921 |
Agricultural changes at Euphrates and Steppe sites in the mid-8th to the 6th Millenium B.Cde Moulins, Dominique January 1994 (has links)
No description available.
|
922 |
Genetic control of the immune response to antigenMcDermott, Adrian Bernard January 2000 (has links)
No description available.
|
923 |
A measurement of #GAMMA#(Z'0 -> B'* X)/#GAMMA#(Z'0 -> hadronic) using the DELPHI detector at LEP and development of a testbeam data acquisition systemLast, Iain Jeffrey January 1996 (has links)
No description available.
|
924 |
Bombesin family receptor and ligand gene expression in human colorectal and gastric cancerChave, Helen Sally January 2000 (has links)
No description available.
|
925 |
The NADPH oxidase in human neutrophil cell-free systemsHope, Elizabeth Lee January 1993 (has links)
No description available.
|
926 |
Secretion of GBP, an infective stage-specific protein of Leishmania majorGokoo, Suzanne January 1997 (has links)
No description available.
|
927 |
Enantioselective synthesis of cyclic imidesAdams, David J. January 2000 (has links)
No description available.
|
928 |
Receptor-mediated iron and haem transport in HaemophilusParsons, Tina January 1995 (has links)
No description available.
|
929 |
A measurement of the ratio of partial decay widths..Normand, Ainsley Margaret January 1996 (has links)
No description available.
|
930 |
Redox properties of cathepsin B in relation to its activity in vivo.Pillay, Ché Sobashkar. 21 October 2013 (has links)
The main site for protein degradation along the endosomal pathway is believed to be the late
endosome. Lysosomes are thought to be storage organelles that, when necessary, inject
proteases into the late endosome. It was hypothesised that differences in the lumenal redox
environments between the two organelles could be responsible for their functional
differences. In an attempt to quantify this potential difference, the lysosomal cysteine
protease cathepsin B was isolated by an improved purification procedure. Several
intracellular reducing agents were used to activate cathepsin B, the most effective being
cysteine. Cysteine was used to activate cathepsin B under various pH conditions in order to
model endosomal conditions. An inverse relationship was found between the pH and the
concentration of cysteine required to activate cathepsin B. This suggested that cathepsin B
may have an optimal redox potential. In order to determine this potential, cysteinexystine
redox buffers were made up and used in determination of the activity of the enzyme against a
synthetic and a whole protein substrate (haemoglobin). No distinct redox potential could be
determined using either substrate, but it was found that cystine stimulated proteolysis of
haemoglobin. A similar stimulatory effect was observed for cathepsin D and papain
hydrolysis of haemoglobin. This effect is possibly due to the ability of cystine to promote
substrate structure, effectively increasing the substrate concentration. These findings and
other results obtained from the literature have been used to create a model of how proteolysis
may be regulated along the endosomal system. / Thesis (M.Sc.)-University of Natal, Pietermaritzburg, 1999.
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