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Journal articles on the topic 'Inhibiteur enzyme conversion'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

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1

du Cailar, G., C. Rugale, J. Ribstein, and A. Mimran. "Apport sodé et régression de l'hypertrophie cardiaque chez l'hypertendutraité par inhibiteur de ('enzyme de conversion." La Revue de Médecine Interne 22 (December 2001): 456s. http://dx.doi.org/10.1016/s0248-8663(01)80078-3.

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2

Buneeva, O. A., L. N. Aksenova, and A. E. Medvedev. "A Simple Approach for Pilot Analysis of Time-dependent Enzyme Inhibition: Discrimination Between Mechanism-based Inactivation and Tight Binding Inhibitor Behavior." Biomedical Chemistry: Research and Methods 3, no. 1 (2020): e00115. http://dx.doi.org/10.18097/bmcrm00115.

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The increase in enzyme inhibition developed during prolonged incubation of an enzyme preparation with a chemical substance may be associated with both the non-covalent and also with covalent enzyme-inhibitor complex formation. The latter case involves catalytic conversion of a mechanism-based irreversible inhibitor (a poor substrate) into a reactive species forming covalent adduct(s) with the enzyme and thus irreversibly inactivating the enzyme molecule. Using a simple approach, based on comparison of enzyme inhibition after preincubation with a potential inhibitor at 4ºC or 37ºC we have analy

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3

Glenn, Katie, and Kerry S. Smith. "Allosteric Regulation of Lactobacillus plantarum Xylulose 5-Phosphate/Fructose 6-Phosphate Phosphoketolase (Xfp)." Journal of Bacteriology 197, no. 7 (2015): 1157–63. http://dx.doi.org/10.1128/jb.02380-14.

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ABSTRACTXylulose 5-phosphate/fructose 6-phosphate phosphoketolase (Xfp), which catalyzes the conversion of xylulose 5-phosphate (X5P) or fructose 6-phosphate (F6P) to acetyl phosphate, plays a key role in carbohydrate metabolism in a number of bacteria. Recently, we demonstrated that the fungalCryptococcus neoformansXfp2 exhibits both substrate cooperativity for all substrates (X5P, F6P, and Pi) and allosteric regulation in the forms of inhibition by phosphoenolpyruvate (PEP), oxaloacetic acid (OAA), and ATP and activation by AMP (K. Glenn, C. Ingram-Smith, and K. S. Smith. Eukaryot Cell13:657

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Rohman, Ali, Bauke W. Dijkstra та Ni Nyoman Tri Puspaningsih. "β-Xylosidases: Structural Diversity, Catalytic Mechanism, and Inhibition by Monosaccharides". International Journal of Molecular Sciences 20, № 22 (2019): 5524. http://dx.doi.org/10.3390/ijms20225524.

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Xylan, a prominent component of cellulosic biomass, has a high potential for degradation into reducing sugars, and subsequent conversion into bioethanol. This process requires a range of xylanolytic enzymes. Among them, β-xylosidases are crucial, because they hydrolyze more glycosidic bonds than any of the other xylanolytic enzymes. They also enhance the efficiency of the process by degrading xylooligosaccharides, which are potent inhibitors of other hemicellulose-/xylan-converting enzymes. On the other hand, the β-xylosidase itself is also inhibited by monosaccharides that may be generated in

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Velez, Juan Carlos Q., Alison M. Bland, John M. Arthur, John R. Raymond, and Michael G. Janech. "Characterization of renin-angiotensin system enzyme activities in cultured mouse podocytes." American Journal of Physiology-Renal Physiology 293, no. 1 (2007): F398—F407. http://dx.doi.org/10.1152/ajprenal.00050.2007.

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Intraglomerular ANG II has been linked to glomerular injury. However, little is known about the contribution of podocytes (POD) to intraglomerular ANG II homeostasis. The aim of the present study was to examine the processing of angiotensin substrates by cultured POD. Our approach was to use matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) mass spectrometry for peptide determination from conditioned cell media and customized AQUA peptides for quantification. Immortalized mouse POD were incubated with 1-2 μM ANG I, ANG II, or the renin substrate ANG-(1-14) for different ti

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Tomohiro, Shiho, Ayako Kawaguti, Yukiyo Kawabe, Sakae Kitada, and Osamu Kuge. "Purification and characterization of human phosphatidylserine synthases 1 and 2." Biochemical Journal 418, no. 2 (2009): 421–29. http://dx.doi.org/10.1042/bj20081597.

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PS (phosphatidylserine) in mammalian cells is synthesized by two distinct base-exchange enzymes, PSS1 (PS synthase 1) and PSS2, which are responsible for the conversion of PC (phosphatidylcholine) and PE (phosphatidylethanolamine) respectively into PS in intact cells. The PS synthesis in cultured mammalian cells is inhibited by exogenous PS, and this feedback control occurs through inhibition of PSSs by PS. In the present study, we purified epitope-tagged forms of human PSS1 and PSS2. The purified PSS2 was shown to catalyse the conversion of PE, but not PC, into PS, this being consistent with

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7

Dunston, T. T., M. A. Khomutov, S. B. Gabelli, et al. "Identification of a novel substrate-derived spermine oxidase inhibitor." Acta Naturae 12, no. 3 (2020): 140–44. http://dx.doi.org/10.32607/actanaturae.10992.

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Homeostasis of the biogenic polyamines spermine (Spm) and spermidine (Spd), present in M-mM concentrations in all eukaryotic cells, is precisely regulated by coordinated activities of the enzymes of polyamine synthesis, degradation, and transport, in order to sustain normal cell growth and viability. Spermine oxidase (SMOX) is the key and most recently discovered enzyme of polyamine metabolism that plays an essential role in regulating polyamine homeostasis by catalyzing the back-conversion of Spm to Spd. The development of many types of epithelial cancer is associated with inflammation, and d

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8

de la FUENTE, Juan L., Angel RUMBERO, Juan F. MARTÍN та Paloma LIRAS. "Δ-1-Piperideine-6-carboxylate dehydrogenase, a new enzyme that forms α-aminoadipate in Streptomyces clavuligerus and other cephamycin C-producing actinomycetes". Biochemical Journal 327, № 1 (1997): 59–64. http://dx.doi.org/10.1042/bj3270059.

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Δ-1-Piperideine-6-carboxylate (P6C) dehydrogenase activity, which catalyses the conversion of P6C into α-aminoadipic acid, has been studied in the cephamycin C producer Streptomyces clavuligerus by both spectrophotometric and radiometric assays. The enzyme has been purified 124-fold to electrophoretic homogeneity with a 26% yield. The native protein is a monomer of 56.2 kDa that efficiently uses P6C (apparent Km 14 μM) and NAD+ (apparent Km 115 μM), but not NADP+ or other electron acceptors, as substrates. The enzyme activity was inhibited (by 66%) by its end product NADH at 0.1 mM concentrati

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9

Chen, X., and J. D. Catravas. "Neutrophil-mediated endothelial angiotensin-converting enzyme dysfunction: role of oxygen-derived free radicals." American Journal of Physiology-Lung Cellular and Molecular Physiology 265, no. 3 (1993): L243—L249. http://dx.doi.org/10.1152/ajplung.1993.265.3.l243.

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We examined the mechanisms whereby phorbol 12-myristate 13-acetate (PMA)-activated rabbit peritoneal neutrophils [polymorphonuclear leukocytes (PMN)] altered endothelial-bound angiotensin-converting enzyme (ACE) activity in cultured bovine pulmonary arterial endothelial cells (EC). PMA or PMN alone had no effect on ACE activity. When PMN were coincubated with PMA (10 ng/ml) for 4 h in Earle's salt solution, endothelial ACE activity was decreased by 87%. No EC cytotoxicity was observed at this time as determined by 51Cr release from prelabeled EC. Activated PMN-mediated decreased ACE activity w

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10

Sato, N., Y. Ito, T. Iida, K. Fukuyama, and W. L. Epstein. "Characterization of two dipeptidases purified from hepatic schistosome egg granulomas in mice. Leukotriene D4 hydrolases of granulomatous tissue." Biochemical Journal 284, no. 3 (1992): 885–90. http://dx.doi.org/10.1042/bj2840885.

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Extracts prepared from tissue with granulomatous inflammation experimentally produced in liver of CBA-strain mice showed increased hydrolysis of leukotriene D4 (LTD4), Leu-Leu and Ala-Gly as compared with normal hepatic cells. Two dipeptidases, Leu-Leu dipeptidase and Ala-Gly dipeptidase, were purified from hepatic granulomas, and quantitative conversion of LTD4 into leukotriene E4 (LTE4) by both enzymes was demonstrated. M(r) values of the purified enzymes were 178,000 for Leu-Leu dipeptidase and 183,000 for Ala-Gly dipeptidase. The enzymes showed homogeneity, appearing as a single band on SD

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11

Koo, Bonwook, Jaemin Jo, and Seong-Min Cho. "Drying Effect on Enzymatic Hydrolysis of Cellulose Associated with Porosity and Crystallinity." Applied Sciences 10, no. 16 (2020): 5545. http://dx.doi.org/10.3390/app10165545.

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The effect of drying on the enzymatic hydrolysis of cellulose was determined by analysis of porosity and crystallinity. Fiber hornification induced by drying produced an irreversible reduction in pore volume due to shrinkage and pore collapse, and the decrease in porosity inhibited enzymatic hydrolysis. The drying effect index (DEI) was defined as the difference in enzymatic digestibility between oven- and never-dried pulp, and it was determined that more enzymes caused a higher DEI at the initial stage of enzymatic hydrolysis and the highest DEI was also observed at the earlier stages with hi

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12

Yang, Chin-Yuh, Ching-Liang Meng, and Patrick Y. K. Wong. "Human parathyroid hormone fragment stimulates thede novosynthesis of prostaglandin endoperoxide synthase in chick calvaria." Mediators of Inflammation 2, no. 2 (1993): 143–47. http://dx.doi.org/10.1155/s0962935193000213.

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The human parathyroid hormone N-terminal fragment [hPTH-(1–34)] increases the conversion of exogenous unsaturated fatty acids to prostaglandins (PGs) in calvarial homogenates. Enzyme activities were completely blocked by indomethacin (5 × 10−7M), a PG synthase inhibitor, and actinomycin D (5 μM), an inhibitor of transcription, by binding to DNA. In addition, a potent inhibitor of protein synthesis, cycloheximide (10 μM), totally inhibited the stimulating effect of hPTH-(1–34) on prostaglandin endoperoxide synthase (PG synthase, EC 1.14.99.1). The stimulatory effect of hPTH-(1–34) on PG synthas

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13

Hisaki, K., Y. Matsumura, H. Maekawa, K. Fujita, M. Takaoka, and S. Morimoto. "Conversion of big ET-1 in the rat lung: role of phosphoramidon-sensitive endothelin-1-converting enzyme." American Journal of Physiology-Heart and Circulatory Physiology 266, no. 2 (1994): H422—H428. http://dx.doi.org/10.1152/ajpheart.1994.266.2.h422.

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We examined conversion of Big endothelin-1 (ET-1) to mature ET-1 and pressor action during perfusion of the isolated perfused rat lung with Big ET-1. Big ET-1 caused a concentration-related increase in perfusion pressure and the pressor molar potency of the peptide was fivefold less than that of ET-1. Pressor responses to Big ET-1 were accompanied by an increase in immunoreactive-ET (IR-ET) levels in the perfusate and in the lung tissues. Pretreatment with phosphoramidon (10(-4) M), a metalloproteinase inhibitor, markedly suppressed the pressor action and increment in IR-ET in the tissues. Une

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14

Kettle, A. J., C. A. Gedye, M. B. Hampton, and C. C. Winterbourn. "Inhibition of myeloperoxidase by benzoic acid hydrazides." Biochemical Journal 308, no. 2 (1995): 559–63. http://dx.doi.org/10.1042/bj3080559.

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Myeloperoxidase is the most abundant protein in neutrophils and catalyses the conversion of H2O2 and chloride into HOCl. To help clarify the role of this enzyme in bacterial killing and inflammation, a specific and potent inhibitor needs to be identified. We have studied a series of benzoic acid hydrazides and found that in general they inhibit the peroxidation activity of myeloperoxidase with an IC50 value of less than 10 microM. The IC50 values of derivatives with substituents containing oxygen or nitrogen were related to their Hammett substituent constants. This indicates that myeloperoxida

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15

Kokko, Leena, Nina Johansson, Timo Lövgren, and Tero Soukka. "Enzyme Inhibitor Screening Using a Homogeneous Proximity-Based Immunoassay for Estradiol." Journal of Biomolecular Screening 10, no. 4 (2005): 348–54. http://dx.doi.org/10.1177/1087057104272191.

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The authors have previously reported a homogeneous time-resolved fluorescence proximity immunoassay for estradiol. The assay was based on luminescence resonance energy transfer between a long lifetime fluorescent europium(III) chelate-dyed nanoparticle donor and a short lifetime, near-infrared fluorescent acceptor. The energy transfer prolonged the lifetime of the sensitized acceptor emission, and the fluorescence of the acceptor was measured using a time-resolved detection. The developed immunoassay was employed to screen inhibitors for enzyme 17β-hydroxysteroid dehydrogenase type 1. The enzy

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16

PFEIFFER, Silvia, C. F. Antonius GORREN, Eva PITTERS, Kurt SCHMIDT, R. Ernst WERNER, and Bernd MAYER. "Allosteric modulation of rat brain nitric oxide synthase by the pterin-site enzyme inhibitor 4-aminotetrahydrobiopterin." Biochemical Journal 328, no. 2 (1997): 349–52. http://dx.doi.org/10.1042/bj3280349.

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We investigated the functional and allosteric effects of the 4-amino analogue of tetrahydrobiopterin, (6R)-2,4-diamino-5,6,7,8-tetrahydro-6-(l-erythro-1,2-dihydroxypropyl)pteridine (4-amino-H4biopterin) on pteridine-free rat neuronal nitric oxide synthase. In the presence of added (6R)-5,6,7,8-tetrahydro-L-erythrobiopterin (H4biopterin; 10 μM), 4-amino-H4biopterin completely inhibited the conversion of both L-arginine and NG-hydroxy-L-arginine with half-maximally effective concentrations of 1.1±0.09 and 1.3±0.09 μM, respectively. Inhibition was reversible, as shown by a time-dependent restorat

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17

MOORE, Allison B., and Sheldon W. MAY. "Kinetic and inhibition studies on substrate channelling in the bifunctional enzyme catalysing C-terminal amidation." Biochemical Journal 341, no. 1 (1999): 33–40. http://dx.doi.org/10.1042/bj3410033.

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A series of experiments has been conducted to investigate the possibility that substrate channelling might occur in the bifunctional forms of enzymes carrying out C-terminal amidation, a post-translational modification essential to the biological activity of many neuropeptides. C-terminal amidation entails sequential action by peptidylglycine mono-oxygenase (PAM, EC 1.14.17.3) and peptidylamidoglycolate lyase (PGL, EC 4.3.2.5), with the mono-oxygenase catalysing conversion of a glycine-extended pro-peptide into the corresponding α-hydroxyglycine derivative, which is then converted by the lyase

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18

Danielsen, E. M., and G. M. Cowell. "Biosynthesis of intestinal microvillar proteins Processing of N-linked carbohydrate is not required for surface expression." Biochemical Journal 240, no. 3 (1986): 777–82. http://dx.doi.org/10.1042/bj2400777.

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Castanospermine, an inhibitor of glucosidase I, the initial enzyme in the trimming of N-linked carbohydrate, was used to study the importance of carbohydrate processing in the biosynthesis of microvillar enzymes in organ-cultured pig intestinal explants. For aminopeptidase N (EC 3.4.11.2), aminopeptidase A (EC 3.4.11.7), sucrase-isomaltase (EC 3.2.1.48-10) and maltase-glucoamylase (EC 3.2.1.20), castanospermine caused the formation of novel transient forms of higher Mr than corresponding controls, indicating a blocked removal of glucose residues. For the first three enzymes, the ‘mature’ (Golg

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19

Velez, Juan Carlos Q., Jessalyn L. Ierardi, Alison M. Bland, et al. "Enzymatic processing of angiotensin peptides by human glomerular endothelial cells." American Journal of Physiology-Renal Physiology 302, no. 12 (2012): F1583—F1594. http://dx.doi.org/10.1152/ajprenal.00087.2012.

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The intraglomerular renin-angiotensin system (RAS) is linked to the pathogenesis of progressive glomerular diseases. Glomerular podocytes and mesangial cells play distinct roles in the metabolism of angiotensin (ANG) peptides. However, our understanding of the RAS enzymatic capacity of glomerular endothelial cells (GEnCs) remains incomplete. We explored the mechanisms of endogenous cleavage of ANG substrates in cultured human GEnCs (hGEnCs) using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry and isotope-labeled peptide quantification. Overall, hGEnCs metabolized

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Li, Xiaopeng, Heather Rayford, Ruijie Shu, Jiaju Zhuang, and Bruce D. Uhal. "Essential role for cathepsin D in bleomycin-induced apoptosis of alveolar epithelial cells." American Journal of Physiology-Lung Cellular and Molecular Physiology 287, no. 1 (2004): L46—L51. http://dx.doi.org/10.1152/ajplung.00442.2003.

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Our earlier studies showed that bleomycin-induced apoptosis of type II alveolar epithelial cells (AECs) requires the autocrine synthesis and proteolytic processing of angiotensinogen into ANG II and that inhibitors of ANG-converting enzyme (ACEis) block bleomycin-induced apoptosis (Li X, Zhang H, Soledad-Conrad V, Zhuang J, and Uhal BD. Am J Physiol Lung Cell Mol Physiol 284: L501–L507, 2003). Given the documented role of cathepsin D (CatD) in apoptosis of other cell types, we hypothesized that CatD might be the AEC enzyme responsible for the conversion of angiotensinogen into ANG I, the subst

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Son, Jong-Keun, and John P. N. Rosazza. "Cyclic Guanosine-3′,5′-Monophosphate and Biopteridine Biosynthesis in Nocardia sp." Journal of Bacteriology 182, no. 13 (2000): 3644–48. http://dx.doi.org/10.1128/jb.182.13.3644-3648.2000.

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ABSTRACT Nocardia sp. strain NRRL 5646 contains a nitric oxide synthase (NOS) enzyme system capable of generating nitric oxide (NO) from arginine and arginine-containing peptides. To explain possible roles of the NOS system in this bacterium, guanylate cyclase (GC) and tetrahydrobiopterin (H4B) biosynthetic enzymes were identified in cell extracts and in culture media. Cell extracts contained GC activity, as measured by the conversion of GTP to cyclic guanosine-3′,5′-monophosphate (cGMP) at 9.56 pmol of cGMP h−1 mg of protein−1. Concentrations of extracellular cGMP in culture media were signif

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Lin, Chin-chung, Che Fang, Salete Benetton, Gui-fen Xu, and Li-Tain Yeh. "Metabolic Activation of Pradefovir by CYP3A4 and Its Potential as an Inhibitor or Inducer." Antimicrobial Agents and Chemotherapy 50, no. 9 (2006): 2926–31. http://dx.doi.org/10.1128/aac.01566-05.

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ABSTRACT Metabolic activation of pradefovir to 9-(2-phosphonylmethoxyethyl)adenine (PMEA) was evaluated by using cDNA-expressed CYP isozymes in portal vein-cannulated rats following oral administration and in human liver microsomes. The enzyme induction potential of pradefovir was evaluated in rats following multiple oral dosing and in primary cultures of human hepatocytes. The results indicated that CYP3A4 is the only cDNA-expressed CYP isozyme catalyzing the conversion of pradefovir to PMEA. Pradefovir was converted to PMEA in human liver microsomes with a Km of 60 μM, a maximum rate of meta

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23

Hoover, Gordon J., Gerald A. Prentice, A. Rod Merrill, and Barry J. Shelp. "Kinetic mechanism of a recombinant Arabidopsis glyoxylate reductase: studies of initial velocity, dead-end inhibition and product inhibition." Canadian Journal of Botany 85, no. 9 (2007): 896–902. http://dx.doi.org/10.1139/b07-082.

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Kinetic analysis of substrate specificity revealed that a recombinant Arabidopsis protein catalyzes the conversion of glyoxylate to glycolate (Km,glyoxylate = 4.5 μmol·L–1) and succinic semialdehyde (SSA) to γ-hydroxybutyrate (Km, SSA = 0.87 mmol·L–1) via an essentially irreversible, NADPH-based mechanism. In this report, the enzyme was further characterized via initial-velocity, dead-end inhibition and product inhibition studies. The kinetic mechanism was ordered Bi Bi, involving the complexation of NADPH to the enzyme before glyoxylate or SSA, and the release of NADP+ before glycolate or γ-h

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Baverel, G., G. Martin, and C. Michoudet. "Glutamine synthesis from aspartate in guinea-pig renal cortex." Biochemical Journal 268, no. 2 (1990): 437–42. http://dx.doi.org/10.1042/bj2680437.

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1. Glutamine was found to be the main carbon and nitrogen product of the metabolism of aspartate in isolated guinea-pig kidney-cortex tubules. Glutamate, ammonia and alanine were only minor products. 2. Carbon-balance calculations and the release of 14CO2 from [U-14C]aspartate indicate that oxidation of the aspartate carbon skeleton occurred. 3. A pathway involving aspartate aminotransferase, glutamate dehydrogenase, glutamine synthetase, phosphoenolpyruvate carboxykinase, pyruvate kinase, pyruvate dehydrogenase and enzymes of the tricarboxylic acid cycle is proposed for the conversion of aspa

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Andersson, C., M. Söderström, and B. Mannervik. "Activation and inhibition of microsomal glutathione transferase from mouse liver." Biochemical Journal 249, no. 3 (1988): 819–23. http://dx.doi.org/10.1042/bj2490819.

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Mouse liver microsomal glutathione transferase was purified in an N-ethylmaleimide-activated as well as an unactivated form. The enzyme had a molecular mass of 17 kDa and a pI of 8.8. It showed cross-reactivity with antibodies raised against rat liver microsomal glutathione transferase, but not with any of the available antisera raised against cytosolic glutathione transferases. The fully N-ethylmaleimide-activated enzyme could be further activated 1.5-fold by inclusion of 1 microM-bromosulphophthalein in the assay system. The latter effect was reversible, which was not the case for the N-ethy

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Meijer, Nathan, Geert Stoopen, H. J. van der Fels-Klerx, Joop J. A. van Loon, John Carney, and Guido Bosch. "Aflatoxin B1 Conversion by Black Soldier Fly (Hermetia illucens) Larval Enzyme Extracts." Toxins 11, no. 9 (2019): 532. http://dx.doi.org/10.3390/toxins11090532.

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The larvae of the black soldier fly (Hermetia illucens L., BSFL) have received increased industrial interest as a novel protein source for food and feed. Previous research has found that insects, including BSFL, are capable of metabolically converting aflatoxin B1 (AFB1), but recovery of total AFB1 is less than 20% when accounting for its conversion to most known metabolites. The aim of this study was to examine the conversion of AFB1 by S9 extracts of BSFL reared on substrates with or without AFB1. Liver S9 of Aroclor-induced rats was used as a reference. To investigate whether cytochrome P45

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KATUGAMPOLA, Sidath D., and Anthony P. DAVENPORT. "Radioligand binding reveals chymase as the predominant enzyme for mediating tissue conversion of angiotensin I in the normal human heart." Clinical Science 102, no. 1 (2001): 15–21. http://dx.doi.org/10.1042/cs1020015.

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We investigated the binding characteristics of angiotensin receptors and used this assay to determine the predominant enzyme capable of converting angiotensin I in the human left ventricle. In homogenates of human left ventricle, 125I-[Sar1,Ile8]angiotensin II bound with sub-nanomolar affinity, with a corresponding KD of 0.42±0.09nM, a Bmax of 11.2±2.3fmolċmg-1 protein and a Hill slope of 1.04±0.04. The rank order of inhibitory potency of competing ligands for the 125I-[Sar1,Ile8]angiotensin II binding site was CGP42112 > angiotensin II⩾ angiotensin III = angiotensin I > losartan. The an

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PALMIERI, Gianna, Michela DI PALO, Andrea SCALONI, Stefania ORRÙ, Gennaro MARINO, and Giovanni SANNIA. "Glutamate-1-semialdehyde aminotransferase from Sulfolobus solfataricus*." Biochemical Journal 320, no. 2 (1996): 541–45. http://dx.doi.org/10.1042/bj3200541.

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Glutamate-1-semialdehyde aminotransferase (GSA-AT) from the extremely thermophilic bacterium Sulfolobus solfataricus has been purified to homogeneity and characterized. GSA-AT is the last enzyme in the C5 pathway for the conversion of glutamate into the tetrapyrrole precursor Δ-aminolaevulinate (ALA) in plants, algae and several bacteria. The active form of GSA-AT from S. solfataricus seems to be a homodimer with a molecular mass of 87 kDa. The absorption spectrum of the purified aminotransferase is indicative of the presence of pyridoxamine 5´-phosphate (PMP) cofactor, and the catalytic activ

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CHEN, Hao, and Mont R. JUCHAU. "Recombinant human glutathione S-transferases catalyse enzymic isomerization of 13-cis-retinoic acid to all-trans-retinoic acid in vitro." Biochemical Journal 336, no. 1 (1998): 223–26. http://dx.doi.org/10.1042/bj3360223.

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The steric conversion of 13-cis-retinoic acid (13-cRA) to all-trans-retinoic acid (t-RA) has been proposed as an activation mechanism for the observed therapeutic and teratogenic activities of 13-cRA. Here we have investigated the catalysis of isomerization of 13-cRA to t-RA by recombinant human glutathione S-transferases (GSTs). Substrate was incubated with GST in 0.1 M sodium phosphate buffer, pH 7.5, at 37 °C in total darkness. The t-RA generated was measured quantitatively by HPLC. Under the reaction conditions used, GSTP1–1 was far more effective than human GSTM1–1 or human GSTA1–1 in cat

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Zhou, Linchao, Leonardo da Costa Sousa, Bruce E. Dale, Jia-Xun Feng, and Venkatesh Balan. "The effect of alkali-soluble lignin on purified core cellulase and hemicellulase activities during hydrolysis of extractive ammonia-pretreated lignocellulosic biomass." Royal Society Open Science 5, no. 6 (2018): 171529. http://dx.doi.org/10.1098/rsos.171529.

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Removing alkali-soluble lignin using extractive ammonia (EA) pretreatment of corn stover (CS) is known to improve biomass conversion efficiency during enzymatic hydrolysis. In this study, we investigated the effect of alkali-soluble lignin on six purified core glycosyl hydrolases and their enzyme synergies, adopting 31 enzyme combinations derived by a five-component simplex centroid model, during EA-CS hydrolysis. Hydrolysis experiment was carried out using EA-CS(−) (approx. 40% lignin removed during EA pretreatment) and EA-CS(+) (where no lignin was extracted). Enzymatic hydrolysis experiment

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Krappmann, Sven, Ralph Pries, Gerd Gellissen, Mark Hiller, and Gerhard H. Braus. "HARO7 Encodes Chorismate Mutase of the Methylotrophic Yeast Hansenula polymorpha and Is Derepressed upon Methanol Utilization." Journal of Bacteriology 182, no. 15 (2000): 4188–97. http://dx.doi.org/10.1128/jb.182.15.4188-4197.2000.

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The HARO7 gene of the methylotrophic, thermotolerant yeast Hansenula polymorpha was cloned by functional complementation. HARO7 encodes a monofunctional 280-amino-acid protein with chorismate mutase (EC 5.4.99.5) activity that catalyzes the conversion of chorismate to prephenate, a key step in the biosynthesis of aromatic amino acids. The HARO7 gene product shows strong similarities to primary sequences of known eukaryotic chorismate mutase enzymes. After homologous overexpression and purification of the 32-kDa protein, its kinetic parameters (k cat = 319.1 s−1,nH = 1.56, [S]0.5 = 16.7 mM) as

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Schilling, Stephan, and Hans-Ulrich Demuth. "Continuous assays of glutaminyl cyclase: from development to application." Spectroscopy 18, no. 2 (2004): 363–73. http://dx.doi.org/10.1155/2004/413050.

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Glutaminyl cyclase (QC, EC 2.3.2.5) catalyses the formation of pyroglutamyl residues from glutamine at the N-terminus of peptides and proteins. In previously applied assays, QC activity was determined by either analysing the products formed using HPLC coupled with photometric or fluorometric detection, radioimmunoassay, or by detecting the release of ammonia spectrophotometrically. Although these methods are sensitive, they are all discontinuous and therefore time-consuming and laborious. To conduct a detailed kinetic investigation of QC catalysis, we developed coupled continuous assays suitab

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Famuwagun, Akinsola A., Adeola M. Alashi, Saka O. Gbadamosi, et al. "Effect of Protease Type and Peptide Size on the In Vitro Antioxidant, Antihypertensive and Anti-Diabetic Activities of Eggplant Leaf Protein Hydrolysates." Foods 10, no. 5 (2021): 1112. http://dx.doi.org/10.3390/foods10051112.

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Solanum macrocarpon (eggplant) leaf protein isolate (ELI) was hydrolyzed using four different enzymes to produce hydrolysates from alcalase (AH), chymotrypsin (CH) pepsin (PH) and trypsin (TH). CH had an overall stronger antioxidant property and was separated using ultrafiltration membranes into <1, 1–3 and 3–5 kDa peptide fractions. Gel-permeation chromatography confirmed conversion of the ELI (average of 22 kDa) into protein hydrolysates that contained smaller peptides (<6 kDa). A total of 23 peptides consisting of tri and tetrapeptides were identified from the CH, which is a wider spe

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Ma, Yufang, Richard J. Stern, Michael S. Scherman, et al. "Drug Targeting Mycobacterium tuberculosis Cell Wall Synthesis: Genetics of dTDP-Rhamnose Synthetic Enzymes and Development of a Microtiter Plate-Based Screen for Inhibitors of Conversion of dTDP-Glucose to dTDP-Rhamnose." Antimicrobial Agents and Chemotherapy 45, no. 5 (2001): 1407–16. http://dx.doi.org/10.1128/aac.45.5.1407-1416.2001.

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ABSTRACT An l-rhamnosyl residue plays an essential structural role in the cell wall of Mycobacterium tuberculosis. Therefore, the four enzymes (RmlA to RmlD) that form dTDP-rhamnose from dTTP and glucose-1-phosphate are important targets for the development of new tuberculosis therapeutics. M. tuberculosis genes encoding RmlA, RmlC, and RmlD have been identified and expressed inEscherichia coli. It is shown here that genes for only one isotype each of RmlA to RmlD are present in the M. tuberculosis genome. The gene for RmlB is Rv3464. Rv3264c was shown to encode ManB, not a second isotype of R

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Kihn, Lee, Dorothy Rutkowski, and Robert A. Stinson. "Incorporation of human liver and placental alkaline phosphatases into liposomes and membranes is via phosphatidylinositol." Biochemistry and Cell Biology 68, no. 9 (1990): 1112–18. http://dx.doi.org/10.1139/o90-166.

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As assessed by incorporation into liposomes and by adsorption to octyl-Sepharose, the integrity of the membrane anchor for the purified tetrameric forms of alkaline phosphatase from human liver and placenta was intact. Any treatment that resulted in a dimeric enzyme precluded incorporation and adsorption. An intact anchor also allowed incorporation into red cell ghosts. The addition of hydrophobic proteins inhibited incorporation into liposomes to varying degrees. Alkaline phosphatase was 100% releasable from liposomes and red cell ghosts by a phospholipase C specific for phosphatidylinositol.

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NISHIKAWA, Yuji, Siddhartha KAR, Laurie WIEST, Anthony E. PEGG та Brian I. CARR. "Inhibition of spermidine synthase gene expression by transforming growth factor-β1 in hepatoma cells". Biochemical Journal 321, № 2 (1997): 537–43. http://dx.doi.org/10.1042/bj3210537.

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We screened genes responsive to transforming growth factor-α (TGF-α1) protein in a human hepatoma cell line (Hep3B) using a PCR-mediated differential display technique, in order to investigate the mechanisms involved in TGF-α-induced growth suppression. We found a gene that was down-regulated by TGF-α1 to be completely identical in an approx. 620 bp segment to the gene for the enzyme spermidine synthase, which mediates the conversion of putrescine into spermidine. Both spermidine synthase mRNA expression and its enzyme activity were decreased after TGF-α1 treatment of Hep3B cells. The inhibiti

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Gorski, T. P., and D. J. Campbell. "Angiotensin-converting enzyme determination in plasma during therapy with converting enzyme inhibitor: two methods compared." Clinical Chemistry 37, no. 8 (1991): 1390–93. http://dx.doi.org/10.1093/clinchem/37.8.1390.

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Abstract For normal and above-normal concentrations of angiotensin-converting enzyme (ACE; EC 3.4.15.1) activity in plasma, results of a manual fluorometric method [with hippuryl-histidyl-leucine (HHL), 5 mmol/L, as substrate] correlated well with those of an automated spectrophotometric method [with 3-(2-furylacryloyl)-L-phenylalanyl-glycyl-glycine (FAPGG), 2 mmol/L, as substrate]. However, for patients receiving converting enzyme inhibitor (CEI) therapy, the spectrophotometric method showed much greater suppression of plasma ACE activity than did the fluorometric method. To determine which o

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Marchetti, Jeannine, Claudia M. B. Helou, Catherine Chollet, Rabary Rajerison, and François Alhenc-Gelas. "ACE and non-ACE mediated effect of angiotensin I on intracellular calcium mobilization in rat glomerular arterioles." American Journal of Physiology-Heart and Circulatory Physiology 284, no. 6 (2003): H1933—H1941. http://dx.doi.org/10.1152/ajpheart.00042.2003.

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Because renin and angiotensin I (ANG I) level are high in the renal circulation, the conversion of ANG I is a critical step in the regulation of glomerular hemodynamics. We studied this conversion by investigating the effect of ANG I on intracellular Ca2+concentration ([Ca2+]i) in rat juxtamedullary glomerular afferent and efferent arterioles (AA and EA, respectively). Two types of EA were considered, thin EA and muscular EA, terminating as peritubular capillaries and vasa rectae, respectively. In all arterioles, ANG I elicited [Ca2+]i elevations. Maximal responses of 171 ± 28 (AA), 183 ± 7 (m

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Fridman, R., R. E. Bird, M. Hoyhtya, et al. "Expression of human recombinant 72 kDa gelatinase and tissue inhibitor of metalloproteinase-2 (TIMP-2): characterization of complex and free enzyme." Biochemical Journal 289, no. 2 (1993): 411–16. http://dx.doi.org/10.1042/bj2890411.

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The human 72 kDa gelatinase/type IV collagenase is a metalloproteinase that is thought to play a role in metastasis and angiogenesis. The 72 kDa progelatinase can be isolated from conditioned media as a complex with the tissue inhibitor of metalloproteinase-2 (TIMP-2). To investigate 72 kDa gelatinase-TIMP-2 interactions and to compare the activity of the complex versus that of the free enzyme, we have expressed and purified human 72 kDa progelatinase and TIMP-2 as single proteins in a recombinant vaccinia virus mammalian cell expression system. The recombinant 72 kDa progelatinase was able to

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VUJCIC, Slavoljub, Paula DIEGELMAN, Cyrus J. BACCHI, Debora L. KRAMER, and Carl W. PORTER. "Identification and characterization of a novel flavin-containing spermine oxidase of mammalian cell origin." Biochemical Journal 367, no. 3 (2002): 665–75. http://dx.doi.org/10.1042/bj20020720.

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During polyamine catabolism, spermine and spermidine are first acetylated by spermidine/spermine N1-acetyltransferase (SSAT) and subsequently oxidized by polyamine oxidase (PAO) to produce spermidine and putrescine, respectively. In attempting to clone the PAO involved in this back-conversion pathway, we encountered an oxidase that preferentially cleaves spermine in the absence of prior acetylation by SSAT. A BLAST search using maize PAO sequences identified homologous mammalian cDNAs derived from human hepatoma and mouse mammary carcinoma: the encoded proteins differed by 20 amino acids. When

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Wang, Yuhui, and Hei Sook Sul. "Ectodomain Shedding of Preadipocyte Factor 1 (Pref-1) by Tumor Necrosis Factor Alpha Converting Enzyme (TACE) and Inhibition of Adipocyte Differentiation." Molecular and Cellular Biology 26, no. 14 (2006): 5421–35. http://dx.doi.org/10.1128/mcb.02437-05.

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ABSTRACT Preadipocyte factor 1 (Pref-1), an epidermal growth factor repeat containing transmembrane protein found in the preadipocytes, inhibits adipocyte differentiation in vitro and in vivo. Here, we examined the processing of membrane form of Pref-1A to release the 50-kDa soluble form that inhibits adipocyte differentiation. The ectodomain cleavage of Pref-1 is markedly enhanced by phorbol 12-myristate 13-acetate in a dose- and time-dependent manner. The basal and stimulated cleavage is inhibited by the broad metalloproteinase inhibitor GM6001, a fact that suggests that cleavage of membrane

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Wu, Ge, Yue Yuan, and C. Nicholas Hodge. "Determining Appropriate Substrate Conversion for Enzymatic Assays in High-Throughput Screening." Journal of Biomolecular Screening 8, no. 6 (2003): 694–700. http://dx.doi.org/10.1177/1087057103260050.

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It is generally accepted that the conversion of substrate should be kept at less than 10% of the total substrate used when studying enzyme kinetics. However, 10% or less substrate conversion often will not produce sufficient signal changes required for robust high-throughput screening (HTS). To increase the signal-to-background ratio, HTS is often performed at higher than 10% substrate conversion. Because the consequences of high substrate conversion are poorly understood, the screening results are sometimes questioned by enzymologists. The quality of an assay is judged by the ability to detec

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43

Rupasinghe, H. P. V., K. C. Almquist, G. Paliyath та D. P. Murr. "083 Is HMGR the Key Regulator of α-Farnesene Biosynthesis of Apple?" HortScience 35, № 3 (2000): 403A—403. http://dx.doi.org/10.21273/hortsci.35.3.403a.

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We tested the hypothesis that conversion of 3-hydroxy-3-methylglutaryl co-enzyme A (HMG CoA) to mevalonate (MVA) catalyzed by HMG CoA reductase (HMGR) is the rate limiting step for α-farnesene biosynthesis of apples. In higher plants, isopentenyl pyrophosphate (IPP) is derived via two pathways: 1) the classical mevalonate pathway, and 2) the novel glyceraldehyde-3-phosphate (GAP)/pyruvate pathway independent of HMGR action. When apple skin discs were incubated with MVA, or GAP and pyruvate, MVA increased α-farnesene levels in the skin but not GAP and pyruvate. Treating apple fruits with Lovast

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44

Sonda, Sabrina, Giusy Sala, Riccardo Ghidoni, Andrew Hemphill, and Jean Pieters. "Inhibitory Effect of Aureobasidin A on Toxoplasma gondii." Antimicrobial Agents and Chemotherapy 49, no. 5 (2005): 1794–801. http://dx.doi.org/10.1128/aac.49.5.1794-1801.2005.

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ABSTRACT The apicomplexan parasite Toxoplasma gondii is a leading opportunistic pathogen associated with AIDS and congenital birth defects. Due to the need for identifying new parasite-specific treatments, the possibility of targeting sphingolipid biosynthesis in the parasite was investigated. Aureobasidin A, an inhibitor of the enzyme synthesizing the sphingolipid inositol phosphorylceramide, which is present in fungi, plants, and some protozoa but absent in mammalian cells, was found to block in vitro T. gondii replication without affecting host cell metabolism. Aureobasidin A treatment did

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45

Wang, Po-Hsiang, Yi-Lung Chen, Sean Ting-Shyang Wei, et al. "Retroconversion of estrogens into androgens by bacteria via a cobalamin-mediated methylation." Proceedings of the National Academy of Sciences 117, no. 3 (2019): 1395–403. http://dx.doi.org/10.1073/pnas.1914380117.

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Steroid estrogens modulate physiology and development of vertebrates. Conversion of C19 androgens into C18 estrogens is thought to be an irreversible reaction. Here, we report a denitrifying Denitratisoma sp. strain DHT3 capable of catabolizing estrogens or androgens anaerobically. Strain DHT3 genome contains a polycistronic gene cluster, emtABCD, differentially transcribed under estrogen-fed conditions and predicted to encode a cobalamin-dependent methyltransferase system conserved among estrogen-utilizing anaerobes; an emtA-disrupted DHT3 derivative could catabolize androgens but not estroge

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46

Makar, Subhajit, Abhrajyoti Ghosh, Ashok Kumar, and Sushil K. Singh. "Recent Studies on Aromatase and Sulfatase Involved in Breast Cancer and their Inhibitors." Current Enzyme Inhibition 16, no. 1 (2020): 20–44. http://dx.doi.org/10.2174/1573408016666200325120248.

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Enzyme aromatase uses several androgen substrates for the biosynthesis of estrogen, i.e. conversion of androstenedione to estrone and testosterone to biologically potent estradiol. Aromatase inhibitors (AIs) such as anastrozole, letrozole and exemestane have been established in standard endocrine therapy of breast cancer, by interfering with estrogen signaling cascade. Steroid sulphatase (STS) regulates the level of active oestrogens and androgens in human target organs and steroidogenic tissues, which have a key role in hormone dependent breast cancers (HDBC). Sulfatase is still under the exp

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47

Church, WR, TL Messier, MM Tucker, and KG Mann. "An inhibitory monoclonal antibody to factor X that blocks prothrombin activation but not prothrombinase enzyme assembly." Blood 72, no. 6 (1988): 1911–21. http://dx.doi.org/10.1182/blood.v72.6.1911.1911.

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Abstract A monoclonal antibody (designated alpha BFX-2b) prepared against bovine factor X inhibited factor X activity in human, bovine, porcine, rabbit, and canine plasma. In assays using purified prothrombinase components, factor Xa, factor Va, phospholipid vesicles, and calcium ion with the fluorescent active site thrombin inhibitor dansylarginyl-N-(3-ethyl-1,5- pentanediyl)amide, the antibody inhibited the conversion of prothrombin to thrombin. Antibody alpha BFX-2b also blocked prothrombinase cleavage of the macromolecular substrates prethrombin 1 and prethrombin 2 but did not inhibit fact

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48

Church, WR, TL Messier, MM Tucker, and KG Mann. "An inhibitory monoclonal antibody to factor X that blocks prothrombin activation but not prothrombinase enzyme assembly." Blood 72, no. 6 (1988): 1911–21. http://dx.doi.org/10.1182/blood.v72.6.1911.bloodjournal7261911.

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A monoclonal antibody (designated alpha BFX-2b) prepared against bovine factor X inhibited factor X activity in human, bovine, porcine, rabbit, and canine plasma. In assays using purified prothrombinase components, factor Xa, factor Va, phospholipid vesicles, and calcium ion with the fluorescent active site thrombin inhibitor dansylarginyl-N-(3-ethyl-1,5- pentanediyl)amide, the antibody inhibited the conversion of prothrombin to thrombin. Antibody alpha BFX-2b also blocked prothrombinase cleavage of the macromolecular substrates prethrombin 1 and prethrombin 2 but did not inhibit factor Xa hyd

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Webb, Rachel J., Neera Sunak, Lisa Wren та Anthony E. Michael. "Inactivation of glucocorticoids by 11β-hydroxysteroid dehydrogenase enzymes increases during the meiotic maturation of porcine oocytes". REPRODUCTION 136, № 6 (2008): 725–32. http://dx.doi.org/10.1530/rep-08-0289.

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Recent reports have shown that glucocorticoids can modulate oocyte maturation in both teleost fish and mammals. Within potential target cells, the actions of physiological glucocorticoids are modulated by 11β-hydroxysteroid dehydrogenase (HSD11B) isoenzymes that catalyse the interconversion of cortisol and cortisone. Hence, the objective of this study was to establish whether HSD11B enzymes mediate cortisol–cortisone metabolism in porcine oocytes and, if so, whether the rate of glucocorticoid metabolism changes during oocyte maturation. Enzyme activities were measured in cumulus–oocyte complex

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Wong, P. Y. D., W. O. Fu, S. J. Huang, and W. K. Law. "Effect of angiotensins on electrogenic anion transport in monolayer cultures of rat epididymis." Journal of Endocrinology 125, no. 3 (1990): 449–56. http://dx.doi.org/10.1677/joe.0.1250449.

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ABSTRACT Confluent monolayers cultured from the rat cauda epididymidis have been shown to respond to angiotensin I (AI) and angiotensin II (AII) when studied under short-circuit conditions and bathed on both sides with Krebs–Henseleit solution. Both the decapeptide AI and the octapeptide AII elicited transient increases in short-circuit current (SCC) when added to the basolateral as well as to the apical surfaces, with the effect of basolateral application greater than that of apical application. The maximal responses produced by AI and AII were similar with median effective concentrations of

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