Relevant bibliographies by topics / Amidase

Contents

  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers
  6. Reports

Academic literature on the topic 'Amidase'

Author: Grafiati
Published: 4 June 2021
Last updated: 11 September 2023

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Journal articles on the topic "Amidase"

1

Soong, Chee-Leong, Jun Ogawa, and Sakayu Shimizu. "A Novel Amidase (Half-Amidase) for Half-Amide Hydrolysis Involved in the Bacterial Metabolism of Cyclic Imides." Applied and Environmental Microbiology 66, no. 5 (2000): 1947–52. http://dx.doi.org/10.1128/aem.66.5.1947-1952.2000.

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ABSTRACT A novel amidase involved in bacterial cyclic imide metabolism was purified from Blastobacter sp. strain A17p-4. The enzyme physiologically functions in the second step of cyclic imide degradation, i.e., the hydrolysis of monoamidated dicarboxylates (half-amides) to dicarboxylates and ammonia. Enzyme production was enhanced by cyclic imides such as succinimide and glutarimide but not by amide compounds which are conventional substrates and inducers of known amidases. The purified amidase showed high catalytic efficiency toward half-amides such as succinamic acid (Km = 6.2 mM; k cat = 5
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Trott, Sandra, Sibylle Bürger, Carsten Calaminus, and Andreas Stolz. "Cloning and Heterologous Expression of an Enantioselective Amidase from Rhodococcus erythropolis Strain MP50." Applied and Environmental Microbiology 68, no. 7 (2002): 3279–86. http://dx.doi.org/10.1128/aem.68.7.3279-3286.2002.

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ABSTRACT The gene for an enantioselective amidase was cloned from Rhodococcus erythropolis MP50, which utilizes various aromatic nitriles via a nitrile hydratase/amidase system as nitrogen sources. The gene encoded a protein of 525 amino acids which corresponded to a protein with a molecular mass of 55.5 kDa. The deduced complete amino acid sequence showed homology to other enantioselective amidases from different bacterial genera. The nucleotide sequence approximately 2.5 kb upstream and downstream of the amidase gene was determined, but no indications for a structural coupling of the amidase
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Bhalla, Tek Chand, and Harish Kumar. "Nocardia globerula NHB-2: a versatile nitrile-degrading organism." Canadian Journal of Microbiology 51, no. 8 (2005): 705–8. http://dx.doi.org/10.1139/w05-046.

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A versatile nitrile-degrading bacterium was isolated by enrichment culture from the soil of a forest near Manali, Himachal Pradesh, India, and was identified as Nocardia globerula. This organism contains 3 enzymes with nitrile-degrading activity: nitrilase, nitrile hydratase, and amidase. Nocardia globerula NHB-2 cells grown on nutrient broth supplemented with 1% glucose and 0.1% yeast extract exhibited nitrile hydratase–amidase activity specific for saturated aliphatic nitriles or amide, while addition of acetonitrile in nutrient broth yielded cells with nitrile hydratase–amidase that in addi
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Sonke, Theo, Sandra Ernste, Renate F. Tandler, et al. "l-Selective Amidase with Extremely Broad Substrate Specificity from Ochrobactrum anthropi NCIMB 40321." Applied and Environmental Microbiology 71, no. 12 (2005): 7961–73. http://dx.doi.org/10.1128/aem.71.12.7961-7973.2005.

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ABSTRACT An industrially attractive l-specific amidase was purified to homogeneity from Ochrobactrum anthropi NCIMB 40321 wild-type cells. The purified amidase displayed maximum initial activity between pH 6 and 8.5 and was fully stable for at least 1 h up to 60°C. The purified enzyme was strongly inhibited by the metal-chelating compounds EDTA and 1,10-phenanthroline. The activity of the EDTA-treated enzyme could be restored by the addition of Zn2+ (to 80%), Mn2+ (to 400%), and Mg2+ (to 560%). Serine and cysteine protease inhibitors did not influence the purified amidase. This enzyme displaye
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Martinez-Rodríguez, Sergio, Rafael Contreras-Montoya, Jesús M. Torres, Luis Álvarez de Cienfuegos, and Jose Antonio Gavira. "A New L-Proline Amide Hydrolase with Potential Application within the Amidase Process." Crystals 12, no. 1 (2021): 18. http://dx.doi.org/10.3390/cryst12010018.

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L-proline amide hydrolase (PAH, EC 3.5.1.101) is a barely described enzyme belonging to the peptidase S33 family, and is highly similar to prolyl aminopeptidases (PAP, EC. 3.4.11.5). Besides being an S-stereoselective character towards piperidine-based carboxamides, this enzyme also hydrolyses different L-amino acid amides, turning it into a potential biocatalyst within the Amidase Process. In this work, we report the characterization of L-proline amide hydrolase from Pseudomonas syringae (PsyPAH) together with the first X-ray structure for this class of L-amino acid amidases. Recombinant PsyP
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NOVO, Carlos, Sebastien FARNAUD, Renée TATA, Alda CLEMENTE, and Paul R. BROWN. "Support for a three-dimensional structure predicting a Cys-Glu-Lys catalytic triad for Pseudomonas aeruginosa amidase comes from site-directed mutagenesis and mutations altering substrate specificity." Biochemical Journal 365, no. 3 (2002): 731–38. http://dx.doi.org/10.1042/bj20011714.

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The aliphatic amidase from Pseudomonas aeruginosa belongs to the nitrilase superfamily, and Cys166 is the nucleophile of the catalytic mechanism. A model of amidase was built by comparative modelling using the crystal structure of the worm nitrilase—fragile histidine triad fusion protein (NitFhit; Protein Data Bank accession number 1EMS) as a template. The amidase model predicted a catalytic triad (Cys-Glu-Lys) situated at the bottom of a pocket and identical with the presumptive catalytic triad of NitFhit. Three-dimensional models for other amidases belonging to the nitrilase superfamily also
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Fournand, David, Frederic Bigey, and Alain Arnaud. "Acyl Transfer Activity of an Amidase from Rhodococcussp. Strain R312: Formation of a Wide Range of Hydroxamic Acids." Applied and Environmental Microbiology 64, no. 8 (1998): 2844–52. http://dx.doi.org/10.1128/aem.64.8.2844-2852.1998.

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ABSTRACT The enantioselective amidase from Rhodococcus sp. strain R312 was produced in Escherichia coli and was purified in one chromatographic step. This enzyme was shown to catalyze the acyl transfer reaction to hydroxylamine from a wide range of amides. The optimum working pH values were 7 with neutral amides and 8 with α-aminoamides. The reaction occurred according to a Ping Pong Bi Bi mechanism. The kinetic constants demonstrated that the presence of a hydrophobic moiety in the carbon side chain considerably decreased the K m amide values (e.g.,K m amide = 0.1 mM for butyramide, isobutyra
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Bury-Moné, Stéphanie, Stéphane Skouloubris, Catherine Dauga, et al. "Presence of Active Aliphatic Amidases in Helicobacter Species Able To Colonize the Stomach." Infection and Immunity 71, no. 10 (2003): 5613–22. http://dx.doi.org/10.1128/iai.71.10.5613-5622.2003.

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ABSTRACT Ammonia production is of great importance for the gastric pathogen Helicobacter pylori as a nitrogen source, as a compound protecting against gastric acidity, and as a cytotoxic molecule. In addition to urease, H. pylori possesses two aliphatic amidases responsible for ammonia production: AmiE, a classical amidase, and AmiF, a new type of formamidase. Both enzymes are part of a regulatory network consisting of nitrogen metabolism enzymes, including urease and arginase. We examined the role of the H. pylori amidases in vivo by testing the gastric colonization of mice with H. pylori SS1
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Uchiyama, Taku, and Kentaro Miyazaki. "Product-Induced Gene Expression, a Product-Responsive Reporter Assay Used To Screen Metagenomic Libraries for Enzyme-Encoding Genes." Applied and Environmental Microbiology 76, no. 21 (2010): 7029–35. http://dx.doi.org/10.1128/aem.00464-10.

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ABSTRACT A reporter assay-based screening method for enzymes, which we named product-induced gene expression (PIGEX), was developed and used to screen a metagenomic library for amidases. A benzoate-responsive transcriptional activator, BenR, was placed upstream of the gene encoding green fluorescent protein and used as a sensor. Escherichia coli sensor cells carrying the benR-gfp gene cassette fluoresced in response to benzoate concentrations as low as 10 μM but were completely unresponsive to the substrate benzamide. An E. coli metagenomic library consisting of 96,000 clones was grown in 96-w
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TSUBOI, Kazuhito, Christine HILLIGSMANN, Séverine VANDEVOORDE, Didier M. LAMBERT, and Natsuo UEDA. "N-Cyclohexanecarbonylpentadecylamine: a selective inhibitor of the acid amidase hydrolysing N-acylethanolamines, as a tool to distinguish acid amidase from fatty acid amide hydrolase." Biochemical Journal 379, no. 1 (2004): 99–106. http://dx.doi.org/10.1042/bj20031695.

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Anandamide (N-arachidonoylethanolamine) and other bioactive N-acylethanolamines are degraded to their corresponding fatty acids and ethanolamine. This hydrolysis is mostly attributed to catalysis by FAAH (fatty acid amide hydrolase), which exhibits an alkaline pH optimum. In addition, we have identified another amidase which catalyses the same reaction exclusively at acidic pH values [Ueda, Yamanaka and Yamamoto (2001) J. Biol. Chem. 276, 35552–35557]. In attempts to find selective inhibitors of this acid amidase, we screened various derivatives of palmitic acid, 1-hexadecanol, and 1-pentadecy
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Dissertations / Theses on the topic "Amidase"

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Capo, Florence. "Détection et régulation du peptidoglycane lors de la réponse antibactérienne chez la Drosophile." Thesis, Aix-Marseille, 2017. http://www.theses.fr/2017AIXM0448/document.

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Les interactions cellules épithéliales-bactéries peuvent conduire à l'établissement d'une tolérance vis-à-vis des bactéries commensales ou à l’élimination des bactéries pathogènes par le système immunitaire. La détection des bactéries est une étape indispensable à l’orientation de cette réponse. Contrairement aux mammifères, la reconnaissance des bactéries chez la drosophile repose principalement sur la détection d’un composant de la paroi bactérienne, le peptidoglycane (PG), par une famille de récepteurs, les "PeptidoGlycan Recognition Receptors" (PGRPs). Chez la drosophile, le PG des bactéri
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Mahenthiralingam, Eshwar. "The amidase promotor of Mycobacterium smegmatis." Thesis, Open University, 1990. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.278899.

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Hendil-Forssell, Peter. "Rational engineering of esterases for improved amidase specificity in amide synthesis and hydrolysis." Doctoral thesis, KTH, Industriell bioteknologi, 2016. http://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-196892.

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Biocatalysis is an ever evolving field that uses enzymes or microorganisms for chemical synthesis. By utilizing enzymes that generally have evolved for specific reactions under mild conditions and temperatures, biocatalysis can be a more environmentally friendly option compared to traditional chemistry. Amide-type chemistries are important and bond formation avoiding poor atom economy is of high priority in organic chemistry. Biocatalysis could potentially be a solution but restricted substrate scope is a limitation. Esterases/lipases usually display broad substrate scope and catalytic promisc
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Mobbs, George. "Structural studies on glutamine de-amidase enzymes." Thesis, University of Sheffield, 2014. http://etheses.whiterose.ac.uk/8549/.

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Nojiri, Masutoshi. "Studies on enzymatic synthesis of optically active amides for pharmaceutical intermediates." Kyoto University, 2018. http://hdl.handle.net/2433/232150.

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Du, Preez Ryne. "Development of a membrane immobilised amidase bioreactor system." Thesis, Link to the online version, 2008. http://hdl.handle.net/10019/1996.

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Harding, Ross Lyndon. "Molecular studies on N-Acetylmuramyl-L-alanine amidase." Thesis, University of Southampton, 2001. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.482122.

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Hope, Matthew. "Mandelamide hydrolose structural studies of a novel amidase /." Waltham, Mass. : Brandeis University, 2009. http://dcoll.brandeis.edu/handle/10192/23237.

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Kerridge, Alison P. "The microbial biotransformation of nitrile compounds." Thesis, University of Exeter, 1995. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.262431.

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Silman, Nigel James. "Physiology and biochemistry of amidase production by Methylophilus methylotrophus." Thesis, University of Leicester, 1990. http://hdl.handle.net/2381/35151.

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The physiological regulation of amidase production by Methylophilus methylotrophus was studied following growth of the organism under various conditions of nutrient sufficiency and limitation in batch, fed-batch and continuous cultures. Amidase was severely repressed by ammonia, and was induced by short chain aliphatic amides. Growth of the wild-type organism in acetamide-1imited continuous culture led to the selection of a hyperactive strain , the subsequent growth of which under acrylamide limitation led to the production of another strain (MM8) which exhibited even higher activities. Chemic
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Books on the topic "Amidase"

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Arthur, Greenberg, Breneman Curt M, and Liebman Joel F, eds. The amide linkage: Structural significance in chemistry, biochemistry, and materials science. Wiley-Interscience, 2003.

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Watson, Jude. Queen Amidala. Scholastic, 1999.

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Sentā, Aichi-ken Maizō Bunkazai. Amidaji iseki. Aichi-ken Maizō Bunkazai Sentā, 1990.

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Trangmar, Susan. Amidst. Dash Gallery, 1994.

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Robinson, Lisa Beth. Amidah. Somnambulist Tango Press, 2013.

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Iinkai, Shizuoka-shi Kyōiku. Mokuzō amida nyorai zazō hozon shūri hōkokusho: Shizuoka-shi shitei yūkei bunkazai Matsuno amidadō butsuzōgun. Shizuoka-shi Kyōiku Iinkai, 2002.

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Rojano, Guillermo Fernández. Por amor de las amidas. Ayuntamiento de Jaén, Concejalía de Cultura y Turismo, Servicio de Publicaciones, 1993.

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Arthur, Greenberg, Breneman Curt M, and Liebman Joel F, eds. The amide linkage: Selected structural aspects in chemistry, biochemistry, and materials science. Wiley-Interscience, 2000.

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Sentā, Aichi-ken Maizō Bunkazai. Ōbuchi Iseki, Amidaji Iseki. Aichi-ken Maizō Bunkazai Sentā, 1988.

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Tōdaiji betsuin Suō Amidaji. Amidaji, 1986.

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Book chapters on the topic "Amidase"

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Schomburg, Dietmar, and Margit Salzmann. "Amidase." In Enzyme Handbook 4. Springer Berlin Heidelberg, 1991. http://dx.doi.org/10.1007/978-3-642-84437-9_122.

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Schomburg, Dietmar, and Margit Salzmann. "Omega-amidase." In Enzyme Handbook 4. Springer Berlin Heidelberg, 1991. http://dx.doi.org/10.1007/978-3-642-84437-9_121.

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Schomburg, Dietmar, and Margit Salzmann. "Penicillin amidase." In Enzyme Handbook 4. Springer Berlin Heidelberg, 1991. http://dx.doi.org/10.1007/978-3-642-84437-9_129.

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Schomburg, Dietmar, and Margit Salzmann. "Acylagmatine amidase." In Enzyme Handbook 4. Springer Berlin Heidelberg, 1991. http://dx.doi.org/10.1007/978-3-642-84437-9_156.

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Schomburg, Dietmar, and Margit Salzmann. "Nicotinamide-nucleotide amidase." In Enzyme Handbook 4. Springer Berlin Heidelberg, 1991. http://dx.doi.org/10.1007/978-3-642-84437-9_158.

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Schomburg, Dietmar, and Ida Schomburg. "(R)-amidase 3.5.1.100." In Class 3.4–6 Hydrolases, Lyases, Isomerases, Ligases. Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-36260-6_11.

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Schomburg, Dietmar, and Dörte Stephan. "N-Carbamoylsarcosine amidase." In Enzyme Handbook 16. Springer Berlin Heidelberg, 1998. http://dx.doi.org/10.1007/978-3-642-58903-4_104.

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Schomburg, Dietmar, and Dörte Stephan. "N-Carbamoylputrescine amidase." In Enzyme Handbook 16. Springer Berlin Heidelberg, 1998. http://dx.doi.org/10.1007/978-3-642-58903-4_98.

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Schomburg, Dietmar, and Margit Salzmann. "N-Acetylmuramoyl-L-alanine amidase." In Enzyme Handbook 4. Springer Berlin Heidelberg, 1991. http://dx.doi.org/10.1007/978-3-642-84437-9_146.

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Schomburg, Dietmar, and Dörte Stephan. "D-Benzoylarginine-4-nitroanilide amidase." In Enzyme Handbook 16. Springer Berlin Heidelberg, 1998. http://dx.doi.org/10.1007/978-3-642-58903-4_117.

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Conference papers on the topic "Amidase"

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Nanì, MariaFrancesca, Giuseppe Lucariello, Ester Pagano, et al. "N-Acylethanolamine acid amidase (NAAA) inhibition rescues intestinal fibrosis through IL-23 pathway." In 50. Jahrestagung der Gesellschaft für Gastroenterologie in Bayern e.V. Georg Thieme Verlag, 2023. http://dx.doi.org/10.1055/s-0043-1764094.

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Nanì, MariaFrancesca, Giuseppe Lucariello, Ester Pagano, et al. "N-Acylethanolamine acid amidase (NAAA) inhibition rescues intestinal fibrosis through IL-23 pathway." In 50. Jahrestagung der Gesellschaft für Gastroenterologie in Bayern e.V. Georg Thieme Verlag, 2023. http://dx.doi.org/10.1055/s-0043-1764100.

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Silva, N. A. F., D. Gil, A. Karmali, and M. Matos. "Potentiometric biosensor for acrylamide determination in wastewater using wild type amidase fromPseudomonas aeruginosa." In WASTE MANAGEMENT 2008. WIT Press, 2008. http://dx.doi.org/10.2495/wm080801.

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Scalvini, Laura, Marco Mor, Andrea Ghidini, et al. "Molecular modelling studies on PEA hydrolysis by the enzyme <em>N</em>-acylethanolamine acid amidase." In 7th International Electronic Conference on Medicinal Chemistry. MDPI, 2021. http://dx.doi.org/10.3390/ecmc2021-11515.

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Fujikawa, K., T. Funakoshi, J. F. Tait, and R. L. Heimark. "PLACENTAL ANTICOAGULANT PROTEIN." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643912.

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An anticoagulant protein was purified from the soluble fraction of human placenta by ammonium sulfate precipitation and column chromatography on DEAE-Sepharose, Sephadex G-75, and mono S (Pharmacia). Approximately 30 mg of the protein was purified from one placenta. The purified protein gave a single band on SDS polyacrylamide gel and had a molecular weight of 36,500. This protein inhibited both kaolin and thromboplastin induced clotting times of normal human plasma. It also inhibited the clotting time of platelet-rich plasma induced by factor Xa, but did not affect thrombin activity of fibrin
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Maxman, Tobaron. "Amidah." In ACM SIGGRAPH ASIA 2009 Art Gallery & Emerging Technologies: Adaptation. ACM Press, 2009. http://dx.doi.org/10.1145/1665137.1665162.

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Nettleton, Donna, and Richard Groenwald. "AMIDARS Flight Performance." In 32nd Annual Technical Symposium, edited by Paul A. Henkel, Francis R. LaGesse, and Wayne W. Schurter. SPIE, 1989. http://dx.doi.org/10.1117/12.948609.

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Ishio, Takashi, Yui Watanabe, and Katsuro Inoue. "AMIDA." In Companion of the 13th international conference. ACM Press, 2008. http://dx.doi.org/10.1145/1370175.1370212.

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Wagner, Fred W. "Recombinant production of amidated peptides." In Future Aspect in Peptide Chemistry - Ringberg Conference. Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, 1999. http://dx.doi.org/10.1135/css199901147.

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Romans, Nance C. "Amidars High-Performance, Real-Time Display." In 33rd Annual Techincal Symposium, edited by Paul A. Henkel, Francis R. LaGesse, and Wayne W. Schurter. SPIE, 1990. http://dx.doi.org/10.1117/12.962477.

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Reports on the topic "Amidase"

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Niles, Keron. Resilience Amidst Rising Tides. International Centre for Trade and Sustainable Development, 2010. http://dx.doi.org/10.7215/co_ip_20100224.

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Roy, Denny. China-Japan Relations: Cooperation Amidst Antagonism. Defense Technical Information Center, 2004. http://dx.doi.org/10.21236/ada627502.

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Diwakar, Vidya. Ending extreme poverty amidst fragility, conflict, and violence. Data and Evidence to End Extreme Poverty, 2023. http://dx.doi.org/10.55158/deeptp2.

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This paper examines how Fragile, Conflict-affected, and Violent (FCV) settings have impacted efforts to reduce extreme poverty today and concludes that given the complex relationship between FCVs and poverty, a flexible portfolio approach that responds to different sources of impoverishment is needed.
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Whitaker, Craig, Jay R. Heckert, and Ian C. Uber. Synthesis of Amide Functionalized Carbon Nanotubes. Defense Technical Information Center, 2007. http://dx.doi.org/10.21236/ada519137.

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Glardon, Thomas L. Balancing U.S. Interests Amidst the India and Pakistan Conflict. Defense Technical Information Center, 2005. http://dx.doi.org/10.21236/ada432021.

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Brown, Sylvester H. The Army Reserve Meeting Homeland Security Obligations Amidst Transformation. Defense Technical Information Center, 2008. http://dx.doi.org/10.21236/ada478342.

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McCall, Jamie, Khaliid Scott, and Urmi Bhatt. Small Business Stories: Surviving and Thriving Amidst the Pandemic. Carolina Small Business Development Fund, 2021. http://dx.doi.org/10.46712/covid.stories.

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The COVID-19 pandemic will leave an enduring mark on North Carolina’s small business community. Using a phenomenological framework, we conducted a series of in-depth semi-structured interviews with small business owners about how they addressed the pandemic’s challenges. Four central themes emerged that illustrate the complexity and nuance of small business resiliency. Our data suggest that to survive and thrive, entrepreneurs had to: (1) be adaptable and willing to pivot, (2) have an entrepreneurial spirit, (3) leverage their social capital, and (4) have the knowledge and ability to apply for
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Bleakley, Hoyt, Louis Cain, and Joseph Ferrie. Amidst Poverty and Prejudice: Black and Irish Civil War Veterans. National Bureau of Economic Research, 2013. http://dx.doi.org/10.3386/w19605.

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Lee, Ernest C. Sarin Nerve Gas: A Rationale for Vigilance Amidst War and Peace. Defense Technical Information Center, 2003. http://dx.doi.org/10.21236/ada415163.

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Siegel, Dina, and Sara Pasqualoni. Industrial Hygiene and OEM: Optimizing Collaboration Amidst the COVID-19 Pandemic. Office of Scientific and Technical Information (OSTI), 2020. http://dx.doi.org/10.2172/1699398.

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