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On the biosynthesis and processing of cathepsin G, leukocyte elactase, and azurocidin neutrophil granule members of a hematopoietic serine protease superfamily /Lindmark, Anders. January 1997 (has links)
Thesis (doctoral)--Lund University, 1997. / Added t.p. with thesis statement inserted.
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Molecular biology and clinical studies of human cystatin CÓlafsson, Ísleifur. January 1994 (has links)
Thesis (doctoral)--Lund University, 1994. / Added t.p. with thesis statement inserted.
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Molecular studies on cysteine proteinase in Solanum melongena (BRINJAL) /Xu, Fangxiu. January 1999 (has links)
Thesis (Ph. D.)--University of Hong Kong, 1999. / Includes bibliographical references (leaves 120-142).
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The active site cysteine of arginine kinase structural and functional analysis of partially active mutants /Gattis, James L. Chapman, Michael S., January 2004 (has links)
Thesis (Ph. D.)--Florida State University, 2004. / Advisor: Dr. Michael Chapman, Florida State University, College of Arts and Sciences, Dept. of Chemistry and Biochemistry. Title and description from dissertation home page (viewed Sept. 15, 2005). Document formatted into pages; contains vi, 76 pages. Includes bibliographical references.
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Molecular biology and clinical studies of human cystatin CÓlafsson, Ísleifur. January 1994 (has links)
Thesis (doctoral)--Lund University, 1994. / Added t.p. with thesis statement inserted.
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Characterization of the promoter of SmCP, the gene encoding Solanum melongena cysteine proteinaseRawat, Reetika. January 2004 (has links)
Thesis (Ph. D.)--University of Hong Kong, 2005. / Title proper from title frame. Also available in printed format.
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Characterization of proteinase inhibitor II from Solanum Americanum /Sin, Suk-fong. January 2004 (has links)
Thesis (Ph. D.)--University of Hong Kong, 2005.
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Design and synthesis of phosphorus-based inhibitors for the HIV-1 proteinasePerrey, David Alan January 1995 (has links)
A number of peptide fragments including (2S)-Pro-(2S)-Ile-NHiBu (72) and (2S)-Phe-(2S)-Ile-NHiBu (73) and l-(benzyloxycarbonyl)-aminophosphinic acid methyl esters (analogues of Phe (76), Cha (77) and Leu (78)) have been synthesised and coupled to give a series of phosphonamidate methyl ester-based peptide inhibitors of HIV-1 proteinase. These compounds were tested against the proteinase enzyme in vitro using a spectrophotometric assay and displayed activities in the 1-100 muM range. Remarkably, comparison of these data with data obtained for activities against HIV-1 in cultured human lymphocytes showed an in vitro:in vivo ratio of approximately 1:1. These results are indicative of a highly efficient cell uptake mechanism and exceed the reported in vitro:in vivo ratios for HIV proteinase inhibitors by a factor of 103. It is also apparent from the results that the compounds are not rapidly degraded in human lymphocytes. The activities of these compounds, however, was rather insensitive to small structural changes, undermining our attempts to optimise them. A phosphonamidate ethyl ester (Cbz-Phe-PO(OCH2CH3)NH-(2S)-Phe-(2S)-Ile- NHiBu (94)) was prepared and this possessed an IC50 of 4.5 muM, indicating that it might be possible to incorporate larger ligands onto the ester portion of the molecule. Due to the problems associated with peptidic compounds as therapeutic agents, a number of non-peptidic targets were designed. 3,3'-Di- (benzyloxycarbonyl)-aminobenzoin (103) was synthesised in three steps from m- nitrobenzaldehyde and this displayed an IC50 of 8 muM. Molecular modelling of a second target, a bicyclic phosphorodiamidate (106), showed that this compound should adopt a skewed position within the enzyme's active site, with the OH group between the catalytic aspartates (Asp 25 and Asp 25') and the P=0 strongly hydrogen-bonded to one of the flap Ile's but relatively distant from the other. A synthesis of this molecule from tris (hydroxymethyl)amino-methane was undertaken, but problems with this led to the design of the less-substituted phosphorodiamidate (116). An alternative route from diethyl malonate was begun, although to date this has not been completed. This work is now under investigation by others in our group.
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Proteinases Larvares de Dermatobia hominis (Linnaeus Jr., 1781) (DIPTERA: CUTEREBRIDAE). / Dermatobia hominis (Linnaeus Jr., 1781) (DIPTERA: CUTEREBRIDAE) Larvae Proteinases.Pires, Fabiano Araujo 26 April 2007 (has links)
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Previous issue date: 2007-04-26 / Conselho Nacional de Desenvolvimento Cient?fico e Tecnol?gico / We performed a combination of proteinase assay, either in solution or immobilized in sodium
dodecyl sulfate-polyacrylamide gel copolymerized with gelatin, to detect and quantify
proteinases of Dermatobia hominis second (L2) and third (L3) instar larvae. In quantitative
assays, we examined proteinase activity by hydrolysis of a panel of peptide bonds specific for
the main proteinase classes. We verified that the pGlu-Phe-Leu p-nitroanilide substrate was
hydrolyzed by crude extracts of L2 (3.0 ? 0.2 nmoles hour-1 mg of protein-1) and L3 (7.7 ? 0.1
nmoles hour-1 mg of protein-1) and that both activities were partially inhibited by transepoxysuccinyl-
L-leucylamido-(4-guanidino)butane, 15 % and 3 % respectively. Also, we
demonstrated that the Na-p-Tosyl-L-Arg methyl ester substrate was hydrolyzed by crude
extracts of L2 (117 ? 24 nmoles hour-1 mg of protein-1) and L3 (111 ? 10 nmoles hour-1 mg of
protein-1), suggesting a predominance of esterase activity in the crude larval preparation.
Interestingly, the specific activity of serine-proteinases was totally inhibited by
Phenylmethylsulphonyl fluoride in the L3 crude extract, while only 10 % of this enzyme class
activity was inhibited in the L2 crude extract. Also, we have detected crude extract L2 (Km =
7,59) larvae have more affinity than L3 larvae (Km = 35,75) to Na-p-Tosyl-L-Arg methyl
ester. The results of the qualitative assays with substrate gels suggested that L2 and L3 larvae
express serine-proteinases with similar (13 kDa and 22 kDa) and distinct (50 kDa in L2 and
30 kDa in L3) relative molecular masses. Additionally, we have isolated an enriched esterase
activity from L3 crude extract using successive chromatographies in Aprotinine-Agarose and
DEAE-Sephacell columns. By this strategy we detected only one 50 kDa proteinase in this
larvae crude extract. Finally, these findings contribute to the biochemical characterization of
D. hominis L2 and L3 larvae. / Neste trabalho foram realizados ensaios de atividade de proteinase em solu??o e com
prote?nas imobilizadas em gel de poliacrilamida contendo dodecil sulfato de s?dio
copolimerizado com gelatina, para detec??o e quantifica??o das proteinases presentes nos
extratos larvares de segundo (L2) e terceiro (L3) est?gios de Dermatobia hominis. Nos
ensaios quantitativos, utilizou-se um painel de pept?deos sint?ticos espec?ficos para as
principais classes de proteinases. Verificamos que o substrato pGlu-Phe-Leu p-nitroanilide foi
hidrolisado pelo extrato total de L2 (3,0 ? 0,2 nmoles hora-1 mg de prote?na-1) e L3 (7,7 ? 0,1
nmoles hora-1 mg de prote?na-1) e que ambas atividades foram parcialmente inibidas pelo
trans-epoxysuccinyl-L-leucylamido-(4-guanidino)butane, 15 % e 3 % respectivamente.
Tamb?m, demonstramos que o substrato Na-p-Tosyl-L-Arg methyl ester foi hidrolisado pelos
extratos totais de L2 (117 ? 24 nmoles hora-1 mg de prote?na-1) e L3 (111 ? 10 nmoles hora-1
mg de proteina-1), sugerindo uma predomin?ncia da atividade ester?sica nestes extratos. A
atividade espec?fica de serino-proteinases foi totalmente inibida pelo phenylmethylsulphonyl
fluoride nos extratos de L3, enquanto que somente 10 % desta atividade foi inibida nos
extrados de L2. Al?m disso, n?s detectamos que o extrato total das larvas L2 (Km = 7,59) tem
maior afinidade ao Na-p-Tosyl-L-Arg methyl ester do que o extrato total das larva de L3 (Km
= 35,75). Os resultados do ensaio qualitativo com g?is de substrato sugerem que os extratos
larvares L2 e L3 expressam serino-proteinases com similares (13 kDa e 22 kDa) e distintas
(50 kDa em L2 e 30 kDa em L3) massas moleculares relativas. Adicionalmente, isolamos
uma atividade ester?sica enriquecida do extrato total de L3 utilizando sucessivas
cromatografias em colunas de Aprotinina-Agarose e DEAE-Sephacell. Com esta estrat?gia,
detectamos somente uma banda de proteinase de 50 kDa neste extrato total. Estes resultados
contribuem para a caracteriza??o das proteinases larvares de D. hominis.
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Synthesis and kinetics of cysteine proteinase inhibitorsTehrani, Kamin A. 08 1900 (has links)
No description available.
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