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Studies in neuraminidases

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Kabayo, John P. (1978) Studies in neuraminidases. PhD thesis, University of Warwick.

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Official URL: http://webcat.warwick.ac.uk/record=b1750464~S1

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Abstract

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.

Item Type: Thesis (PhD)
Subjects: Q Science > QD Chemistry
Library of Congress Subject Headings (LCSH): Neuraminidase, Glycosidases, Streptomyces griseus, Clostridium perfringens, Catalysts, Enzymes
Official Date: October 1978
Dates:
DateEvent
October 1978Submitted
Institution: University of Warwick
Theses Department: Department of Chemistry
Thesis Type: PhD
Publication Status: Unpublished
Supervisor(s)/Advisor: Hutchinson, D. W. (David Wesley)
Sponsors: Makerere University, Humanitarian Trust, Commonwealth Inter-University Exchange Fund, Africa Educational Trust (London, England)
Extent: vii, 140 leaves
Language: eng

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