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  • Evaluation of in Silico Approach for Prediction of Presence of Opioid Peptides in Wheat
    Evaluation of in silico approach for prediction of presence of opioid peptides in wheat This is the Accepted version of the following publication Garg, Swati, Apostolopoulos, Vasso, Nurgali, Kulmira and Mishra, Vijay Kumar (2018) Evaluation of in silico approach for prediction of presence of opioid peptides in wheat. Journal of Functional Foods, 41. 34 - 40. ISSN 1756-4646 The publisher’s official version can be found at https://www.sciencedirect.com/science/article/pii/S1756464617307454 Note that access to this version may require subscription. Downloaded from VU Research Repository https://vuir.vu.edu.au/36577/ 1 1 Evaluation of in silico approach for prediction of presence of opioid peptides in wheat 2 gluten 3 Abstract 4 Opioid like morphine and codeine are used for the management of pain, but are associated 5 with serious side-effects limiting their use. Wheat gluten proteins were assessed for the 6 presence of opioid peptides on the basis of tyrosine and proline within their sequence. Eleven 7 peptides were identified and occurrence of predicted sequences or their structural motifs were 8 analysed using BIOPEP database and ranked using PeptideRanker. Based on higher peptide 9 ranking, three sequences YPG, YYPG and YIPP were selected for determination of opioid 10 activity by cAMP assay against µ and κ opioid receptors. Three peptides inhibited the 11 production of cAMP to varied degree with EC50 values of YPG, YYPG and YIPP were 5.3 12 mM, 1.5 mM and 2.9 mM for µ-opioid receptor, and 1.9 mM, 1.2 mM and 3.2 mM for κ- 13 opioid receptor, respectively.
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  • Stream Bed Erosion Labs Stream Bed Erosion
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  • 2019-2020 Award Recipients
    2019-2020 AWARD RECIPIENTS The Office of Undergraduate Research and Creative Activities is pleased to announce the MAYS and RPG recipients for the 2019-2020 academic year. Please join us in congratulating these students and their faculty mentors. Major Academic Year Support (MAYS) Student: Kelly Ackerly Mentor: Dr. Daniel Greenberg Major: Psychology Department: Psychology An Exploration of Maternal Factors Affecting Children’s Autobiographical Memory In day-to-day interactions, mothers and their young children discuss memories of events they have experienced. Research has demonstrated the relationship between these interactions and the development of children’s memories. It is through these interactions that children learn how to interpret personal experiences and develop the skill of talking about them with others in a coherent way. Additionally, studies have found that children are more likely to form false memories—that is, inaccurate “memories” of events that did not actually occur – because their memories are more easily manipulated. In this study, we will explore whether the way mothers talk to their children about ambiguous events affects the children’s interpretations and memories of the event. We will also attempt to determine if there is a relationship between mothers’ negativity during discussions and their child’s formation of false memories. To explore this idea, mothers and their children (aged 3 to 6 years) are given a handful of ambiguous situations to interpret separately. Children are given the opportunity to make slime with a research assistant while a second research assistant acts out ambiguous situations that could have a positive or negative interpretation. The children are evaluated on the way they interpret the situations and whether they form a negative false memory.
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  • Proquest Dissertations
    Opioid peptide permeation across the blood- brain and blood-cerebrospinal fluid barriers Item Type text; Dissertation-Reproduction (electronic) Authors Abbruscato, Thomas John, 1970- Publisher The University of Arizona. Rights Copyright © is held by the author. Digital access to this material is made possible by the University Libraries, University of Arizona. Further transmission, reproduction or presentation (such as public display or performance) of protected items is prohibited except with permission of the author. Download date 04/10/2021 05:24:05 Link to Item http://hdl.handle.net/10150/282429 INFORMATION TO USERS This manuscript has been reproduced from the microfihn master. UMI fihns the text direct^ from the original or copy submitted. Thus, some thesis and dissertation copies are in typewriter &ce, while others may be from any type of computer printer. The quality of this reproductioii is dependent upon the quality of the copy submitted. Broken or indistinct print, colored or poor quality illustrations and photographs, print bleedthrough, substandard margins, and improper alignment can adversely affect reproduction. In the unlikely event that the author did not send UMI a complete manuscript and there are missing pages, these will be noted. Also, if unauthorized copyright material had to be removed, a note will indicate the deletion. Oversize materials (e.g., maps, drawings, charts) are reproduced by sectioning the original, b^inning at the upper left-hand comer and continuing from left to right in equal sections with small overlaps. Each original is also photographed in one exposure and is included in reduced form at the back of the book. Photographs included in the original manuscript have been reproduced xerographically in this copy.
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  • Casomorphins and Gliadorphins Have Diverse Systemic Effects Spanning Gut, Brain and Internal Organs
    International Journal of Environmental Research and Public Health Article Casomorphins and Gliadorphins Have Diverse Systemic Effects Spanning Gut, Brain and Internal Organs Keith Bernard Woodford Agri-Food Systems, Lincoln University, Lincoln 7674, New Zealand; [email protected] Abstract: Food-derived opioid peptides include digestive products derived from cereal and dairy diets. If these opioid peptides breach the intestinal barrier, typically linked to permeability and constrained biosynthesis of dipeptidyl peptidase-4 (DPP4), they can attach to opioid receptors. The widespread presence of opioid receptors spanning gut, brain, and internal organs is fundamental to the diverse and systemic effects of food-derived opioids, with effects being evidential across many health conditions. However, manifestation delays following low-intensity long-term exposure create major challenges for clinical trials. Accordingly, it has been easiest to demonstrate causal relationships in digestion-based research where some impacts occur rapidly. Within this environment, the role of the microbiome is evidential but challenging to further elucidate, with microbiome effects ranging across gut-condition indicators and modulators, and potentially as systemic causal factors. Elucidation requires a systemic framework that acknowledges that public-health effects of food- derived opioids are complex with varying genetic susceptibility and confounding factors, together with system-wide interactions and feedbacks. The specific role of the microbiome within
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  • Prokaryote Coloring with Answers with Answers
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  • Characterisation and Partial Purification of a Novel Prohormone Processing Enzyme from Ovine Adrenal Medulla
    Volume 246, number 1,2, 44-48 FEB 06940 March 1989 Characterisation and partial purification of a novel prohormone processing enzyme from ovine adrenal medulla N. Tezapsidis and D.C. Parish Biochemistry Group, School of Biological Sciences, University of Sussex, Falmer, Brighton, Sussex, England Received 3 January 1989 An enzymatic activity has been identified which is capable of generating a product chromatographically identical with adrenorphin from the model substrate BAM 12P. This enzyme was purified by gel filtration and ion-exchange chromatog- raphy and characterised as having a molecular mass between 30 and 45 kDa and an acidic pL The enzyme is active at the acid pH expected in the secretory vesicle interior and is inhibited by EDTA, suggesting that it is a metalloprotease. This activity could not be mimicked by incubation with lysosomal fractions and it meets the criteria to be considered as a possible prohormone processing enzyme. Prohormone processing; Adrenorphin; Secretory vesiclepurification 1. INTRODUCTION The purification of an endopeptidase responsi- ble for the generation of adrenorphin was under- Active peptide hormones are released from their taken, using the ovine adrenal medulla as a source. precursors by endoproteolytic cleavage at highly Adrenorphin is known to be located in the adrenal specific sites. The commonest of these is cleavage medulla of all species so far investigated [6]. at pairs of basic residues such as lysine and Secretory vesicles (also known as chromaffin arginine [1,2]. However another common class of granules) were isolated as a preliminary purifica- processing sites are known to be at single arginine tion step, since it is known that prohormone pro- residues, adjacent to a proline [3].
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  • TCPDF Example
    Chapter 2 : Gentaur Products List • Ac Leu28 31 Neuropeptide Y 24 36 • Sar1 Ala8 Angiotensin II Gly Ser Arg Ile Asp Arg Ile Gly Ala Gln Ser Gly Met Gly Cys • Gln18 Platelet Factor 4 15 22 human • Sar1 Gly8 Angiotensin II Gly Arg Arg Phe MW 2561 87 Disulfide bridge Cys4 Cys20 • Platelet Factor 4 58 70 human AA Pro Leu Tyr Lys Lys Ile • Sar1 Thr8 Angiotensin II MW 2561 87 Ile Lys Lys Leu Leu Glu Ser MW 1573 01 • Sar1 Val5 Ala8 Angiotensin II • Biotin • Pneumadin human AA Ala Gly Glu Pro Lys Leu Asp Ala • Sar1 Angiotensin I II 1 7 amide • Atrial Natriuretic Factor 1 29 chicken AA Met Met Arg Asp Gly Val NH2 MW 955 08 • Val4 Angiotensin III Ser Gly Cys Phe Gly Arg Arg Ile Asp Arg Ile Gly Ser Leu Ser • Pneumadin rat AA Tyr Gly Glu Pro Lys Leu Asp Ala Gly Val • Brain Injury Derived Neurotrophic Peptide AA Glu Ala Leu Gly Met Gly Cys Asn Gly Ser Arg Lys Asn Disulfide bridge NH2 MW 1047 18 Glu Leu Ala Arg Gly Ala Ile Phe Gln Ala NH2 MW 1387 61 Cys7 Cys23 MW • Osteostatin amide human AA Thr Arg Ser Ala Trp Leu Asp • Neurotrophic Factor for Retinal Cholinergic Neurons AA • Atrial Natriuretic Factor 3 28 human AA Arg Arg Ser Ser Ser Gly Val Thr Gly Ser Gly Leu Glu Gly Asp His Leu Ser Tyr Leu Leu Pro Ala Gln Val Asn Ile Asp MW 1145 33 Cys Phe Gly Gly Arg Met Asp Arg Ile Gly Ala Gln Ser Gly Asp Thr Ser Thr Thr Ser Leu Glu Leu Asp Ser Arg NH2 MW • Biotin Obestatin human AA Biotin Phe Asn Ala Pro Phe Leu Gly Cys Asn Ser Phe Arg Tyr Disulfide bridge Cys5 3450 64 Asp Val Gly Ile Lys Leu Ser Gly Val Gln Tyr Gln Gln His Ser Cys21 MW 2880 3 • Osteostatin
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  • Table of Contents
    Table of Contents Table of Contents 4 Educational Resources 5 Payment Options 7 Getting Started With Our Lab Services 8 Frequently Asked Questions 9 Testimonials 10 Tests 11 Organic Acids Test (OAT) 12 Sample Test 13 Report Analysis 14 IgG Food Allergy Test w/ Candida 15 Sample Report 16 Metals Tests 17 Gluten / Casein Peptides Test 19 IgE Food and Inhalant Allergy Tests 20 Hormone Panels 21 Amino Acids Tests 22 Vitamin D Test 23 Advanced Cholesterol Profile 24 Immune Deficiency Profile 25 Comprehensive Stool Analysis 26 Copper / Zinc Profile 27 Comprehensive Fatty Acids Test 28 GPL-3 29 GPL-4 30 OAT + IgG Food Allergy Test w/ Candida Combo 31 Comprehensive Test Panels 32 Comprehensive Autism Panel 32 Comprehensive AD(H)D Panel 32 Comprehensive Mental Health Panel 32 Comprehensive Wellness Panel 32 The Great Plains Laboratory, Inc. Information Guide A research-based clinical laboratory offering services worldwide. 1 William Shaw, Ph.D., Director | 11813 West 77th Street, Lenexa, KS 66214 | (913) 341-8949 | Fax (913) 341-6207call: | (913) www.GPL4U.com 341-8949 The Great Plains Laboratory, Inc. (GPL) is a research-based clinical laboratory that offers testing for nutritional factors in chronic illnesses worldwide. Our company was founded in 1996 and is currently serving more than 100 countries. We provide a variety of metabolic tests that are not routinely available through other laboratories, and have tested more than 200,000 patients with autism and other related disorders. Our goal is to help people achieve their maximum potential through quality laboratory testing, knowledgeable staff, and excellent customer service.
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  • Genscript Product Catalog 2013-2014 Genscript Product Catalog
    GenScript Product Catalog 2013-2014 GenScript Product Catalog www.genscript.com GenScript USA Inc. 860 Centennial Ave. Piscataway, NJ 08854USA Tel: 1-732-885-9188 / 1-732-885-9688 Toll-Free Tel: 1-877-436-7274 Fax: 1-732-210-0262 / 1-732-885-5878 Email: [email protected] Nucleic Acid Purification and Analysis Business Development Tel: 1-732-317-5088 PCR PCR and Cloning Email: [email protected] Protein Analysis Antibodies 2013-2014 Peptides Welcome to GenScript GenScript USA Incorporation, founded in 2002, is a fast-growing biotechnology company and contract research organization (CRO) specialized in custom services and consumable products for academic and pharmaceutical research. Built on our assembly-line mode, one-stop solutions, continuous improvement, and stringent IP protection, GenScript provides a comprehensive portfolio of products and services at the most competitive prices in the industry to meet your research needs every day. Over the years, GenScript’s scientists have developed many innovative technologies that allow us to maintain our position at the cutting edge of biological and medical research while offering cost-effective solutions for customers to accelerate their research. Our advanced expertise includes proprietary technology for custom gene synthesis, OptimumGeneTM codon optimization technology, CloneEZ® seamless cloning technology, FlexPeptideTM technology for custom peptide synthesis, BacPowerTM technology for protein expression and purification, T-MaxTM adjuvant and advanced nanotechnology for custom antibody production, as well as our ONE-HOUR WesternTM detection system and eStain® protein staining system. GenScript offers a broad range of reagents, optimized kits, and system solutions to help you unravel the mysteries of biology. We also provide a comprehensive portfolio of customized services that include Bio-Reagent, Bio-Assay, Lead Optimization, and Antibody Drug Development which can be effectively integrated into your value chain and your operations.
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  • Pharmaceutical Nasal Compositions and Methods for Peptid Treatment
    (19) TZZ ¥Z_T (11) EP 2 283 850 B1 (12) EUROPEAN PATENT SPECIFICATION (45) Date of publication and mention (51) Int Cl.: of the grant of the patent: A61K 31/485 (2006.01) A61K 9/107 (2006.01) 25.04.2018 Bulletin 2018/17 A61K 9/08 (2006.01) A61K 38/02 (2006.01) A61K 38/25 (2006.01) A61K 31/12 (2006.01) (2006.01) (2006.01) (21) Application number: 10186116.9 A61K 31/365 A61K 9/00 A61K 47/32 (2006.01) A61K 47/22 (2006.01) A61K 47/06 (2006.01) A61K 47/08 (2006.01) (22) Date of filing: 07.03.2005 A61K 47/10 (2017.01) A61K 47/18 (2017.01) A61K 47/44 (2017.01) (54) Pharmaceutical nasal compositions and methods for peptid treatment Pharmazeutische nasale Zubereitungen und Peptidbehandlungen Compositions pharmaceutiques nasales et traitements aux peptides (84) Designated Contracting States: • Reppucci, Carl AT BE BG CH CY CZ DE DK EE ES FI FR GB GR North Andover, MA 01845 (US) HU IE IS IT LI LT LU MC NL PL PT RO SE SI SK TR (74) Representative: Chajmowicz, Marion et al (30) Priority: 05.03.2004 US 895465 Becker & Associés 25, rue Louis Le Grand (43) Date of publication of application: 75002 Paris (FR) 16.02.2011 Bulletin 2011/07 (56) References cited: (62) Document number(s) of the earlier application(s) in WO-A-03/000158 accordance with Art. 76 EPC: 05724894.0 / 1 773 369 Remarks: Thefile contains technical information submitted after (73) Proprietor: CPEX Pharmaceuticals, Inc. the application was filed and not included in this Exeter, NH 03833 (US) specification (72) Inventors: • Gyurik, Robert Exeter, NH 03833 (US) Note: Within nine months of the publication of the mention of the grant of the European patent in the European Patent Bulletin, any person may give notice to the European Patent Office of opposition to that patent, in accordance with the Implementing Regulations.
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  • Opioid Imaging
    529 NEUROIMAGING CLINICS OF NORTH AMERICA Neuroimag Clin N Am 16 (2006) 529–552 Opioid Imaging Alexander Hammers, PhDa,b,c,*, Anne Lingford-Hughes, PhDd,e - Derivation, release, peptide action, Changes in receptor availability in pain and metabolism and discomfort: between-group - Receptors and ligands comparisons Receptors Direct intrasubject comparisons of periods Species differences with pain and pain-free states Regional and layer-specific subtype - Opioid imaging in epilepsy distributions Focal epilepsies Ligands Idiopathic generalized epilepsy - Positron emission tomography imaging Summary of opioid receptors - Opioid imaging in other specialties Introduction PET imaging Movement disorders Quantification of images Dementia Available ligands and their quantification Cardiology - Opioid receptor imaging in healthy - Opioid imaging in psychiatry: addiction volunteers - Summary - Opioid imaging in pain-related studies - Acknowledgments - References Opioids derive their name from the Greek o´pioy agonists provided evidence for the existence of mul- for poppy sap. Various preparations of the opium tiple receptors [4]. In the early 1980s, there was ev- poppy Papaver somniferum have been used for pain idence for the existence of at least three types of relief for centuries. Structure and stereochemistry opiate receptors: m, k, and d [5,6]. A fourth ‘‘orphan’’ are essential for the analgesic actions of morphine receptor (ORL1 or NOP1) displays a high degree and other opiates, leading to the hypothesis of the of structural homology with conventional opioid existence of specific receptors. Receptors were iden- receptors and was identified through homology tified simultaneously by three laboratories in 1973 with the d receptor [7], but the endogenous ligand, [1–3]. The different pharmacologic activity of orphanin FQ/nociceptin, does not interact directly Dr.
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