymes were examined by polyacrylamide gel electrophoresis. Similar patterns for PMN leucocytes and blood plasma precluded the use of iso­enzyme separations for differentiating between LDH enzymes from these two sources. The predominance of the LDH-1 isoenzyme in normal milk indicated that LDH originated from mammary tissue in the healthy udder. In mastitic milk, LDH contributions from all sources were apparent. During these studies, assay procedures for the determination of LDH in milk were developed and a color­metric kit test assessed as a field procedure for testing quarter milks. Positive test results with the kit were unreliable, particularly for freshly-collected milk. Improved diagnostic efficien¢y was achieved using a spectrophotometric assay for LDH. Application of the NAGase and LDH tests to the diagnosis of mastitis in goat's milk showed that changes in milk enzyme levels with minor pathogen infections were insufficient to allow discrimination between uninfect­ed and infected halves.
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Abelin, Törnblom Susanne. "Mediators of cervical ripening in preterm birth : experimental and clinical investigations /." Stockholm, 2005. http://diss.kib.ki.se/2005/91-7140-305-1/.

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Moolman, Lizette. "Induction of auto-antibodies to Cathepsin B." Thesis, 2001. http://hdl.handle.net/10413/9940.

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Because tumours are comprised of "self" cells and antigens, they escape recognition by the immune system, which discriminates between "self" and "non-self". One such antigen is cathepsin B, a lysosomal cysteine proteinase, that has been implicated as one of the proteolytic enzymes involved in tumour invasion and metastasis. Cathepsin B autoantibodies could open possibilities which may be useful in cancer immunotherapy. In this study generation of cathepsin B autoantibodies was attempted by manipulating the immune system into recognising and responding to cathepsin B in complex with a "foreign" protein, bovine serum albumin (BSA). Cathepsin B was isolated from rabbit liver using the three phase partitioning (TPP) method, modified by adding t-butanol in the homogenisation buffer. Isolation of cathepsin Band cathepsin L, using this novel method, minimised the formation of artefacts such as a covalent cathepsin L-stefin B complex and produced higher yields of enzyme. Pure rabbit liver cathepsin B was conjugated to BSA, using glutaraldehyde as coupling agent, and administered intramuscularly into rabbits. Another three inoculation protocols, which functioned as controls were: i) free cathepsin B administered intramuscularly, ii) complexed cathepsin B administered intravenously, and iii) free cathepsin B administered intravenously. IgGs isolated from inoculated rabbits' serum were assayed by a three layer ELISA system, immunoinhibition assays and dot blots. The anti-complex (intramuscular) antibodies showed the highest recognition for cathepsin B and were the only antibodies that were immunoinhibitory. This suggests that the immune system was, to some extend, successfully manipulated into recognising the complexed "self" cathepsin B.
Thesis (M.Sc.)-University of Natal, Pietermaritzburg, 2001.
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Basu, Saurajyoti, John E. Brown, G. Michael Flannigan, Jason H. Gill, Paul M. Loadman, Brian Naylor, Andy J. Scally, et al. "Immunohistochemical analysis of NAD(P)H:quinone oxidoreductase and NADPH cytochrome P450 reductase in human superficial bladder tumours: Relationship between tumour enzymology and clinical outcome following intravesical mitomycin C therapy." 2004. http://hdl.handle.net/10454/6409.

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A central theme within the concept of enzyme-directed bioreductive drug development is the potential to predict tumour response based on the profiling of enzymes involved in the bioreductive activation process. Mitomycin C (MMC) is the prototypical bioreductive drug that is reduced to active intermediates by several reductases including NAD(P)H:quinone oxidoreductase (NQO1) and NADPH cytochrome P450 reductase (P450R). The purpose of our study was to determine whether NQO1 and P450R protein expression in a panel of low-grade, human superficial bladder tumours correlates with clinical response to MMC. A retrospective clinical study was conducted in which the response to MMC of 92 bladder cancer patients was compared to the immunohistochemical expression of NQO1 and P450R protein in archived paraffin-embedded bladder tumour specimens. A broad spectrum of NQO1 protein levels exists in bladder tumours between individual patients, ranging from intense to no immunohistochemical staining. In contrast, levels of P450R were similar with most tumours having moderate to high levels. All patients were chemotherapy naïve prior to receiving MMC and clinical response was defined as the time to first recurrence. A poor correlation exists between clinical response and NQO1, P450R or the expression patterns of various combinations of the 2 proteins. The results of our study demonstrate that the clinical response of superficial bladder cancers to MMC cannot be predicted on the basis of NQO1 and/or P450R protein expression and suggest that other factors (other reductases or post DNA damage events) have a significant bearing on tumour response.
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Phillips, Roger M., S. Basu, Jason H. Gill, and Paul M. Loadman. "Immunohistochemical analysis of NAD(P)H:quinone oxidoreductase and NADPH cytochrome P450 reductase in human superficial bladder tumours: Relationship between tumour enzymology and clinical outcome following intravesical mitomycin C therapy." 2009. http://hdl.handle.net/10454/2702.

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A central theme within the concept of enzyme-directed bioreductive drug development is the potential to predict tumour response based on the profiling of enzymes involved in the bioreductive activation process. Mitomycin C (MMC) is the prototypical bioreductive drug that is reduced to active intermediates by several reductases including NAD(P)H:quinone oxidoreductase (NQO1) and NADPH cytochrome P450 reductase (P450R). The purpose of our study was to determine whether NQO1 and P450R protein expression in a panel of low-grade, human superficial bladder tumours correlates with clinical response to MMC. A retrospective clinical study was conducted in which the response to MMC of 92 bladder cancer patients was compared to the immunohistochemical expression of NQO1 and P450R protein in archived paraffin-embedded bladder tumour specimens. A broad spectrum of NQO1 protein levels exists in bladder tumours between individual patients, ranging from intense to no immunohistochemical staining. In contrast, levels of P450R were similar with most tumours having moderate to high levels. All patients were chemotherapy naïve prior to receiving MMC and clinical response was defined as the time to first recurrence. A poor correlation exists between clinical response and NQO1, P450R or the expression patterns of various combinations of the 2 proteins. The results of our study demonstrate that the clinical response of superficial bladder cancers to MMC cannot be predicted on the basis of NQO1 and/or P450R protein expression and suggest that other factors (other reductases or post DNA damage events) have a significant bearing on tumour response.
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Elliott, Edith. "A study of proteinases of invasive cells using cryoultramicrotomy and immunogold labelling." Thesis, 1993. http://hdl.handle.net/10413/9526.

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This study forms part of an investigation into the possible relevance of the lysosomal proteinases, cathepsins B, H, Land D, in cancer cell invasion. In this study, the main technique adopted was the Tokuyasu "cryo" method, in which the tissues were fixed, frozen and sectioned and labelled using the relevant antibodies, which were detected with protein A gold probes. In order to implement the Tokuyasu technique, it was necessary to rebuild a knife maker, for the production of adequately sharp glass knives, and to modify a sputter-coater into a glow-discharger, for rendering carbon-coated grids hydrophilic, to promote adhesion of hydrated sections. This study was directed towards human tissues and peptide antibodies were investigated as a means of avoiding isolation of proteins from scarce human tissue, and as a means of obtaining antibodies that will target specific regions of proteins of interest. Peptide antibodies were also considered promising for studies of proteinase trafficking and as immunoinhibiting agents, potentially useful in cancer therapy. Various prediction programmes were investigated for their effectiveness in predicting whether a given peptide sequence will elicit antibodies that will react with the native protein. Successful prediction would increase the success rate of peptide antibody production and thus lower the cost. Leucocytes were studied as a model of an invasive cell, since they are more readily available than tumour cells and serve the purpose during the development of methods. In the course of these studies, an optimal protocol for the fixation of PMNs was developed, involving lateral fixation of cut sections, that should be useful for future studies on these cells. Elastase and cathepsins D and G were found on the surface of activated PMNs and could thus play a role in the invasive properties of these cells. Studies on MCF-10A "normal" breast epithelial cells and their ras-transformed Neo-T counterparts revealed that upon transformation, lysosomes shift from a perinuclear position, to a more peripheral position. None of the cathepsins studied was found on the cell surface of either the normal or ras-transfected cells, suggesting that surface distribution of these enzymes may not be a requirement for invasiveness. These studies suggest that immunocytochemical investigation of cells, in the process of invading through a barrier membrane, might be profitable in elucidating the role of proteinases in invasive cancer.
Thesis (Ph.D.)-University of Natal, Pietermaritzburg, 1993.
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Books on the topic "Clinical enzymology"

1

Hawcroft, David. Diagnostic enzymology. Edited by James A. M. 1923- and ACOL. Chichester: Published on behalf of ACOL by Wiley, 1987.

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Practical enzymology. 2nd ed. Weinheim: Wiley-Blackwell, 2011.

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Lewis, Stevens, ed. Fundamentals of enzymology. 2nd ed. Oxford: Oxford University Press, 1989.

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1923-, James A. M., and ACOL (Project), eds. Diagnostic enzymology. Chichester: Published on behalf on ACOL, London, by Wiley, 1987.

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Lott, John A. Clinical enzymology: A case-oriented approach. New York City, N.Y: Field, Rich, and Associates, 1986.

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Lester, Packer, ed. Oxidants and antioxidants. San Diego: Academic Press, 1999.

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Park, Kwan-Hwa. Carbohydrate-active enzymes: Structure, function and applications. Cambridge: Woodhead Publishing Ltd, 2008.

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L, Campbell Judith, and Modrich Paul, eds. DNA repair. Amsterdam: Elsevier/Academic Press, 2006.

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Jung, K. 1942 Jan. 22-, Mattenheimer Hermann, and Burchardt U, eds. Urinary enzymes in clinical and experimental medicine. Berlin: Springer-Verlag, 1992.

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(Editor), F. W. Schmidt, and Ellen Schmidt (Editor), eds. Clinical Enzymology. S Karger AG, 1987.

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Book chapters on the topic "Clinical enzymology"

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Faye, Bernard, and Mohammed Bengoumi. "Clinical Enzymology." In Camel Clinical Biochemistry and Hematology, 123–72. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-95562-9_5.

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Moss, Donald W. "New Perspectives in Clinical Enzymology." In Clinical Chemistry, 377–83. Boston, MA: Springer US, 1989. http://dx.doi.org/10.1007/978-1-4613-0753-2_36.

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Loos, Michael, and Jochem Alsenz. "The Clinical Enzymology of the Complement System." In Clinical Chemistry, 387–95. Boston, MA: Springer US, 1989. http://dx.doi.org/10.1007/978-1-4613-0753-2_38.

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Napoli, J. L. "Enzymology and biogenesis of retinoic acid." In Vitamin A and Retinoids: An Update of Biological Aspects and Clinical Applications, 17–27. Basel: Birkhäuser Basel, 2000. http://dx.doi.org/10.1007/978-3-0348-8454-9_2.

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Ellen and Friedrich Werner Schmidt. "Serum Cholinesterase: Genetics, Enzymology, Diagnostic Use and the Association with Clinical Disorders." In Esterases, Lipases, and Phospholipases, 13–25. Boston, MA: Springer US, 1994. http://dx.doi.org/10.1007/978-1-4899-0993-0_2.

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Kramer, John W., and Walter E. Hoffmann. "Clinical Enzymology." In Clinical Biochemistry of Domestic Animals, 303–25. Elsevier, 1997. http://dx.doi.org/10.1016/b978-012396305-5/50013-0.

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Chatterjea, MN. "Clinical Enzymology." In Viva in Biochemistry, 432. Jaypee Brothers Medical Publishers (P) Ltd., 2010. http://dx.doi.org/10.5005/jp/books/11115_23.

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Tiwari, Prafulla. "Clinical Enzymology." In Methods in Drug Evaluation, 10. Jaypee Brothers Medical Publishers (P) Ltd., 2018. http://dx.doi.org/10.5005/jp/books/18035_3.

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"Clinical Enzymology." In Handbook of Clinical Biochemistry, 325–47. WORLD SCIENTIFIC, 2011. http://dx.doi.org/10.1142/9789812837394_0013.

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Vasudevan, DM, Sreekumari S, and Kannan Vaidyanathan. "Clinical Enzymology." In Textbook of Biochemistry for Medical Students, 78. Jaypee Brothers Medical Publishers (P) Ltd., 2016. http://dx.doi.org/10.5005/jp/books/13014_7.

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