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dc.contributor.authorPeach, Robert James
dc.date.accessioned2010-09-14T22:06:23Z
dc.date.available2010-09-14T22:06:23Z
dc.date.issued1986
dc.identifier.urihttps://hdl.handle.net/10182/2513
dc.description.abstractHuman Tamm-Horsfall protein (THP) was isolated by salt precipitation from pooled normal urine. Monoclonal antibodies were generated against this glycoprotein by fusion of human THP-primed mouse splenocytes with a mouse myeloma cell line. Six stable monoclonal antibody-producing clones were formed. Each antibody was carefully characterized by three methods immunoperoxidase light microscopy, ELISA inhibition, and Western blotting. Once the specificity of the monoclonal antibodies had been established, they were used to study the distribution of THP in human renal tissue, and measure the concentration of the glycoprotein in serum. One of these monoclonal antibodies (THPC4) was used to develop an immunogold technique to study the ultrastructural localization of THP in human kidneys. Results showed that THP had a discrete renal distribution, being associated with the luminal plasmalemma of distal convoluted tubules, and the whole cell plasmalemma of epithelium lining the thick ascending limb of Henle's loop. Despite some reports in the literature, THP appears to be mainly a membrane-associated protein. This may be related to its, as yet unknown, physiological role. An ELISA assay, again using THPC4, was established to try and determine concentrations of THP in serum of normal subjects. A range of 80-620 ng/mL was found. The use of monoclonal antibodies of defined specificity has provided the means for a more reliable assessment of levels of THP in serum, and distribution within the kidney. It may now be possible to determine a physiological role and pathological significance of THP in renal disease.en
dc.language.isoenen
dc.publisherLincoln College, University of Canterburyen
dc.rights.urihttps://researcharchive.lincoln.ac.nz/page/rights
dc.subjecttamm-horsfall proteinen
dc.subjectmonoclonal antibodiesen
dc.subjectEnzyme-Linked Immunosorbent Assay (ELISA)en
dc.subjectimmunoperoxidase light microscopyen
dc.subjectpre-embedding immunogold electron microscopyen
dc.subjectwestern blottingen
dc.subjectpolyacrylamide gel electrophoresisen
dc.subjectautoradiographyen
dc.subjectdistal convoluted tubuleen
dc.subjectascending limb of Henle's loopen
dc.titleMonoclonal antibodies against human urinary Tamm-Horsfall proteinen
dc.typeThesisen
thesis.degree.grantorUniversity of Canterburyen
thesis.degree.levelMastersen
thesis.degree.nameMaster of Applied Scienceen
lu.thesis.supervisorDay, Tony
lu.contributor.unitDepartment of Wine, Food and Molecular Biosciencesen
dc.rights.accessRightsDigital thesis can be viewed by current staff and students of Lincoln University only. Print copy available for reading in Lincoln University Library. en
dc.subject.anzsrc110303 Clinical Microbiologyen
dc.subject.anzsrc110312 Nephrology and Urologyen
dc.subject.anzsrc0601 Biochemistry and Cell Biologyen
dc.subject.anzsrc060601 Animal Physiology - Biophysicsen


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