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dc.contributor.advisorDennison, Clive.
dc.creatorMoolman, Lizette.
dc.date.accessioned2013-11-08T07:10:25Z
dc.date.available2013-11-08T07:10:25Z
dc.date.created2001
dc.date.issued2013-11-08
dc.identifier.urihttp://hdl.handle.net/10413/9940
dc.descriptionThesis (M.Sc.)-University of Natal, Pietermaritzburg, 2001.en
dc.description.abstractBecause 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.en
dc.language.isoen_ZAen
dc.subjectCathepsin B.en
dc.subjectClinical enzymology.en
dc.subjectAutoantibodies.en
dc.subjectTheses--Biochemistry.en
dc.subjectCancer--Immunological aspects.en
dc.titleInduction of auto-antibodies to Cathepsin B.en
dc.typeThesisen


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