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Arginine Amino Acid
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Editors: Nathan L. Jacobs
Book Description:
Arginine is a conditionally nonessential amino acid, meaning most of the time it can be manufactured by the human body, and does not need to be obtained directly through the diet. Arginine plays an important role in cell division, the healing of wounds, removing ammonia from the body, immune function, and the release of hormones. This book presents topical research in the study of arginine amino acids, including the techniques and methodologies used for the measurement of arginine in different matrixes; alternative metabolic pathways of arginine and their pathophysiological roles; the biosynthesis of arginine in the mammalian liver and kidney; the relationship between the structure and toxicity evaluated by in vitro methods of a series of arginine-based surfactants; the physico-chemical properties of arginine; and the central functions of L-arginine and its metabolites for stress behavior. (Imprint: Nova Biomedical)


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Table of Contents:
Preface

Analytical Methods of the Determination of Arginine Amino Acid;pp. 1-31
(R.M. Callejon, C. Ubeda, A.M. Troncoso, M.L. Morales, Área de Nutrición y Bromatología, Facultad de Farmacia, Universidad de Sevilla, Sevilla, Spain)

Alternative Metabolic Pathways of Arginine and their Pathophysiological Roles;pp. 33-66
(András Hrabák, Zoltán Kukor, Department of Medical Chemistry, Molecular Biology and Pathobiochemistry, Semmelweis University, Budapest, Hungary)

Free Amino Acid Analysis in Natural Matrices;pp. 67-90
(Graciliana Lopes, Patrícia Valentão, Paula B. Andrade, REQUIMTE/Department of Pharmacognosy, Faculty of Pharmacy, Porto University, Porto, Portugal)

Discovery of Argininosuccinate Synthetase and Argininosuccinate Lyase;pp. 91-110
(Olivier Levillain, Université Claude Bernard Lyon I, Physiologie Intégrative, Cellulaire et Moléculaire, UMR 5123 CNRS, Bâtiment, Villeurbanne Cedex, France)

Expression and Localization of Argininosuccinate Synthetase and Argininosuccinate Lyase in the Female and Male Rat Kidneys ;pp. 111-123
(Olivier Levillain, Heinrich Wiesinger, Université Lyon I, Lyon, France, Laboratoire de Physiologie Intégrative, Cellulaire et Moléculaire. CNRS UMR 5123, Bâtiment. R. Dubois, 43, Bvd du 11 Novembre 1918. F-69622 Villeurbanne Cedex, France, and others)

Chemical Structure and Toxicity in Arginine-Based Surfactants;pp. 125-142
(Aurora Pinazo, Lourdes Pérez, Maria Rosa Infante, Maria Pilar Vinardell, Montse Mitjans, Maria Carmen Morán, Verónica Martínez, Institut de Química Avançada de Catalunya, CSIC, Barcelona, Spain, and others)

Arginine: Physico-Chemical Properties, Interactions with Ion-Exchange Membranes, Recovery and Concentration by Electrodialysis;pp. 143-162
(T. Eliseeva, E. Krisilova, G. Oros, V. Selemenev, Voronezh State University, Voronezh, Russia)

Central Functions of L-Arginine and its Metabolites for Stress Behavior;pp. 163-189
(Shozo Tomonaga, D. Michael Denbow, Mitsuhiro Furuse, Laboratory of Advanced Animal and Marine Bioresources, Faculty of Agriculture, Kyushu University, Fukuoka, Japan, and others)

Arginine Requirement and Metabolism in Marine Fish Larvae: Review of Recent Findings;pp. 191-205
(Margarida Saavedra, Instituto Nacional de Investigação Agrária e das Pescas (INIAP/IPIMAR-CRIPSul), Olhão, Portugal)

Arginine-Rich Cell-Penetrating Peptides in Cellular Internalization;pp. 207-218
(Betty Revon Liu, Huey-Jenn Chiang, Han-Jung Lee, Department of Natural Resources and Environmental Studies, National Dong Hwa University, Hualien, Taiwan, and others)

Effects of Deep Sea Water on Changes in Free Amino Acids and Tolerance to Fusarium Root Rot in Myocorrhizal Asparagus Plants;pp. 219-227
(Abu Shamim Mohammad Nahiyan, Mika Yokoyama, Yoichi Matsubara, The United Graduate School of Agricultural Science, Gifu University, Japan, and others)

Influence of Arginine-Containing Peptides on the Haemostasis System;pp. 229-235
(Maria Golubeva, Marina Grigorjeva, Lab. Blood Coagulation, Biology Dept., Leninsky gory, Moscow State University, Moscow, Russia)

Newly identified transcriptional regulation by Mcm1p at ARG1 promoter;pp. 237-249
(Sungpil Yoon, Research Institute, National Cancer Center, 809 Madu 1-dong, Ilsan-gu, Goyang-si Gyeonggi-do, 411-764, Republic of Korea)

Index

   Series:
      Microbiology Research Advances
      Protein Biochemistry, Synthesis, Structure and Cellular Functions
   Binding: Hardcover
   Pub. Date: 2011 - 2nd quarter
   Pages: 7 x 10 (NBC - R) 267 pp.
   ISBN: 978-1-61761-981-6
   Status: AV
  
Status Code Description
AN Announcing
FM Formatting
PP Page Proofs
FP Final Production
EP Editorial Production
PR At Prepress
AP At Press
AV Available
  
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