DOCSLIB.ORG

Part 7. Indexes

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read full-text
Part 7. Indexes Peptide Sequences Index Part 7. Indexes Index A. Peptide Sequences White & White - Proteins, Peptides & Amino Acids SourceBook 975 Peptide Sequences Index Ala-Ala-Pro-Lys . 218 A Ala-Ala-Pro-Met . 218 Ala-Ala-Pro-Nle . 218 Abu-Ala· 208 Ala-Ala-Pro-Nva . 218 Abu-Arg . 208, 740 Ala-Ala-Pro-Orn • 218 Abu-Asn-Arg-Leu-Glu-Ala-Ser-Ser-Arg-Ser-Ser-Lys . 208 Ala-Ala-Pro-Phe . 209, 218, 219, 385 Abu-Gly . 208, 369 Ala-Ala-Pro-Val . 217, 219, 220 Abu-Ile-His-Pro-Phe-His-Leu-Val-Ile-His-Thr· 208 Ala-Ala-Ser-Thr-Thr-Thr-Asn-Tyr-Thr . 220 Abu-Ser-Gln-Asn-Tyr-Pro-lie-Val-Gin· 208 Ala-Ala-Trp-Phe-Lys· 220 Abz-Ala-Ala-Phe-Phe . 208 Ala-Ala-Trp-Phe-Pro-pro-Nle . 220 Abz-Ala-Arg-Val-Nle-Phe-Glu-Ala-Nle . 208 Ala-Ala-Tyr . 221 Abz-Ala-Gly-Leu-Ala . 208 Ala-Ala-Tyr-Ala . 221 Abz-Ala-Phe-Ala-Phe-Asp-Val-Phe-Tyr-Asp . 209 Ala-Ala-Tyr-Ala-Ala . 221 Abz-Arg-Val-Lys-Arg-Gly-Leu-Ala-Tyr-Asp . 209 Ala-Ala-Val· 221, 222 Abz-Arg-Val-Nle-Phe-Glu-Ala-Nle . 209 Ala-Ala-Val-Ala • 221, 222 Abz-Gln-Val-Val-Ala-Gly-Ala . 209 Ala-Ala-Val-Ala-Leu-Leu-Pro-Ala-Val-Leu-Leu-Ala-Leu-Leu- Abz-Glu-Thr-Leu-Phe-Gln-Gly-Pro-Val-Phe . 209 Ala-Pro-Asp-Glu-Val-Asp . 221 Abz-Gly . 209, 385 Ala-Ala-Val-Ala-Leu-Leu-Pro-Ala-Val-Leu-Leu-Ala-Leu-Leu­ Abz-Gly-Ala-Ala-Pro-Phe-Tyr-Asp . 209 Ala-Pro-Ile-Glu-Thr-Asp . 221 Abz-Gly-Gly-Ala-Ser-Ser-Arg-Leu-Tyr-Arg . 209 Ala-Ala-Val-Ala-Leu-Leu-Pro-Ala-Val-Leu-Leu-Ala-Leu-Leu­ Abz-Gly-Phe-Pro . 209 Ala-Pro-Leu-Glu-His-Asp . 221 Abz-Gly-Pro-Leu-Ala . 209 Ala-Ala-Val-Ala-Leu-Leu-Pro-Ala-Val-Leu-Leu-Ala-Leu-Leu­ Abz-Gly-Trp-Thr-Leu-Asn-Ser-Ala-Gly-Tyr-Leu-Lys-Tyr . Ala-Pro-Leu-Glu-Val-Asp . 221 209 Ala-Ala-Val-Ala-Leu-Leu-Pro-Ala-Val-Leu-Leu-Ala-Leu-Leu­ Abz-Lys-Ala-Arg-Val-Nle-Phe-Glu-Ala-Nle . 209 Ala-Pro-Tyr-Val-Ala-Asp • 222 Abz-Lys-Pro-Leu-Gly . 209 Ala-Ala-Val-Ala-Leu-Leu-Pro-Ala-Val-Leu-Leu-Ala-Leu-Leu­ Abz-Lys-Pro-Leu-Gly-Leu-Ala-Arg . 209 Ala-Pro-Val-Gln-Arg-Asn-Gly-Gln-Lys-Leu-Met-Pro • 222 Abz-Thr-Ile-Nle-Phe-Gln-Arg· 209 Ala-Ala-Val-Ala-Leu-Leu-Pro-Ala-Val-Leu-Leu-Ala-Leu-Leu­ Aib-His-Nal-Nal-Phe-Lys . 210 Ala-Pro-Val-Gln-Arg-Lys-Arg-Gln-Lys-Leu-Met-Pro . 222 Ala-Abu· 210, 541 Ala-Ala-Val-Ala-Leu-Leu-Pro-Ala-Val-Leu-Leu-Ala-Leu-Leu­ Ala-Ala· 209, 210, 211, 212, 213, 214, 215, 216, 217, Ala-Pro-Val-Glu-lIe-Asp . 222 218, 219, 220, 221, 222, 238, 246, 307, 313, 353, 354, Ala-Ala-Val-Asp-Leu-Ser-His-Phe-Leu-Lys-Glu-Lys • 222 375, 385,422,429,471, 500, 528, 548, 567, 613, 663 Ala-Arg . 208, 209, 222, 223, 224, 246, 253, 256, 257, Ala-Ala-Abz . 212 258,277,284,287,305,306,313,317,344,369,373, Ala-Ala-Ala· 212, 213, 214, 238, 246, 313 380,422,427,429,432,433,440,447,487,492,495, Ala-Ala-Ala-Ala . 213, 313 496,517,518, 519, 522, 549, 550, 554, 569, 598, 599, Ala-Ala-Ala-Ala-Ala . 213, 313 600, 609, 625, 631, 637, 638, 639 Ala-Ala-Ala-Ala-Ala-Ala . 213, 313 Ala-Arg-Arg . 222, 223 Ala-Ala-Ala-Ala-Glu-Glu-Glu-Glu-Glu . 213 Ala-Arg-Arg-Ala . 223 Ala-Ala-Ala-Tyr . 214 Ala-Arg-Arg-Asn-Arg-Arg-Arg-Arg-Trp-Arg-Glu-Arg-Gln-Arg Ala-Ala-Ala-Tyr-Ala . 214 ·223 Ala-Ala-Ala-Tyr-Ala-Ala . 214 Ala-Arg-Arg-Pro-Glu-Gly-Arg-Thr-Trp-Ala-Gln-Pro-Gly-Tyr . Ala-Ala-Ala-Tyr-Gly-Gly-Phe-Leu . 214 223 Ala-Ala-Ala-Tyr-Gly-Gly-Phe-Met • 214 Ala-Arg-Gly-Ile-Lys-Gly-Ile-Arg-Gly-Phe-Ser-Gly . 223 Ala-Ala-Asn . 214, 313, 353, 354, 613 Ala-Arg-Leu-Asp-Th r-Ser-Ser-Gln-Phe-Arg-Lys-Lys-Trp­ Ala-Ala-Asp' 214 Asn-Lys-Trp-Ala-Leu-Ser-Arg . 223 Ala-Ala-Asp-Ile-Ser-Gln-Trp-Ala-Gly-Pro-Leu • 214 Ala-Arg-Leu-Asp-Val-Ala-Ala-Glu-Phe-Arg-Lys-Lys-Trp-Asn­ Ala-Ala-Gin· 214 Lys-Trp-Ala-Leu-Ser-Arg . 223 Ala-Ala-Gly . 215, 500, 663 Ala-Arg-Leu-Asp-Val-Ala-Ser-Glu-Phe-Arg-Lys-Lys-Trp­ Ala-Ala-Gly-Ile-Gly-lIe-Leu-Thr-Val . 215 Asn-Lys-Trp-Ala-Leu-Ser-Arg . 223 Ala-Ala-Gly-Met-Gly-Phe-Phe-Gly-Ala-Arg . 215 Ala-Arg-Lys-pSer-Thr-Gly-Gly-Lys-Ala-Pro-Arg-Lys-Gln- Ala-Ala-Gly-Pro-Glu-Met-Val-Arg-Gly-Gln-Val-Phe-Cys . Leu-Cys • 223 215 Ala-Arg-Pro-Ala-Lys . 223 Ala-Ala-Leu· 215, 307 Ala-Arg-Pro-Gly-Tyr-Leu-Ala-Phe-Pro-Arg-Met . 223 Ala-Ala-Leu-Asp-Leu-Ser-His-Phe-Leu-Lys-Glu-Lys . 215 Ala-Arg-Ser-Ala-Pro-Thr-Pro-Met-Ser-Pro-Tyr • 223 Ala-Ala-Leu-Val-Arg-Gln-Met-Ser-Val-Ala-Phe-Phe-Phe-Lys Ala-Arg-Thr-Lys-Gln-Thr-Ala-Arg-Lys-Ser-Th r-Gly-Gly-Lys- ·215 Ala-pro-Arg-Lys-Gln-Leu-Cys . 224 Ala-Ala-Lys . 215, 216, 429 Ala-Arg-Tyr-Tyr-Ser-Ala-Leu-Arg-His-Tyr-Ile-Asn-Leu-lIe- Ala-Ala-Lys-Ile-Gln-Ala-Ser-Phe-Arg-Gly-His-Met-Ala-Arg- Thr-Arg-Gln-Arg-Tyr . 224, 496, 554, 569, 637, 638 Lys-Lys· 215, 216 Ala-Arg-Val-Leu-Ala-Glu-Ala . 224 Ala-Ala-Phe . 216, 217, 567 Ala-Arg-Val-Nle-Phe-Glu-Ala-Nle . 224 Ala-Ala-Pro· 209, 217, 218, 219, 220, 385 Ala-Arg-Val-Nle-Tyr-Glu-Ala-Nle . 224 Ala-Ala-Pro-Abu . 217 Ala-Asn • 216, 224, 225, 247, 313, 316, 518, 577, 593, Ala-Ala-Pro-Ala • 217 621 Ala-Ala-Pro-Ala-Ala . 217 Ala-Asn-GI u-Arg-Ala-Asp-Leu-lie-Ala -Tyr-Leu-Gln-Gln-Ala­ Ala-Ala-Pro-Arg . 217 Thr-Lys . 224 Ala-Ala-Pro-Asp . 217 Ala-Asn-Phe-Leu-Val-Trp-Glu-Ile-Val-Arg-Lys-Lys-Pro • 224 Ala-Ala-Pro-Glu . 217 Ala-Asn-Pro-Asp-Cys-Lys-Thr-Ile-Leu-Lys-Ala- Leu-Gly-Pro­ Ala-Ala-Pro-Ile . 218 Ala-Ala-Thr . 224 Ala-Ala-Pro-Leu . 218 976 User's Guide pp. 1-2, Glossary/Indexes pp. 963-1063 Peptide Sequences Index Ala-Asp· 214, 224, 225, 236, 245, 246, 253, 365,487, Ala-Gly-Asn-Lys-Val-Ile-Ser-Pro-Ser-Glu-Asp-Arg-Arg-GIn­ 488, 528, 581, 599, 600, 628, 668, 669 Cys·231 Ala-Asp-Ala-Gln-His-Ala-Th r-Pro-Pro-Ly-Lys-Lys-Arg-Lys­ Ala-Gly-Asp-Val . 231 Val-Glu-Asp-Pro-Lys-Asp-Phe . 224 Ala-Gly-Cys-Lys-Asn-Phe-Phe-D-Trp-Lys-Thr-Phe-Thr-Ser­ Ala-Asp-Ala-Gln-His-Ala-Thr-Pro-Pro-Lys-Lys-Lys-Arg-Lys­ Cys . 231, 232 Val-Glu-Asp-Pro-Lys-Asp-Phe . 224, 225 Ala-Gly-Cys-Lys-Asn-Phe-Phe-Trp-Lys-Thr-Phe-Thr-Ser­ Ala-Asp-Leu-Ile-Ala-Tyr-Leu . 225 Cys . 231, 232 Ala-Asp-Lys-Ala-Asp-Val-Asn-Val-Leu-Thr-Lys-Ala-Lys-Ser­ Ala-Gly-Cys-Lys-Asn-Phe-Phe-Trp-Lys-Thr-Tyr-Thr-Ser-Cys Gin· 225 ·232,233 Ala-Asp-Ser-Asp-Gly-Lys . 225 Ala-Gly-Cys-Lys-Phe-Phe-Asp-Trp-Lys-Thr-Phe-Thr-Asp- Ala-Asp-Ser-Gly-Glu-Gly-Asp-Phe-Leu-Ala-Glu-Gly-Gly-Gly­ Ser-Cys . 233 Val-Arg . 225 Ala-Gly-Cys-Tyr-Phe-Gln-Asn-Cys-Pro-Arg-Gly . 233 Ala-Asp-Val-Asn-Val-Leu-Thr-Lys-Ala-Lys-Ser-Gln . 225, Ala-Gly-Gln-Trp-Phe-Gly-Asp . 233 245 Ala-Gly-Glu-Gly-Leu-Asn-Ser-Gln-Phe-Trp-Ser-Leu-Ala-Ala- Ala-Asp-Val-Asp-Val-Leu-Thr-Lys-Ala-Lys-Ser-Gln . 225, Pro-Gln-Arg-Phe . 233 245,487,628 Ala-Gly-Glu-Gly-Leu-Ser-Ser-Pro-Phe-Trp-Ser-Leu-Ala-Ala- Ala-Cys-Ala-Trp-Leu-Glu-Ala-Gln-Glu-Glu-Glu-Glu-Val-GIy . Pro-Gln-Arg-Phe . 233 225 Ala-Gly-Glu-Pro-Lys-Leu-Asp-Ala-Gly-Val . 233 Ala-Cys-Asp-Thr-Ala-Thr-Cys-Va1-Thr-His-Arg-Leu-Ala-Gly­ Ala-Gly-Glu-Ser . 233 Leu-Leu-Ser-Arg-Ser . 226, 227 Ala-Gly-Gly . 233, 234, 261, 385 Ala-Cys-Tyr-Cys-Arg-Ile-Pro-Ala -Cys-Ile-Ala-Gly-Glu-Arg­ Ala-Gly-Gly-Gly . 233, 234 Arg-Tyr-Gly-Thr-Cys-Ile-Tyr-Gln-Gly-Arg-Leu-Trp-Ala­ Ala-Gly-Gly-Gly-Gly . 234 Phe-Cys-Cys . 227 Ala-Gly-Ile-Val-Gln-Gln-Gln-Gln-Gln-Leu-Leu-Asp-Val-Va1- Ala-Cys-Tyr-Trp-Lys-Val-Cys-Thr . 227 Lys-Arg-Gln-Gln-Glu-Leu . 234 Ala-Gin· 225, 227, 228, 285, 422, 430, 488, 490, 568, Ala-Gly-Phe-Gly .
Load more

Recommended publications
  • The 2021 List of Pharmacological Classes of Doping Agents and Doping Methods
    BGBl. III - Ausgegeben am 8. Jänner 2021 - Nr. 1 1 von 23 The 2021 list of pharmacological classes of doping agents and doping methods www.ris.bka.gv.at BGBl. III - Ausgegeben am 8. Jänner 2021 - Nr. 1 2 von 23 www.ris.bka.gv.at BGBl. III - Ausgegeben am 8. Jänner 2021 - Nr. 1 3 von 23 THE 2021 PROHIBITED LIST WORLD ANTI-DOPING CODE DATE OF ENTRY INTO FORCE 1 January 2021 Introduction The Prohibited List is a mandatory International Standard as part of the World Anti-Doping Program. The List is updated annually following an extensive consultation process facilitated by WADA. The effective date of the List is 1 January 2021. The official text of the Prohibited List shall be maintained by WADA and shall be published in English and French. In the event of any conflict between the English and French versions, the English version shall prevail. Below are some terms used in this List of Prohibited Substances and Prohibited Methods. Prohibited In-Competition Subject to a different period having been approved by WADA for a given sport, the In- Competition period shall in principle be the period commencing just before midnight (at 11:59 p.m.) on the day before a Competition in which the Athlete is scheduled to participate until the end of the Competition and the Sample collection process. Prohibited at all times This means that the substance or method is prohibited In- and Out-of-Competition as defined in the Code. Specified and non-Specified As per Article 4.2.2 of the World Anti-Doping Code, “for purposes of the application of Article 10, all Prohibited Substances shall be Specified Substances except as identified on the Prohibited List.
    [Show full text]
  • 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.
    [Show full text]
  • Biological, Physiological, Pathophysiological, and Pharmacological Aspects of Ghrelin
    0163-769X/04/$20.00/0 Endocrine Reviews 25(3):426–457 Printed in U.S.A. Copyright © 2004 by The Endocrine Society doi: 10.1210/er.2002-0029 Biological, Physiological, Pathophysiological, and Pharmacological Aspects of Ghrelin AART J. VAN DER LELY, MATTHIAS TSCHO¨ P, MARK L. HEIMAN, AND EZIO GHIGO Division of Endocrinology and Metabolism (A.J.v.d.L.), Department of Internal Medicine, Erasmus Medical Center, 3015 GD Rotterdam, The Netherlands; Department of Psychiatry (M.T.), University of Cincinnati, Cincinnati, Ohio 45237; Endocrine Research Department (M.L.H.), Eli Lilly and Co., Indianapolis, Indiana 46285; and Division of Endocrinology (E.G.), Department of Internal Medicine, University of Turin, Turin, Italy 10095 Ghrelin is a peptide predominantly produced by the stomach. secretion, and influence on pancreatic exocrine and endo- Ghrelin displays strong GH-releasing activity. This activity is crine function as well as on glucose metabolism. Cardiovas- mediated by the activation of the so-called GH secretagogue cular actions and modulation of proliferation of neoplastic receptor type 1a. This receptor had been shown to be specific cells, as well as of the immune system, are other actions of for a family of synthetic, peptidyl and nonpeptidyl GH secre- ghrelin. Therefore, we consider ghrelin a gastrointestinal tagogues. Apart from a potent GH-releasing action, ghrelin peptide contributing to the regulation of diverse functions of has other activities including stimulation of lactotroph and the gut-brain axis. So, there is indeed a possibility that ghrelin corticotroph function, influence on the pituitary gonadal axis, analogs, acting as either agonists or antagonists, might have stimulation of appetite, control of energy balance, influence clinical impact.
    [Show full text]
  • 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.
    [Show full text]
  • 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.
    [Show full text]
  • Drug Testing Program
    DRUG TESTING PROGRAM Copyright © 2021 CrossFit, LLC. All Rights Reserved. CrossFit is a registered trademark ® of CrossFit, LLC. 2021 DRUG TESTING PROGRAM 2021 DRUG TESTING CONTENTS 1. DRUG-FREE COMPETITION 2. ATHLETE CONSENT 3. DRUG TESTING 4. IN-COMPETITION/OUT-OF-COMPETITION DRUG TESTING 5. REGISTERED ATHLETE TESTING POOL (OUT-OF-COMPETITION DRUG TESTING) 6. REMOVAL FROM TESTING POOL/RETIREMENT 6A. REMOVAL FROM TESTING POOL/WATCH LIST 7. TESTING POOL REQUIREMENTS FOLLOWING A SANCTION 8. DRUG TEST NOTIFICATION AND ADMINISTRATION 9. SPECIMEN ANALYSIS 10. REPORTING RESULTS 11. DRUG TESTING POLICY VIOLATIONS 12. ENFORCEMENT/SANCTIONS 13. APPEALS PROCESS 14. LEADERBOARD DISPLAY 15. EDUCATION 16. DIETARY SUPPLEMENTS 17. TRANSGENDER POLICY 18. THERAPEUTIC USE EXEMPTION APPENDIX A: 2020-2021 CROSSFIT BANNED SUBSTANCE CLASSES APPENDIX B: CROSSFIT URINE TESTING PROCEDURES - (IN-COMPETITION) APPENDIX C: TUE APPLICATION REQUIREMENTS Drug Testing Policy V4 Copyright © 2021 CrossFit, LLC. All Rights Reserved. CrossFit is a registered trademark ® of CrossFit, LLC. [ 2 ] 2021 DRUG TESTING PROGRAM 2021 DRUG TESTING 1. DRUG-FREE COMPETITION As the world’s definitive test of fitness, CrossFit Games competitions stand not only as testaments to the athletes who compete but to the training methodologies they use. In this arena, a true and honest comparison of training practices and athletic capacity is impossible without a level playing field. Therefore, the use of banned performance-enhancing substances is prohibited. Even the legal use of banned substances, such as physician-prescribed hormone replacement therapy or some over-the-counter performance-enhancing supplements, has the potential to compromise the integrity of the competition and must be disallowed. With the health, safety, and welfare of the athletes, and the integrity of our sport as top priorities, CrossFit, LLC has adopted the following Drug Testing Policy to ensure the validity of the results achieved in competition.
    [Show full text]
  • 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].
    [Show full text]
  • (12) United States Patent (10) Patent No.: US 9,687,445 B2 Li (45) Date of Patent: Jun
    USOO9687445B2 (12) United States Patent (10) Patent No.: US 9,687,445 B2 Li (45) Date of Patent: Jun. 27, 2017 (54) ORAL FILM CONTAINING OPIATE (56) References Cited ENTERC-RELEASE BEADS U.S. PATENT DOCUMENTS (75) Inventor: Michael Hsin Chwen Li, Warren, NJ 7,871,645 B2 1/2011 Hall et al. (US) 2010/0285.130 A1* 11/2010 Sanghvi ........................ 424/484 2011 0033541 A1 2/2011 Myers et al. 2011/0195989 A1* 8, 2011 Rudnic et al. ................ 514,282 (73) Assignee: LTS Lohmann Therapie-Systeme AG, Andernach (DE) FOREIGN PATENT DOCUMENTS CN 101703,777 A 2, 2001 (*) Notice: Subject to any disclaimer, the term of this DE 10 2006 O27 796 A1 12/2007 patent is extended or adjusted under 35 WO WOOO,32255 A1 6, 2000 U.S.C. 154(b) by 338 days. WO WO O1/378O8 A1 5, 2001 WO WO 2007 144080 A2 12/2007 (21) Appl. No.: 13/445,716 (Continued) OTHER PUBLICATIONS (22) Filed: Apr. 12, 2012 Pharmaceutics, edited by Cui Fude, the fifth edition, People's Medical Publishing House, Feb. 29, 2004, pp. 156-157. (65) Prior Publication Data Primary Examiner — Bethany Barham US 2013/0273.162 A1 Oct. 17, 2013 Assistant Examiner — Barbara Frazier (74) Attorney, Agent, or Firm — ProPat, L.L.C. (51) Int. Cl. (57) ABSTRACT A6 IK 9/00 (2006.01) A control release and abuse-resistant opiate drug delivery A6 IK 47/38 (2006.01) oral wafer or edible oral film dosage to treat pain and A6 IK 47/32 (2006.01) substance abuse is provided.
    [Show full text]
  • B1–Proteases As Molecular Targets of Drug Development
    Abstracts B1–Proteases as Molecular Targets of Drug Development B1-001 lin release from the beta cells. Furthermore, GLP-1 also stimu- DPP-IV structure and inhibitor design lates beta cell growth and insulin biosynthesis, inhibits glucagon H. B. Rasmussen1, S. Branner1, N. Wagtmann3, J. R. Bjelke1 and secretion, reduces free fatty acids and delays gastric emptying. A. B. Kanstrup2 GLP-1 has therefore been suggested as a potentially new treat- 1Protein Engineering, Novo Nordisk A/S, Bagsvaerd, Denmark, ment for type 2 diabetes. However, GLP-1 is very rapidly degra- 2Medicinal Chemistry, Novo Nordisk A/S, Maaloev, Denmark, ded in the bloodstream by the enzyme dipeptidyl peptidase IV 3Discovery Biology, Novo Nordisk A/S, Maaloev, DENMARK. (DPP-IV; EC 3.4.14.5). A very promising approach to harvest E-mail: [email protected] the beneficial effect of GLP-1 in the treatment of diabetes is to inhibit the DPP-IV enzyme, thereby enhancing the levels of The incretin hormones GLP-1 and GIP are released from the gut endogenously intact circulating GLP-1. The three dimensional during meals, and serve as enhancers of glucose stimulated insu- structure of human DPP-IV in complex with various inhibitors 138 Abstracts creates a better understanding of the specificity and selectivity of drug-like transition-state inhibitors but can be utilized for the this enzyme and allows for further exploration and design of new design of non-transition-state inhibitors that compete for sub- therapeutic inhibitors. The majority of the currently known DPP- strate binding. Besides carrying out proteolytic activity, the IV inhibitors consist of an alpha amino acid pyrrolidine core, to ectodomain of memapsin 2 also interacts with APP leading to which substituents have been added to optimize affinity, potency, the endocytosis of both proteins into the endosomes where APP enzyme selectivity, oral bioavailability, and duration of action.
    [Show full text]
  • 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.
    [Show full text]
  • Isovaline Monohydrate
    organic compounds Acta Crystallographica Section E Structure Reports Online ISSN 1600-5368 Isovaline monohydrate Ray J. Butcher,a* Greg Brewer,b Aaron S. Burtonc and Experimental d Jason P. Dworkin Crystal data ˚ 3 C5H11NO2ÁH2O V = 736.10 (12) A aDepartment of Chemistry, Howard University, 525 College Street NW, Washington, Mr = 135.16 Z =4 DC 20059, USA, bDepartment of Chemistry, Catholic University of America, Orthorhombic, P212121 Cu K radiation Washington, DC 20064, USA, cNASA Johnson Space Center, Astromaterial and a = 5.9089 (5) A˚ = 0.84 mmÀ1 Exploration Science Directorate, Houston, TX 77058, USA, and dSolar System b = 10.4444 (10) A˚ T = 123 K Exploration Division, NASA Goddard Space Flight Center, Greenbelt, MD 20771, c = 11.9274 (11) A˚ 0.48 Â 0.08 Â 0.06 mm USA Correspondence e-mail: [email protected] Data collection Agilent Xcalibur (Ruby, Gemini) 1662 measured reflections Received 23 October 2013; accepted 20 November 2013 diffractometer 1204 independent reflections Absorption correction: multi-scan 1072 reflections with I >2(I) (CrysAlis PRO; Agilent, 2012) Rint = 0.072 ˚ Key indicators: single-crystal X-ray study; T = 123 K; mean (C–C) = 0.005 A; Tmin = 0.383, Tmax = 1.000 R factor = 0.056; wR factor = 0.162; data-to-parameter ratio = 13.2. Refinement R[F 2 >2(F 2)] = 0.056 H atoms treated by a mixture of The title compound, C5H11NO2ÁH2O, is an isomer of the - wR(F 2) = 0.162 independent and constrained amino acid valine that crystallizes from water in its zwitterion S = 1.11 refinement ˚ À3 form as a monohydrate.
    [Show full text]
  • Serine Proteases with Altered Sensitivity to Activity-Modulating
    (19) & (11) EP 2 045 321 A2 (12) EUROPEAN PATENT APPLICATION (43) Date of publication: (51) Int Cl.: 08.04.2009 Bulletin 2009/15 C12N 9/00 (2006.01) C12N 15/00 (2006.01) C12Q 1/37 (2006.01) (21) Application number: 09150549.5 (22) Date of filing: 26.05.2006 (84) Designated Contracting States: • Haupts, Ulrich AT BE BG CH CY CZ DE DK EE ES FI FR GB GR 51519 Odenthal (DE) HU IE IS IT LI LT LU LV MC NL PL PT RO SE SI • Coco, Wayne SK TR 50737 Köln (DE) •Tebbe, Jan (30) Priority: 27.05.2005 EP 05104543 50733 Köln (DE) • Votsmeier, Christian (62) Document number(s) of the earlier application(s) in 50259 Pulheim (DE) accordance with Art. 76 EPC: • Scheidig, Andreas 06763303.2 / 1 883 696 50823 Köln (DE) (71) Applicant: Direvo Biotech AG (74) Representative: von Kreisler Selting Werner 50829 Köln (DE) Patentanwälte P.O. Box 10 22 41 (72) Inventors: 50462 Köln (DE) • Koltermann, André 82057 Icking (DE) Remarks: • Kettling, Ulrich This application was filed on 14-01-2009 as a 81477 München (DE) divisional application to the application mentioned under INID code 62. (54) Serine proteases with altered sensitivity to activity-modulating substances (57) The present invention provides variants of ser- screening of the library in the presence of one or several ine proteases of the S1 class with altered sensitivity to activity-modulating substances, selection of variants with one or more activity-modulating substances. A method altered sensitivity to one or several activity-modulating for the generation of such proteases is disclosed, com- substances and isolation of those polynucleotide se- prising the provision of a protease library encoding poly- quences that encode for the selected variants.
    [Show full text]