Bibliografías temáticas / Bovine pancreatic ribonuclease A

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Literatura académica sobre el tema "Bovine pancreatic ribonuclease A"

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Publicado: 11 de marzo de 2023

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Artículos de revistas sobre el tema "Bovine pancreatic ribonuclease A"

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Slav�k, Tom�?, Josef Matou?ek, Josef Fulka y Ronald T. Raines. "Effect of bovine seminal ribonuclease and bovine pancreatic ribonuclease A on bovine oocyte maturation". Journal of Experimental Zoology 287, n.º 5 (2000): 394–99. http://dx.doi.org/10.1002/1097-010x(20001001)287:5<394::aid-jez7>3.0.co;2-e.

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Bello, Carlo, Adriana Lucchiari, Orfeo Buso y Mauro Tonellato. "Semisynthetic studies on bovine pancreatic ribonuclease". International Journal of Peptide and Protein Research 23, n.º 1 (12 de enero de 2009): 61–71. http://dx.doi.org/10.1111/j.1399-3011.1984.tb02693.x.

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Jeremy Johnson, R., Mary Andorfer, Ashton Chaffee, Melanie Clark, Nathan Clarke, Grace Douglass, Elizabeth Ellis et al. "Proteopedia entry: Bovine pancreatic ribonuclease a". Biochemistry and Molecular Biology Education 40, n.º 1 (26 de noviembre de 2011): 75. http://dx.doi.org/10.1002/bmb.20568.

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Ye, X. Y. y T. B. Ng. "First demonstration of lactoribonuclease, a ribonuclease from bovine milk with similarity to bovine pancreatic ribonuclease". Life Sciences 67, n.º 16 (septiembre de 2000): 2025–32. http://dx.doi.org/10.1016/s0024-3205(00)00784-0.

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Tarragona-Fiol, A., C. J. Taylorson y B. R. Rabin. "Cloning and Expression of An Engineered Human Pancreatic Ribonuclease". Protein & Peptide Letters 1, n.º 2 (septiembre de 1994): 76–83. http://dx.doi.org/10.2174/0929866501666220424121436.

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The coding sequence for the human pancreatic ribonuclease (HP-RNase) gene has been obtained from genomic DNA extracted from buccal epithelial cells. In order to direct the expression of the recombinant human pancreatic enzyme to the periplasmic space of E.coli, the bovine pancreatic RNase signal sequence has been fused 5' to the human gene. Initial attempts to express the recombinant enzyme were not successful, consequently site-directed mutagenesis tehniques were used to genetically engineer the HP-RNase gene to enable expression in E.coli. The resultant engineered enzyme shows similar kinetic characteristics to the homologous bovine enzyme.
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6

RAMNATH, S. y PAUL J. VITHAYATHIL. "IRREVERSIBLE THERMAL DENATURATION OF BOVINE PANCREATIC RIBONUCLEASE-A". International Journal of Peptide and Protein Research 17, n.º 1 (12 de enero de 2009): 107–17. http://dx.doi.org/10.1111/j.1399-3011.1981.tb01973.x.

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Fedorov, Alexander A., Diane Joseph-McCarthy, Elena Fedorov, Dora Sirakova, Isaac Graf y Steven C. Almo. "Ionic Interactions in Crystalline Bovine Pancreatic Ribonuclease A†,‡". Biochemistry 35, n.º 50 (enero de 1996): 15962–79. http://dx.doi.org/10.1021/bi961533g.

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Leich, Franziska, Jens Köditz, Renate Ulbrich-Hofman y Ulrich Arnold. "Tandemization Endows Bovine Pancreatic Ribonuclease with Cytotoxic Activity". Journal of Molecular Biology 358, n.º 5 (mayo de 2006): 1305–13. http://dx.doi.org/10.1016/j.jmb.2006.03.007.

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Matousek, Josef, Josef Soucek, Jan Riha, Todd R. Zankel y Steven A. Benner. "Immunosuppressive activity of angiogenin in comparison with bovine seminal ribonuclease and pancreatic ribonuclease". Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology 112, n.º 2 (octubre de 1995): 235–41. http://dx.doi.org/10.1016/0305-0491(95)00075-5.

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NAMBIAR, Krishnan P., Joseph STACKHOUSE, Scott R. PRESNELL y Steven A. BENNER. "Expression of bovine pancreatic ribonuclease A in Escherichia coli". European Journal of Biochemistry 163, n.º 1 (febrero de 1987): 67–71. http://dx.doi.org/10.1111/j.1432-1033.1987.tb10737.x.

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Tesis sobre el tema "Bovine pancreatic ribonuclease A"

1

Chatani, Eri. "The Structural Basis for the Functionality and Stability of Bovine Pancreatic Ribonuclease A". Kyoto University, 2002. http://hdl.handle.net/2433/149886.

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Kyoto University (京都大学)
0048
新制・課程博士
博士(農学)
甲第9594号
農博第1222号
新制||農||840(附属図書館)
学位論文||H14||N3626(農学部図書室)
UT51-2002-G352
京都大学大学院農学研究科応用生命科学専攻
(主査)教授 林 力丸, 教授 關谷 次郎, 教授 西岡 孝明
学位規則第4条第1項該当
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2

Fujii, Takahiro. "Studies of structural formation of bovine pancreatic ribonuclease A : Role of the carboxyl terminal region". Kyoto University, 2000. http://hdl.handle.net/2433/151623.

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本文データは平成22年度国立国会図書館の学位論文(博士)のデジタル化実施により作成された画像ファイルを基にpdf変換したものである
Kyoto University (京都大学)
0048
新制・課程博士
博士(農学)
甲第8628号
農博第1155号
新制||農||814(附属図書館)
学位論文||H12||N3473(農学部図書室)
UT51-2000-R34
京都大学大学院農学研究科応用生命科学専攻
(主査)教授 林 力丸, 教授 清水 昌, 教授 岩村 俶
学位規則第4条第1項該当
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Tanimizu, Naoki. "Conformational properties of amino acid residues in the active site of bovine pancreatic ribonuclease A". Kyoto University, 1999. http://hdl.handle.net/2433/181366.

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Kyoto University (京都大学)
0048
新制・課程博士
博士(農学)
甲第7960号
農博第1069号
新制||農||785(附属図書館)
学位論文||H11||N3294(農学部図書室)
UT51-99-M265
京都大学大学院農学研究科農芸化学専攻
(主査)教授 林 力丸, 教授 池田 篤治, 教授 岩村 俶
学位規則第4条第1項該当
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4

Council, Claire E. "Evaluation of sequential chemoselective peptide ligation and molecular dynamics simulations as tools for the total synthesis of proteins: an example using bovine pancreatic ribonuclease A". Thesis, University of Surrey, 2013. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.583341.

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Chemoselective ligation between two peptides can be used to produce synthetic peptides and proteins that cannot easily be synthesised as single peptides by solid phase peptide synthesis. Chemoselective reaction between an aldehyde and hydrazine or hydroxylamine, masking the aldehyde as a 1, 2-amino alcohol, has been investigated as a method of sequential ligation that will allow synthesis of individual peptides in high yield and purity, enabling more than two peptides to be ligated. Protected amino acids were used as precursors for the synthesis of 1, 2-amino alcohol derivatives that could be used in solid phase peptide synthesis for the production of peptides bearing a C-terminal 1, 2-amino alcohol, as a masked aldehyde for use in ligation reactions. Limitations of this method led to alternative investigations, using peptides bearing an N-terminal serine as a masked aldehyde, and a C-terminal hydrazide. Bovine pancreatic ribonuclease A was chosen as an example protein for sequential ligation and using this method, peptides were synthesised in high yield and purity for use in ligation reactions. Trial ligation reactions with short test peptides were performed successfully, however problems were experienced during ligations using peptide fragments of ribunuclease due to involvement of the cysteine side chains. Methods to overcome these unwanted reactions resulted in insoluble peptide fragments. Computer modelling using molecular dynamics simulations has been used to investigate the effect of replacing native peptide bonds in ribonuclease on the structure of the protein. The method of molecular dynamics simulation was validated through comparison of the structure of a mutant of ribonuclease from experimental NMR data to the structure produced after a molecular dynamics simulation. Results of the modelling simulations suggest that replacement of native peptide bonds with the chemoselective bond formed through reaction of an aldehyde and hydrazine will have only minor implications for the structure of ribonuclease, and therefore should only have a small impact on enzyme activity .
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5

Alade, Ayoade Nathaniel. "Investigating the Catalytic Role of Lysine Residue 41 in Pancreatic Ribonuclease A". Thesis, California State University, Long Beach, 2017. http://pqdtopen.proquest.com/#viewpdf?dispub=10603029.

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Understanding enzyme catalysis is one of the major goals in biology. Ribonuclease A (RNase A) is a key system to understanding protein structure and function provides an attractive system to investigate the catalytic role of active site interactions. Crystal structures show a lysine residue (Lys41) situated in the RNase A active site, and mutagenesis studies suggest this residue is important for catalysis. To evaluate the catalytic importance of the Lys41-phosphate interaction, double mutant cycle analysis was used. Individual mutation of lysine to arginine (K41R) and substitution of a phosphate oxygen with sulfur led to ∼350 and ∼100-fold decrease in kcat/KM, respectively. However, in the K41R background, substitution of the same oxygen with sulfur decreased activity by a similar amount (within 2-fold) as it did with the wild-type enzyme. This result provides evidence that functional interaction between Lys41 and the phosphate backbone of RNA substrates may not be solely limited between the two groups.

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6

Bertrand, Jay Aaron. "X-ray crystal structures of inhibited bovine pancreatic trypsin". Diss., Georgia Institute of Technology, 1994. http://hdl.handle.net/1853/27321.

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Yuan, Chunhua. "Structural and conformational studies of bovine pancreatic phospholipase A2 /". The Ohio State University, 1997. http://rave.ohiolink.edu/etdc/view?acc_num=osu1487948807588005.

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Doherty, Aidan Joseph. "Studies on the sequence-selective nuclease, bovine pancreatic DNase I". Thesis, University of Southampton, 1992. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.359221.

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Tan, Kok Leong. "Protein engineering of bovine pancreatic deoxyribonuclease I by secreation of polypeptide elements". Thesis, University of Newcastle Upon Tyne, 1999. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.285799.

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Dupureur, Cynthia M. "Structure-function studies in the active site of bovine pancreatic phospholipase A2 /". The Ohio State University, 1992. http://rave.ohiolink.edu/etdc/view?acc_num=osu1487775034179833.

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Libros sobre el tema "Bovine pancreatic ribonuclease A"

1

Trautwein-Fritz, Katrin. Construction of an improved expression system for bovine pancreatic ribonuclease A and construction and characterization of RNase A mutants. Konstanz: Hartung-Gorre, 1992.

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Turner, Paul Michael. The interaction of Porcine Thyroid Ribonuclease Inhibitor with Pancreatic Ribonuclease A and Porcine Thyroid Alkaline Ribonuclease. 1985.

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Capítulos de libros sobre el tema "Bovine pancreatic ribonuclease A"

1

Schomburg, Dietmar y Margit Salzmann. "Pancreatic ribonuclease". En Enzyme Handbook 3, 909–15. Berlin, Heidelberg: Springer Berlin Heidelberg, 1991. http://dx.doi.org/10.1007/978-3-642-76463-9_191.

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Mazzarella, L., L. Vitagliano, A. Zagari y S. Capasso. "Subunit Assembly in Bovine Seminal Ribonuclease". En Topics in Molecular Organization and Engineering, 301–12. Dordrecht: Springer Netherlands, 1994. http://dx.doi.org/10.1007/978-94-011-0822-5_28.

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Warshaw, A. L. "Serum Ribonuclease for Detecting Pancreatic Cell Necrosis". En Acute Pancreatitis, 154–58. Berlin, Heidelberg: Springer Berlin Heidelberg, 1987. http://dx.doi.org/10.1007/978-3-642-83027-3_20.

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Al-Hamidi, A. A. A., M. A. S. Al-Tufail y G. S. Bailey. "Bovine Pancreatic Kallikrein: Purification and Radioimmunoassay". En Recent Progress on Kinins, 121–28. Basel: Birkhäuser Basel, 1992. http://dx.doi.org/10.1007/978-3-0348-7321-5_16.

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Di Donato, A., V. Cafaro, M. De Nigris, G. Minopoli y G. D’Alessio. "Engineering of Bovine Seminal Ribonuclease: Expression of the Secreted Recombinant Protein". En Topics in Molecular Organization and Engineering, 187–92. Dordrecht: Springer Netherlands, 1994. http://dx.doi.org/10.1007/978-94-011-0822-5_15.

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Levitt, Michael y Ruth Sharon. "Simulating Protein Dynamics in Solution: Bovine Pancreatic Trypsin Inhibitor". En Crystallography in Molecular Biology, 197–205. Boston, MA: Springer US, 1987. http://dx.doi.org/10.1007/978-1-4684-5272-3_17.

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Picone, Delia, Antonello Merlino y Roberta Spadaccini. "Bovine Seminal Ribonuclease and Its Special Features: When Two is Better Than One". En Antitumor Potential and other Emerging Medicinal Properties of Natural Compounds, 93–113. Dordrecht: Springer Netherlands, 2013. http://dx.doi.org/10.1007/978-94-007-6214-5_7.

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Levitt, M. "A Calculated Conformation for the Folding Transition State of Bovine Pancreatic Trypsin Inhibitor". En Protein Structure and Protein Engineering, 45–50. Berlin, Heidelberg: Springer Berlin Heidelberg, 1988. http://dx.doi.org/10.1007/978-3-642-74173-9_5.

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Lozzi, L., M. Corti, N. Niccolai, M. Rustici, P. Neri y P. A. Temussi. "Synthesis and purification of site-specific peptide conjugated to bovine pancreatic trypsin inhibitor". En Peptides 1990, 830–31. Dordrecht: Springer Netherlands, 1991. http://dx.doi.org/10.1007/978-94-011-3034-9_342.

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Kemmink, Johan y Thomas E. Creighton. "Preferred Local Conformations of Peptides comprising the Entire Sequence of Bovine Pancreatic Trypsin Inhibitor (BPTI) and their Roles in Protein Folding". En Biological Membranes: Structure, Biogenesis and Dynamics, 139–53. Berlin, Heidelberg: Springer Berlin Heidelberg, 1994. http://dx.doi.org/10.1007/978-3-642-78846-8_14.

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Actas de conferencias sobre el tema "Bovine pancreatic ribonuclease A"

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Castro, J., A. Benito, M. Vilanova, M. Ribó, G. Tornillo y MJ Smalley. "PO-427 A nuclear-directed human pancreatic ribonuclease variant is cytotoxic for breast cancer cells cultured in 3D and kills cancer stem cells". En Abstracts of the 25th Biennial Congress of the European Association for Cancer Research, Amsterdam, The Netherlands, 30 June – 3 July 2018. BMJ Publishing Group Ltd, 2018. http://dx.doi.org/10.1136/esmoopen-2018-eacr25.453.

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Baba, Waqas y Sajid Maqsood. "Novel antihypertensive and anticholesterolemic peptides from peptic hydrolysates of camel whey proteins". En 2022 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2022. http://dx.doi.org/10.21748/qecs2081.

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Hypercholesterolemia and hypertension are major growing concerns that are managed by drugs that inhibit various metabolic enzymes. Milk hydrolysates have been reported to contain various bioactive peptides (BAP) that can inhibit various metabolic enzymes for enhancing human health. As such camel whey proteins were subjected to peptic hydrolysis using a full factorial model (33) with hydrolysis time, temperature, and enzyme concentration as factors. The resulting hydrolysates were analyzed for anti-hypercholesterolemic and hypertensive properties by studying the in vitro inhibition of various enzymatic markers. The hydrolysates with lowest IC50 values were further subjected to LC-MS-QTOF that revealed presence of 185 peptides. Selected peptides that had Peptide Ranker Score greater than 0.8 were further studied for prediction of possible interactions with enzyme markers: pancreatic lipase (PL) cholesterol esterase (CE) and angiotensin converting enzyme (ACE) using in silico analysis. The data generated suggested that most of the peptides could bind active site of PL while as only three peptides could bind active site of CE. Based on higher number of reactive residues in the bioactive peptides (BAP) and greater number of substrate binding sites, FCCLGPVPP was identified as potential CE inhibitory peptide while PAGNFLPPVAAAPVM, MLPLMLPFTMGY, and LRFPL were identified as PL inhibitors. While peptides PAGNFLP, FCCLGPVPP, PAGNFLMNGLMHR, PAVACCLPPLPCHM were identified as potential ACE inhibitors. Molecular docking of selected peptides showed hydrophilic and hydrophobic interactions between peptides and target enzymes. Moreover, due to the importance of renin in managing hypertension, peptides from hydrolysates with high ACE inhibiting potential were predicted for potential to interact with renin using in silico analysis. Molecular docking was subsequently employed to identify how the identified peptides, PVAAAPVM and LRPFL, could interact with renin and potentially inhibit it. Thus, non-bovine (camel) whey hydrolysates might be used as functional ingredients for production of functional foods with antihypertensive and anticholesterolemic properties.
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Skriver, L., L. C. Petersen, L. R. Lund, L. S. Nielsen y K. Danø. "SINGLE-CHAIN UROKINASE TYPE PLASMINOGEN ACTIVATOR (SCU-PA) FROM HT-1080 HUMAN FIBROSARCOMA CELLS IS A GENUINE PROENZYME". En XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644394.

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U-PA is released from many cells as a single polypeptide chain (scu-PA) that is converted into its active two-chain form (tcu-PA) by limited proteolysis with plasmin. There is general agreement that scu-PA has an extremely low amidolytic activity, but different oppinions exist, as to whether scu-PA itself can activate plasminogen. We have reinvestigated the plasminogen activating activity of our scu-PA preparations by means of a direct [125]I-plasminogen conversion assay and two amidolytic assays for plasmin and u-PA activity. In the [125]I-plasminogen conversion assay in the presence of bovine pancreatic trypsin inhibitor (BPTI) the subsequent plasmin catalyzed conversion of scu-PA is blocked while the plasminogen activation is unaffected. In this assay with 3oo nM Glu-plasminogen and 15 pM BPTI, 4o nM scu-PA caused a low but significant plasminogen conversion, which could be fully inhibited by pretreatment of scu-PA with diisopropylfluorophos-phate (DFP). DFP-treated scu-PA was convertible to fully active tcu-PA. Rates of plasminogen activation in this type of assay for scu-PA activity was at least 4oo fold slower than that measured for tcu-PA. A coupled amidolytic assay with Lys-plasminogen, scuPA or tcu-PA, BPTI, and the high affinity plasmin substrate H-D-Val-Phe-LyspNA (S2390) was performed under conditions that ensures a low steady state concentration of free plasmin. In this assay the initial rate of Lys-plasminogen activation by DFP-treated scu-PA was at least 25o fold slower than that measured for tcu-PA. Finally, u-PA activity was measured in an assay with the chromogenic substrate <Glu-Gly-ArgpNA (S2444) (o.8mM) in the presence of highly purified Glu-plasminogen (3oonM) and DFP-treated scu-PA (2nM) in the absence of BPTI. Within the initial 15 min of incubation no detectable hydrolysis of S2444 occurred. Addition of tcu-PA (2pM) or plasmin (o.lnM) to the scu-PA/Glu-plasminogen mixture caused a significant reduction of the lag period before onset of the cascade reaction leading to scu-PA conversion and subsequent hydrolysis of S2444. We conclude that the low rates of plasminogen activation measured in these assays by scu-PA might be accounted for by the presence of trace amounts of tcu-PA in the scu-PA preparations, and that scu-PA meets the requirements for a genuine proenzyme
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