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Title: Studies on neuraminidases
Author: Kabayo, John P.
ISNI:       0000 0001 3593 7109
Awarding Body: University of Warwick
Current Institution: University of Warwick
Date of Award: 1978
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In this thesis, the work undertaken in an attempt to gain insight into the catalytic function of neuraminidase is described. The history, properties and importance of neuraminidases are reviewed in Chapter One. Chapter Two contains an account of the production of neuraminidase from Streptomycesgriseus by induction, of its preparation and purification to homogeneity, of its character- isation as a glycoprotein of 32,000 molecular weight and of its structural and catalytic properties. In Chapter Three, chemical modification methods were employed to seek information regarding the nature of the amino acid residues essential in the activity of S. griseus, Cl. perfringens and influenza virus neuraminidases. In all the three enzymes the results obtained suggested that arginine, tryptophan and carboxylic groups were crucial for the enzyme activity. Based on these findings, a mechanism for neura- minidase action was proposed. The extensively purified neuraminidase from S. griseus was used, in conjunction with an isoelectric focussing technique, to investigate the sialylation differences in human Interferons. The results to these experiments, reported in Appendix I, suggest that fibroblast (and not leucocyte or lymphoblastoid) interferon contains neuramini- dase -releasable s ialic acid residues . The experiments reported in Appendix Il, in which rabbits were immunised with colominic acid or fetuin, were conducted to raise antibodies specific to sialic acid in an attempt todesign a radloimmunoassay for free sialic acid.
Supervisor: Not available Sponsor: Makerere University ; Humanitarian Trust ; Commonwealth Inter-University Exchange Fund ; Africa Educational Trust (London, England)
Qualification Name: Thesis (Ph.D.) Qualification Level: Doctoral
EThOS ID:  DOI: Not available
Keywords: QD Chemistry