Literatura académica sobre el tema "Bowman-Birk inhibitor"
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Artículos de revistas sobre el tema "Bowman-Birk inhibitor"
Wu, Y. Victor y David J. Sessa. "Conformation of Bowman-Birk Inhibitor". Journal of Agricultural and Food Chemistry 42, n.º 10 (octubre de 1994): 2136–38. http://dx.doi.org/10.1021/jf00046a012.
Texto completoChen, Xi, Dong Chen, Linyuan Huang, Xiaoling Chen, Mei Zhou, Xinping Xi, Chengbang Ma, Tianbao Chen y Lei Wang. "Identification and Target-Modification of SL-BBI: A Novel Bowman–Birk Type Trypsin Inhibitor from Sylvirana latouchii". Biomolecules 10, n.º 9 (28 de agosto de 2020): 1254. http://dx.doi.org/10.3390/biom10091254.
Texto completoWan, X. Steven, David G. Serota, Jeffrey H. Ware, James A. Crowell y Ann R. Kennedy. "Detection of Bowman-Birk Inhibitor and Anti-Bowman-Birk Inhibitor Antibodies in Sera of Humans and Animals Treated With Bowman-Birk Inhibitor Concentrate". Nutrition and Cancer 43, n.º 2 (julio de 2002): 167–73. http://dx.doi.org/10.1207/s15327914nc432_7.
Texto completoOthman, Tajul Ariffien, Norliza Abu Bakar, Rabiatul Adawiah Zainal Abidin, Maziah Mahmood, Noor Baity Saidi y Noor Azmi Shaharuddin. "Potential of Plant’s Bowman-Birk Protease Inhibitor in Combating Abiotic Stresses: A Mini Review". Bioremediation Science and Technology Research 2, n.º 2 (31 de enero de 2015): 25–33. http://dx.doi.org/10.54987/bstr.v2i2.179.
Texto completoPusztai, A., G. Grant, S. Bardocz, K. Baintner, E. Gelencser y S. W. Ewen. "Both free and complexed trypsin inhibitors stimulate pancreatic secretion and change duodenal enzyme levels". American Journal of Physiology-Gastrointestinal and Liver Physiology 272, n.º 2 (1 de febrero de 1997): G340—G350. http://dx.doi.org/10.1152/ajpgi.1997.272.2.g340.
Texto completo&NA;. "Bowman-Birk inhibitor concentrate for chemoprevention?" Inpharma Weekly &NA;, n.º 1272 (enero de 2001): 11. http://dx.doi.org/10.2165/00128413-200112720-00024.
Texto completoSong, Hyun Kyu y Se Won Suh. "Preliminary X-ray crystallographic analysis of Bowman–Birk trypsin inhibitor from barley seeds". Acta Crystallographica Section D Biological Crystallography 54, n.º 3 (1 de mayo de 1998): 441–43. http://dx.doi.org/10.1107/s0907444997010986.
Texto completoMiao, Yuxi, Guanzhu Chen, Xinping Xi, Chengbang Ma, Lei Wang, James F. Burrows, Jinao Duan, Mei Zhou y Tianbao Chen. "Discovery and Rational Design of a Novel Bowman-Birk Related Protease Inhibitor". Biomolecules 9, n.º 7 (14 de julio de 2019): 280. http://dx.doi.org/10.3390/biom9070280.
Texto completode Freitas, Sonia Maria, Luciano Paulino Silva, Jose Roberto S. A. Leite y Carlos Bloch Jr. "Stability of a black eyed pea trypsin/chymotrypsin inhibitor (BTCI)". Protein & Peptide Letters 7, n.º 6 (diciembre de 2000): 397–401. http://dx.doi.org/10.2174/092986650706221207164315.
Texto completoAhmed, E. M. y J. A. Applewhite. "Characterization of Trypsin Inhibitor in Florunner Peanut Seeds (Arachis hypogaea L.)1". Peanut Science 15, n.º 2 (1 de julio de 1988): 81–84. http://dx.doi.org/10.3146/i0095-3679-15-2-10.
Texto completoTesis sobre el tema "Bowman-Birk inhibitor"
Martins, Thiago Fernandes. "Purificação e caracterização bioquímica de um inibidor tipo Bowman-Birk de sementes Luetzelburgia auriculata (Allemão) Ducke". reponame:Repositório Institucional da UFC, 2015. http://www.repositorio.ufc.br/handle/riufc/16473.
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Plant protease inhibitors are proteins of low molecular weight, usually present in high concentrations in storage tissues, particularly in seeds of species belong to the Fabaceae family. In this study, a Bowman-Birk protease inhibitor (LzaBBI) was purified from the saline extract of the Luetzelburgia auriculata seeds After boiling of this saline extract, the inhibitor was purified by affinity chromatography on Sepharose® 4B-anhydrotrypsin, followed by ion exchange chromatography on DEAE Sepharose and reverse phase chromatography. Under reducing conditions or not, LzaBBI showed an apparent molecular mass of 17.3 kDa and a single polypeptide chain. The NH2-terminal sequencing of the LzaBBI showed high similarity with other Bowman-Birk inhibitors of legumes. LzaBBI remained stable after boiling at 98 °C for 120 min and also remained stable with trypsin inhibitory activity after incubation in pH buffers with pHs varying from 2 to 11. In addition to its relevant structural stability, of importance in future biotechnological applications, LzaBBI showed negative impact on the Staphylococcus aureus development when at low doses.
Inibidores de proteases vegetais são proteínas de baixa massa molecular, geralmente presentes em altas concentrações nos tecidos de armazenamento, particularmente em sementes de plantas pertencentes à família Fabaceae. Neste estudo, um inibidor de proteases pertencente à família Bowman-Birk (LzaBBI) foi purificado a partir do extrato salino de sementes de Luetzelburgia auriculata. Após fervura desse extrato salino, o inibidor foi purificado por cromatografia de afinidade em matriz de anidrotripsina-Sepharose® 4B, seguido de cromatografia em matriz de troca iônica (DEAE Sepharose) e cromatografia em fase reversa. Em condições redutoras, ou não, o LzaBBI apresentou massa molecular aparente de 17,3 kDa, e uma única cadeia polipeptídica. Sua sequência NH2-terminal possui alta similaridade com inibidores do tipo Bowman-Birk de leguminosas. O LzaBBI permaneceu estável após fervura a 98 °C por 120 min, bem como após incubado na faixa de pHs entre 2 a 11. Além de possuir relevante estabilidade estrutural, de importância para futuras aplicações biotecnológicas, apresentou efeito negativo no crescimento da bactéria Staphylococcus aureus, quando em baixas concentrações.
Martins, Thiago Fernandes. "PurificaÃÃo e caracterizaÃÃo bioquÃmica de um inibidor tipo Bowman-Birk de sementes Luetzelburgia auriculata (AllemÃo) Ducke". Universidade Federal do CearÃ, 2015. http://www.teses.ufc.br/tde_busca/arquivo.php?codArquivo=15486.
Texto completoInibidores de proteases vegetais sÃo proteÃnas de baixa massa molecular, geralmente presentes em altas concentraÃÃes nos tecidos de armazenamento, particularmente em sementes de plantas pertencentes à famÃlia Fabaceae. Neste estudo, um inibidor de proteases pertencente à famÃlia Bowman-Birk (LzaBBI) foi purificado a partir do extrato salino de sementes de Luetzelburgia auriculata. ApÃs fervura desse extrato salino, o inibidor foi purificado por cromatografia de afinidade em matriz de anidrotripsina-Sepharose 4B, seguido de cromatografia em matriz de troca iÃnica (DEAE Sepharose) e cromatografia em fase reversa. Em condiÃÃes redutoras, ou nÃo, o LzaBBI apresentou massa molecular aparente de 17,3 kDa, e uma Ãnica cadeia polipeptÃdica. Sua sequÃncia NH2-terminal possui alta similaridade com inibidores do tipo Bowman-Birk de leguminosas. O LzaBBI permaneceu estÃvel apÃs fervura a 98 ÂC por 120 min, bem como apÃs incubado na faixa de pHs entre 2 a 11. AlÃm de possuir relevante estabilidade estrutural, de importÃncia para futuras aplicaÃÃes biotecnolÃgicas, apresentou efeito negativo no crescimento da bactÃria Staphylococcus aureus, quando em baixas concentraÃÃes.
Plant protease inhibitors are proteins of low molecular weight, usually present in high concentrations in storage tissues, particularly in seeds of species belong to the Fabaceae family. In this study, a Bowman-Birk protease inhibitor (LzaBBI) was purified from the saline extract of the Luetzelburgia auriculata seeds After boiling of this saline extract, the inhibitor was purified by affinity chromatography on Sepharose 4B-anhydrotrypsin, followed by ion exchange chromatography on DEAE Sepharose and reverse phase chromatography. Under reducing conditions or not, LzaBBI showed an apparent molecular mass of 17.3 kDa and a single polypeptide chain. The NH2-terminal sequencing of the LzaBBI showed high similarity with other Bowman-Birk inhibitors of legumes. LzaBBI remained stable after boiling at 98 ÂC for 120 min and also remained stable with trypsin inhibitory activity after incubation in pH buffers with pHs varying from 2 to 11. In addition to its relevant structural stability, of importance in future biotechnological applications, LzaBBI showed negative impact on the Staphylococcus aureus development when at low doses.
José, Márcia Ometto de Mello Alves. "Inibidores de proteinase do tipo Bowman-Birk: evolução molecular, expressão na superfície de fagos filamentosos e seu papel na interação planta-inseto". Universidade de São Paulo, 2002. http://www.teses.usp.br/teses/disponiveis/11/11137/tde-14022003-152133/.
Texto completoThe Bowman-Birk inhibitors (BBIs) are double headed inhibitors of serine proteinase found in plants from Fabaceae and Poaceae families. We describe the primary structure and the gene expression profile of 14 putative BBIs from the sugarcane expressed sequence tag (SUCEST) database and show how we used these newly discovered sequences together with 87 previously described BBI sequences from the "GenBank" database to construct phylogenetic trees for the BBI family. Phylogenetic analysis revealed that BBI-type inhibitors from monocotyledonous and dicotyledonous plants could be clearly separated into different groups, while the overall topology of the BBI tree suggests a different pattern of evolution for BBI families in flowering plants. We also found that BBI proteinase inhibitors from dicotyledonous plants were well conserved, accumulating only slight differences during their evolution. In addition, we found that BBIs from monocotyledonous plants were highly variable, indicating an interesting process of evolution based on internal gene duplications and mutation events. Two serine-type proteinase inhibitors, a trypsin and a chymotrypsin, both derived from the soybean Bowman-Birk inhibitor, were expressed on the surface of a filamentous phage. Site mutations were made in four positions of the reactive sites of these inhibitors and two phage-display libraries were constructed. Later, these libraries were used to select better ligands to the bovine and Diatraea saccharalis trypsin and to the midgut enzymes of this insect pest. The selected variants were sequenced, analyzed and characterized. The results showed that the phage-display technique is efficient to select new proteinase inhibitors. Furthermore, it was possible to modify the chymotrypsin loop into a trypsin loop using the library constructed by the insertion of a degenerated primer.
Kruger, Sarah Jane y n/a. "Characterisation of Proteins from Grevillea robusta and NMR Studies of the Serine Protease Inhibitor". Griffith University. School of Science, 2004. http://www4.gu.edu.au:8080/adt-root/public/adt-QGU20040618.150708.
Texto completoKruger, Sarah Jane. "Characterisation of Proteins from Grevillea robusta and NMR Studies of the Serine Protease Inhibitor". Thesis, Griffith University, 2004. http://hdl.handle.net/10072/366534.
Texto completoThesis (PhD Doctorate)
Doctor of Philosophy (PhD)
School of Science
Full Text
Tchanque, Kemtchou Valéry. "Magnetit-Nanokomposite als Funktionspartikeln für die Bioseparation". Doctoral thesis, Technische Universitaet Bergakademie Freiberg Universitaetsbibliothek "Georgius Agricola", 2014. http://nbn-resolving.de/urn:nbn:de:bsz:105-qucosa-156369.
Texto completoPANZERI, DAVIDE. "A Bioprospecting Multidisciplinary Approach to Valorise Biodiversity: The Case of Bowman-Birk Protease Inhibitors in Vigna unguiculata (L.) Walp". Doctoral thesis, Università degli Studi di Milano-Bicocca, 2023. https://hdl.handle.net/10281/404605.
Texto completoNatural biodiversity is an important source for humans since ancient times. However, biodiversity is experiencing a dramatic decline and many species are at extinction risk. Climate change and human activity are the main drivers of non-sustainable landscape conservation and management. The opportunity to dampen climate change effects is provided by indigenous species, domesticated in local contexts but are little investigated. In this framework, this PhD thesis aims at developing strategies to valorise natural biodiversity, considering different integrative scientific aspects. The first objective of this thesis is the rediscovery of a traditional African legume, Vigna unguiculata (L.) Walp., and assess its adaptability to stressful conditions typically caused by climate change or undemanding agricultural practices. Moreover, the research for bioactive compounds is an added value to give consciousness of the species potential. For this purpose, exploration of genetic diversity of known legume bioactive compounds, the Bowman-Birk protease inhibitors (BBIs) and appraisal of their nutraceutical properties are the second objectives of the project. A multidisciplinary experimental overview has been applied by integrating different approaches to create a coherent workflow. The demonstration of Vigna unguiculata L. as suitable species for climate change was carried out with a field experiment and subsequent laboratory analyses to evaluate production parameters and metabolic features. The genetic diversity of this species was explored through molecular biology techniques and in silico computational and phylogenetic analyses. The nutraceutical features were established by biochemical procedures and cellular biology by testing compounds on different ageing and cancer models. From the point of view of cultivation needs, it is possible to consider V. unguiculata (L.) Walp. as undemanding in terms of water demand and agronomic practices. This makes this legume suitable for conservation agriculture practices in developing countries and where climate change is having a dramatic impact on indigenous crop. This legume is also an important resource of essential macronutrients and to enhance this species and promote its cultivation globally, we also wanted to focus on the presence of bioactive molecules with direct action on humans. The genetic exploration considered almost 200 accessions and found 13 isoforms of BBI were identified in different wild and cultivated accessions, distributed in the African continent and in other areas of the world. Furthermore, we managed to develop an extraction and purification procedure to isolate single isoforms and characterise them. Our data suggest that V. unguiculata BBIs possess a great natural genetic and biochemical diversity. Moreover, the demonstration of BBI-related bioactivities on different models makes them very promising as a high-value natural compound for human wellbeing. The direct action on different tumour cell lines suggests a possible therapeutic application also in synergy with some drugs (i.e. Cetuximab). This opens opportunities for future research on similar related species and genera, and on the analyses to evaluate the most effective isoforms also in in vivo systems. In conclusion, this PhD project demonstrates that i) bioprospection of local species directed to the search for bioactive molecules represents an important lever for safeguarding; ii) the knowledge of evolution and diversification of the plants of interest is a tool to improve bioprospecting actions and identify molecular variants of bioactive compounds; iii) analyses of functional efficacy of bioactive compounds in in vitro and in vivo systems is a fundamental step to dedicate scientific research to the enhancement of biodiversity in an operational context. This is an essential phase to stimulate private investors and businesses to bring economic and social value and biodiversity conservation.
Nievo, Marco. "Peptidic inhibitors of serine proteases : variations on a cyclic template based on the reactive site loop of Bowman Birk inhibitors". Thesis, Imperial College London, 2003. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.407519.
Texto completoDantzger, Miriam 1981. "Inibidor de proteinase do tipo Bowman-Birk isolado de sementes de Clitoria fairchildiana (Fabaceae) : caracterização e atividade biológica sobre Anagasta kuehniella e Corcyra cephalonica". [s.n.], 2014. http://repositorio.unicamp.br/jspui/handle/REPOSIP/314532.
Texto completoTese (doutorado) - Universidade Estadual de Campinas, Instituto de Biologia
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Resumo: Os inibidores de proteinases extraídos de plantas têm se mostrado promissores como um método alternativo no combate aos insetos-pragas. Neste estudo, um inibidor de peptidase foi isolado de sementes de Clitoria fairchildiana (Papilionoideae), denominado CFPI, caracterizado funcional e estruturalmente e sua atividade inseticida foi avaliada. CFPI foi purificado por exclusão molecular, seguido por coluna de interação hidrofóbica e apresentou um pico majoritário com atividade inibitória após ter sido submetido à filtração com alta resolução. Estudos cinéticos realizados com CFPI purificado mostraram uma atividade inibitória do tipo competitiva contra tripsina e quimotripsina bovinas, com uma estequiometria de inibição de 1:1 para ambas as enzimas. A constante de inibição de CFPI contra tripsina e quimotripsina bovinas foram 3,3 x 10-10 e 1,5 x 10-10 M, respectivamente, revelando uma forte capacidade de ligação. Eletroforese em SDS-Page mostrou que CFPI possui uma única cadeia polipeptídica, com uma massa molecular aparente de 15 kDa, sob condições não redutoras. Entretanto, o inibidor apresentou uma massa acurada de 7973 Daltons determinada por MALDI-TOF, sugerindo que CFPI forme dímeros em solução. Essa característica, aliada à estequiometria de inibição para tripsina e quimotripsina, à constante de inibição (Ki) para ambas as enzimas e ao sequenciamento e alinhamento N-terminal, permitiram classificar CFPI como membro da família Bowman-Birk de inibidores. O inibidor manteve-se estável ao aquecimento progressivo por 30 min a cada temperatura, variando de 37 até 100 ?C e a análise de dicroísmo não mostrou mudanças no espectro a 207 nm após aquecimento à 90 ?C e subsequente resfriamento. Além disso, CFPI mostrou atividade sobre uma ampla faixa de pH (2-10). Em contraste, a redução de CFPI com DTT resultou em perda de atividade inibitória contra tripsina e quimotripsina. CFPI exibiu atividade inibitória considerável contra enzimas tripsinas de Anagasta kuehniella (76%), Diatraea saccharalis (59%) e Heliothis virescens (49%). Suas propriedades inseticidas foram confirmadas a partir do impacto negativo causado no crescimento de A. kuehniella e C. cephalonica. O inibidor exerceu efeito antinutricional sobre A. kuehniella tanto na geração F0 como em F1
Abstract: Proteinase inhibitors isolated from plants have shown a promising alternative method against insect pests. In this study, a proteinase inhibitor was isolated from Clitoria fairchildiana seeds (CFPI). CFPI was functional and structurally characterized and its insecticidal activity was evaluated. CFPI was purified by molecular exclusion, following by hydrophobic interaction column and showed a majoritarian peak with inhibitory activity after high resolution filtration gel column. Kinetic studies of the purified inhibitor showed a competitive¿type inhibitory activity against bovine trypsin and chymotrypsin, with an inhibition stoichiometry of 1:1 for both enzymes. The inhibition constants against trypsin and chymotrypsin were 3.3 ×10?10 and 1.5 × 10?10 M, respectively, displaying a tight binding property. SDS¿PAGE showed that CFPI has a single polypeptide chain with an apparent molecular mass of 15 kDa under non¿reducing conditions. However, MALDI¿TOF analysis demonstrated a molecular mass of 7.973 Da, suggesting that CFPI forms dimers in solution. This feature, combined with the stoichiometry of inhibition for trypsin and chymotrypsin, the inhibition constant (Ki) for both enzymes and the N-terminal sequencing, allowed classifying CFPI as a member of Bowman-Birk family inhibitors. CFPI remained stable to progressive heating for 30 min to each temperature range of 37 up to 100 °C and CD analysis exhibited no changes in spectra at 207 nm after heating at 90 °C and subsequent cooling. Moreover, CFPI was active over a wide pH range (2¿10). In contrast, reduction with DTT resulted in a loss of inhibitory activity against trypsin and chymotrypsin. CFPI also exhibited remarkable inhibitory activity against larval midgut trypsin enzymes from Anagasta kuehniella (76%), Diatraea saccharalis (59%) and Heliothis virescens (49%). Its insecticidal properties were further analysed by bioassays and confirmed by negative impact on growth of A. kuehniella and C. cephalonica. The inhibitor exhibited antinutritional effect on A. kuehniella in the F0 and F1 generations
Doutorado
Bioquimica
Doutora em Biologia Funcional e Molecular
yu-Ting, Tasi y 蔡育廷. "The Inhibition Study of the Rice Coleoptile Bowman - Birk Trypsin Inhibitor". Thesis, 2005. http://ndltd.ncl.edu.tw/handle/97114217734752156078.
Texto completo國立成功大學
化學系碩博士班
93
A 16 kDa protease inhibitor had been purified from rice coleoptiles grown in hypoxia condition. This protease inhibitor showed a competitive inhibitor toward trypsin. In order to study the optimum inhibitory ability of this protease, we had measured its activity against trypsin under various pHs and in the presence of Mg2+. It was found that under weak basic condition, it showed better activity to inhibit trypsin. To further study the effect of the presence of Mg2+, various concentration of Mg2+ were added. It was found that at pH7.8 and with the presence of 0 M, 0.5 M, 1.0 M, 1.5 M, and 2.0 M of Mg2+, the respective Ki values were 4.84 x 10-10 M, 4.56 x 10-10 M, 4.39 x 10-10 M, 3.07 x 10-10 M, and 2.45 x 10-10 M, showing that the inhibitory activity in the presence of 2.0 M Mg2+ was about twofold of that without the presence of Mg2+. By contrast, same measurements for soybean protease inhibition activity, it was found that with the increase of the concentration of Mg2+ the inhibition activity decreased with the respective Ki values were 4.21 x 10-11 M, 6.24 x 10-11 M, 8.46 x 10-11 M, 9.34 x 10-11 M, and 1.18 x 10-10 M. It was found that the secondary structures were change with the presence of 2 M of Mg2+, whereas the tertiary structure was unchanged. The fluorescence study showed that the tryptophan fluorescence intensity increased indicating that there was a micro-environmental change around the tryptophan residues. ANS fluorescence also showed there was an increase for hydrophobic area in the presence of Mg2+. The MIANS fluorescence study showed that rice protease inhibitor resulted in the increase of intensity, however, with the presence of Mg2+, the intensity decreased.
Capítulos de libros sobre el tema "Bowman-Birk inhibitor"
Kennedy, Ann R. "The Health Benefits of the Bowman-Birk Inhibitor". En Antitumor Potential and other Emerging Medicinal Properties of Natural Compounds, 183–86. Dordrecht: Springer Netherlands, 2013. http://dx.doi.org/10.1007/978-94-007-6214-5_11.
Texto completoFlecker, Peter. "Analysis of Structure-Activity Relationships of the Bowman-Birk Inhibitor of Serine Proteinases". En Protease Inhibitors as Cancer Chemopreventive Agents, 161–76. Boston, MA: Springer US, 1993. http://dx.doi.org/10.1007/978-1-4615-2882-1_9.
Texto completoBowman, Donald E. "Discovery and Background of the Bowman-Birk Protease Inhibitors". En Protease Inhibitors as Cancer Chemopreventive Agents, 93–96. Boston, MA: Springer US, 1993. http://dx.doi.org/10.1007/978-1-4615-2882-1_4.
Texto completoClemente, Alfonso, Donald MacKenzie, David Jeenes, Jenny Gee, Ian Johnson y Claire Domoney. "Anticarcinogenic Properties of Plant Protease Inhibitors from the Bowman-Birk Class". En Plant Biotechnology 2002 and Beyond, 429–31. Dordrecht: Springer Netherlands, 2003. http://dx.doi.org/10.1007/978-94-017-2679-5_89.
Texto completo"Bowman-Birk Inhibitor". En Encyclopedia of Cancer, 464. Berlin, Heidelberg: Springer Berlin Heidelberg, 2011. http://dx.doi.org/10.1007/978-3-642-16483-5_695.
Texto completoSafavi, Farinaz y Abdolmohamad Rostami. "Bowman-Birk Protease Inhibitor as a Potential Oral Therapy for Multiple Sclerosis". En Soybean - Bio-Active Compounds. InTech, 2013. http://dx.doi.org/10.5772/54066.
Texto completoKennedy, Ann R. "The Status of Human Trials Utilizing Bowman–Birk Inhibitor Concentrate from Soybeans". En SOY in Health and Disease Prevention, 207–23. CRC Press, 2005. http://dx.doi.org/10.1201/9781420026566-12.
Texto completoKennedy, Ann. "The Status of Human Trials Utilizing Bowman–Birk Inhibitor Concentrate from Soybeans". En Nutrition and Disease Prevention, 207–23. CRC Press, 2005. http://dx.doi.org/10.1201/9781420026566.ch12.
Texto completo"The Con A Conjugate of Bowman-Birk Soybean Trypsin Inhibitor is an Anticarcinogen". En Proceedings of IUB Symposium No. 144, The Seventh International Lectin Meeting Bruxelles, Belgium, August 18–23, 1985, 409–16. De Gruyter, 1986. http://dx.doi.org/10.1515/9783112315958-048.
Texto completo"Bowman‐Birk Inhibitors". En Encyclopedia of Genetics, Genomics, Proteomics and Informatics, 230. Dordrecht: Springer Netherlands, 2008. http://dx.doi.org/10.1007/978-1-4020-6754-9_1995.
Texto completoActas de conferencias sobre el tema "Bowman-Birk inhibitor"
Liu, Keshun y Mike Woolman. "Developing an optimized method for measuring chymotrypsin inhibitor activity in protein products". En 2022 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2022. http://dx.doi.org/10.21748/yucc6741.
Texto completoMeyskens, Frank L., Thomas Taylor, William Armstrong, Lorene Kong, Mai Gu, Rachel Gonzalez, Michael Villa et al. "Abstract CN02-05: Phase IIb randomized clinical chemoprevention trial of a soybean-derived compound (Bowman-Birk inhibitor concentrate) for oral leukoplakia". En Abstracts: AACR International Conference on Frontiers in Cancer Prevention Research‐‐ Nov 7-10, 2010; Philadelphia, PA. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1940-6207.prev-10-cn02-05.
Texto completoTaylor, Thomas H., Ann R. Kennedy, Marjorie Perloff y Frank L. Meyskens. "Abstract B82: Two factors contribute to negative results of a phase-IIB chemoprevention trial of Bowman-Birk inhibitor concentrate on oral leukoplakia". En Abstracts: AACR International Conference on Frontiers in Cancer Prevention Research‐‐ Oct 22-25, 2011; Boston, MA. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1940-6207.prev-11-b82.
Texto completo