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Proteinase inhibitor II from Solanum americanum, molecular characterization and potential use in generating insect-resistanttransgenic vegetables徐增富, Xu, Zengfu. January 2001 (has links)
published_or_final_version / abstract / toc / Botany / Doctoral / Doctor of Philosophy
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Studies on food-derived antihypertensive peptides殷子敬, Yan, Tsz-king, Eric. January 2000 (has links)
published_or_final_version / Zoology / Master / Master of Philosophy
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Ruthenium anticancer complexes : a targeted approach to enzyme inhibitionPage, Simon Matthew January 2013 (has links)
No description available.
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Usage patterns and cost analysis of angiotensin-converting enzyme (ACE) inhibitors using a medical aid claims database / Dineo Precious SeletswaneSeletswane, Dineo Precious January 2004 (has links)
ACE inhibitors have been widely used in the treatment of certain diseases of the
cardiovascular system, the major use being hypertension, since all ACE inhibitors are
prescribed for its treatment. ACE inhibitors is also used in the treatment of congestive
heart failure.
The angiotensin-converting enzyme (ACE) converts angiotensin 1 into angiotensin I1
and also stimulates the production of aldosterone (a hormone produced in the adrenal
glands that influences salt and water retention by the kidneys, increasing blood
volume and blood pressure).
The cost benefit, cost-effectiveness and cost utility of ACE inhibitors have not been
established. The objective of the study was to review and analyse the cost of ACE
inhibitors by using a medical aid claims database.
Data for the study population consisted of all prescriptions containing one or more
ACE inhibitor combinations and were extracted from the central database of
Interpharm datasystems for a period of one year, from 1 January 2001 to 31
December 2001. A total of 1 475 532 prescriptions containing a total of 2 953 244
ACE inhibitor items represented the study population.
Through the analysis of the general medicine utilisation patterns that were obtained
from the medicine claims database, it became evident that ACE inhibitor utilisation
contributes considerably to the total prevalence and cost of all the medicine items
available on the database. It constituted a total prevalence of 4,62% (n =1 475 532) of
all the prescriptions and a total prevalence of 2,31% (n =2 953 244) for all the
medicine items in the prescriptions with a cost of 3,65% (n =R379 91 1 472,OO).
It was concluded that in the analysis of ACE inhibitors according to the
innovator/generic classification, the majority of ACE inhibitors prescribed during the
twelve-month period were for the innovator product, with a prevalence of 82,56% (n
=68 162) and a cost of 89,11% (n =R13 863 080, 90). The utilisation of the generic
ACE inhibitors, with a prevalence of 17,44% (n =68 162) and at a cost of 10,89% (n
=R13 863 080, 90), was under-utilised. If the total number of prescriptions containing
innovator ACE inhibitors could be generically substituted, (37,54%) R5 204 392,68 in
cost expenditure could be saved over a twelve-month period. However, the fact that
not all the innovator ACE inhibitors have generic equivalents available must be taken
into account. If only the prescriptions containing ACE inhibitor items that have
generic equivalents were to be substituted with their generic equivalents, R899
751.29(6.5%) would be saved. This was found by adding all the costs saved by
substituting innovator drugs with their generics.
Consequently, it can be concluded that the extensive use of the innovator ACE
inhibitors could mean an exceptional increase in the cost expenditure associated with
ACE inhibitor therapy.
In completion of the study, recommendations were formulated as an aim to optimise
the utilisation of ACE inhibitor generic equivalents. / Thesis (M. Pharm.)--North-West University, Potchefstroom Campus, 2004.
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α-aminoalkylphosphonate di(chlorophenyl) esters as inhibitors of serine proteases : Part II: A kinetic study of the coupling of the hydrolysis product of the N-tosylalanine ester of 5-phenyl-3-hydroxypyrrole to various diazonium salts : Part III: Rates of thrombin acylation and deacylaton upon reaction with low molecular weight acylating agents, carbamylating agents and carbonylatiBrown, Audra Denise 08 1900 (has links)
No description available.
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Lactate dehydrogenase : studies towards the design, synthesis and co-crystallisation of bisubstrate inhibitorsDempster, Sally January 2013 (has links)
No description available.
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The effects of guanidinium chloride, urea and sodium dodecyl sulfate on the endoproteinase Glu-C- catalyzed hydrolysis of N-t-BOC-L-glutamic acid-gas-phenyl esterDelk, Roger Dale January 1994 (has links)
Endoproteinase Glu-C (EPGIu-C, EC 3.4.21.19), an enzyme isolated from the bacteria Staphylococcus aureus, has been found to cleave specifically at the carboxyl-terminal side of glutamyl and aspartyl peptide bonds. EPGIu-C has been reported to be stable and active in the presence of common denaturants such as guanidinium chloride, urea and sodium dodecyl sulfate (Drapeau, G.R. (1977) Methods in Enzymology, 47:189-191). In order assess the denaturant stability and activity of EPGIu-C, the effect of three common protein denaturants, guanidinium chloride, urea, and sodium dodecyl sulfate (SDS) on the proteolytic activity of EPGIu-C was studied.The kinetics of the hydrolyis reaction catalyzed by EPGIu-C was determined using the chromophoric substrate N-tBOC-L-glutamic acid-a-phenyl ester (BGPE).To compare theurea is significantly greater at the higher concentrations of urea. These results suggest that a complete cleavage of proteins substrate by EPGlu-C might occur more rapidly in 8.0 M urea than in 6.0 M GuCl, since EPGlu-C will be operating at a significantly higher catalytic efficiency in the urea solution. / Department of Chemistry
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Usage patterns and cost analysis of angiotensin-converting enzyme (ACE) inhibitors using a medical aid claims database / Dineo Precious SeletswaneSeletswane, Dineo Precious January 2004 (has links)
ACE inhibitors have been widely used in the treatment of certain diseases of the
cardiovascular system, the major use being hypertension, since all ACE inhibitors are
prescribed for its treatment. ACE inhibitors is also used in the treatment of congestive
heart failure.
The angiotensin-converting enzyme (ACE) converts angiotensin 1 into angiotensin I1
and also stimulates the production of aldosterone (a hormone produced in the adrenal
glands that influences salt and water retention by the kidneys, increasing blood
volume and blood pressure).
The cost benefit, cost-effectiveness and cost utility of ACE inhibitors have not been
established. The objective of the study was to review and analyse the cost of ACE
inhibitors by using a medical aid claims database.
Data for the study population consisted of all prescriptions containing one or more
ACE inhibitor combinations and were extracted from the central database of
Interpharm datasystems for a period of one year, from 1 January 2001 to 31
December 2001. A total of 1 475 532 prescriptions containing a total of 2 953 244
ACE inhibitor items represented the study population.
Through the analysis of the general medicine utilisation patterns that were obtained
from the medicine claims database, it became evident that ACE inhibitor utilisation
contributes considerably to the total prevalence and cost of all the medicine items
available on the database. It constituted a total prevalence of 4,62% (n =1 475 532) of
all the prescriptions and a total prevalence of 2,31% (n =2 953 244) for all the
medicine items in the prescriptions with a cost of 3,65% (n =R379 91 1 472,OO).
It was concluded that in the analysis of ACE inhibitors according to the
innovator/generic classification, the majority of ACE inhibitors prescribed during the
twelve-month period were for the innovator product, with a prevalence of 82,56% (n
=68 162) and a cost of 89,11% (n =R13 863 080, 90). The utilisation of the generic
ACE inhibitors, with a prevalence of 17,44% (n =68 162) and at a cost of 10,89% (n
=R13 863 080, 90), was under-utilised. If the total number of prescriptions containing
innovator ACE inhibitors could be generically substituted, (37,54%) R5 204 392,68 in
cost expenditure could be saved over a twelve-month period. However, the fact that
not all the innovator ACE inhibitors have generic equivalents available must be taken
into account. If only the prescriptions containing ACE inhibitor items that have
generic equivalents were to be substituted with their generic equivalents, R899
751.29(6.5%) would be saved. This was found by adding all the costs saved by
substituting innovator drugs with their generics.
Consequently, it can be concluded that the extensive use of the innovator ACE
inhibitors could mean an exceptional increase in the cost expenditure associated with
ACE inhibitor therapy.
In completion of the study, recommendations were formulated as an aim to optimise
the utilisation of ACE inhibitor generic equivalents. / Thesis (M. Pharm.)--North-West University, Potchefstroom Campus, 2004.
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Production and characterization of angiotensin I-convertine enzyme inhibitory peptides from whey fermentation with lactic acid bacteriaAhn, Jae-Eun. January 2001 (has links)
Whey media, containing 2% (w/v) whey powder, 1% (w/v) glucose, and 0.5% (w/v) yeast extract, were fermented with nine Lactobacillus strains to produce angiotensin I-converting enzyme (ACE) inhibitory peptides. Lb. brevis, Lb. helveticus, and Lb. paracasei were most effective in producing whey hydrolysates that contained potent ACE inhibitors, with the inhibition rate ranging from 93.3 +/- 0.3 to 100%. The hydrolysates of three Lactobacillus strains were partially purified by dialysis (6,000--8,000 Da cut-off) to remove larger molecules, and subsequently subjected to RP-HPLC, equipped with a Delta Pak C18 column. Each chromatogram displayed at least three distinct peaks at the hydrophobic region of the elution profile. Altogether fourteen peaks were purified and assayed for ACE inhibitory activity. All peaks except one exhibited ACE inhibitory activities, with IC50 ranging from 5.3 +/- 0.1 to 2637.8 +/- 366.9mug/ml. Three of these peaks contained pentapeptides, which consisted of mostly hydrophobic or aromatic amino acids at the C-terminal.
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Apple polyphenolics and their antioxidant properties : influence of cultivars, post-harvest storage, and 1-MCP treatmentWidyasari, Maria Angela Artania 14 June 2002 (has links)
The distribution of total phenolics, antioxidant capacity, monomeric
anthocyanin, and ascorbic acid contents in the peel and flesh of Red Delicious,
Granny Smith, and Fuji apples during a six-month storage period were determined.
In addition, the effect of 1-MCP (1-Methyl cyclopropene) on these parameters of
the edible portion of apples during storage was also investigated. Two different
assays were employed to determine antioxidant activities: the spectrofluorometric-based
Oxygen Radical absorbing Capacity (ORAC) and the spectrophotometric-based
Ferric Reducing Antioxidant Power (FRAP). Total phenolics were measured
using the Folin-Ciocalteau method. A determination of monomeric anthocyanin
content was also performed using the pH-differential method for Red Delicious
and Fuji apples.
Antioxidant activity was predominantly observed in the aqueous fraction
and was attributed to polyphenolics. Antioxidant activities were highest in the peel,
with Red Delicious peel having the highest values, presumably due to anthocyanin
pigments. At zero time month storage, the ORAC, FRAP, total phenolics, and total
monomeric anthocyanin contents of Red Delicious peel were: 37.7 μmol T.E./g,
62.7 μmol T.E./g, 6.63 mg/g GAE, and 26.4 mg/100g, respectively. The three
tested cultivars were significantly different with respect to ORAC, FRAP, total
phenolics, and monomeric anthocyanin contents. 1-MCP treatment did not have a significant influence on antioxidant activities and monomeric anthocyanin contents
of the three cultivars during storage. Storage did not have significant influence on
ORAC values of the edible portion of apple, however it had significant influence
on the FRAP values. The contribution of ascorbic acid to the total antioxidant
capacity was small. / Graduation date: 2003
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