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Table of Contents:
Preface
Section 1. Introduction
Chapter 1.-An essay of D-amino acid biochemistry: retrospection and perspective; pp. 3-14
(Soda, Japan)
Section 2. Analytical methods of the detection of D-amino acids
Chapter 2.1- Chromatographic determination of free D- and L-amino acids in marine algae; pp. 17-23
(Nagahisa and Yokoyama, Japan)
Chapter 2.2- Determination of acidic D-amino acids and their N-methyl derivatives in bivalves and other mollusks; pp. 25-32
(Yamada et al., Japan)
Chapter 2.3- Purification and determination of N-methyl-D-aspartic acid in biological tissues; pp. 33-40
(D'Aniello, Italy)
Chapter 2.4- A sensitive direct HPLC method for simultaneous determination of N-methyl-(D and L)-aspartate, N-methyl-(D and L)-glutamate and (D and L)-aspartate in biological tissues; pp. 41-47 (Tsesarskaia et al., U.S.A.)
Chapter 2.5- Methods for total determination of D-aspartic acid, D-glutamic acid and N-methyl-D-aspartic acid and for the specific determination of D-aspartic acid; pp. 47-57
(Spinelli et al., Italy)
Chapter 2.6- An improved HPLC method for determination and quantification of D- and L-aspartic acid; pp. 59-64
(Galindo et al., U.S.A.)
Chapter 2.7- Determination of free D-aspartate and D-serine in rat brain and periphery by gas chromatography and high-performance liquid chromatography; pp. 65-73
(Hashimoto and Yoshikawa, Japan)
Chapter 2.8- An LC method for the analysis of D-amino acids; pp. 75-83
(Stenberg, Sweden)
Chapter 2.9- Sensitive determination of D-amino acids in rat brain by HPLC with
a Pirkle-type chiral column, following precolumn fluorescent derivatization with NBD-F; pp. 85-91
(Fukushima et al., Japan)
Chapter 2.10- Determination of small amounts of D-amino acids in mammals using column-switching HPLC; pp. 93-102
(Hamase and Zaitsu, Japan)
Chapter 2.11- Sensitive determination of amino acid enantiomers by CE/LIF; pp. 103-106
(Liu and Zhao, U.S.A.)
Chapter 2.12- Methods of detection for amino acid enatiomers in the vertebrate retina; pp. 107-110
(Miller et al., U.S.A.)
Chapter 2.13- Determination of NG-nitro-arginine enantiomers in rat plasma by capillary electrochromatography with a chiral mobile phase; pp. 111-113
(Xin et al., China)
Chapter 2.14- Analysis of D-amino acids in protein hydrolysates and peptides subjected to Edman degradation; pp. 115-122
(Salzano and Scaloni, Italy)
Chapter 2.15- Quantitative determination of the protein of bacterial origin based on D-amino acid contents; pp. 123-133
(Csapo et al., Hungary)
Chapter 2.16- Detection of D-amino acids by D-amino acid oxidase; pp. 135-148
(Caldinelli et al., Italy)
Section 3. Free D-amino acids in animal tissues and their physiological role
Chapter 3.1- A systematic approach to the brain D-serine system; pp. 151-167
(Nishikawa, Japan)
Chapter 3.2- Immunohistochemical study of D-serine; pp. 169-172 (Semba, Japan)
Chapter 3.3- Immunohistochemistry for D-serine in brain; pp. 173-179 (Schell, U.S.A.)
Chapter 3. 4- Brain slice preparation for evaluation of the pathophysiological functions of D-serine; pp. 181-186
(Katsuki and Akaike, Japan)
Chapter 3.5- Nephrotoxicity of D-serine in rats; pp. 187-190
(Konno, Japan)
Chapter 3.6- Preparation of a polyclonal antiserum against D-aspartate; pp. 191-201
(Lee and Homma, Japan)
Chapter 3.7- Vesicular storage in and secretion of D-aspartate from neuroendocrine cells; pp. 203-213
(Uehara and Moriyama, Japan)
Chapter 3.8- D-Aspartate in frog harderian gland; pp. 215-220 (Monteforte et al., Italy)
Chapter 3.9- The role of D-aspartic acid in the endocrine regulation of the testis: a study in the lizard podarcis s. sicula; pp. 221-230 (Di Fiore and Raucci, Italy)
Chapter 3.10- D-Aspartic acid in the nervous system of a mollusc: immunohistochemical protocol; pp. 231-234
(D'Aniello et al., Italy)
Chapter 3.11- Analysis, distribution, and physiological functions of free D-alanine in aquatic invertebrates; pp. 235-247
(Abe, Japan)
Chapter 3.12- D-Glutamic acid induced muscle contraction in silkworm larva; pp. 249-254
(Hamamoto et al., Japan)
Chapter 3.13- Primary study of D-amino acid accumulation system; pp. 255-258
(Masuda, Japan)
Chapter 3.14- D-Amino acids and immune response; pp. 259-269
(Zisman and Sela, Israel)
Chapter 3.15- Considerations for the use of 'rapid' cell superfusion and voltage clamp to investigate the role of rare amino acids; pp. 271-276
(Brown and Piscopo, Italy)
Chapter 3.16- Are D-amino acids prevalent among eukaryotes?; pp. 277-282
(Nagata, Japan)
Section 4. Free D-amino acid in food stuffs and their nutritional aspects
Chapter 4.1- Nutritional evaluation of D-amino acids; pp. 285-298 (Friedman, U.S.A.)
Chapter 4.2- D-Amino acids in food; pp. 299-315
(Marchelli et al., Italy)
Chapter 4.3- D-Amino acid determination in foods, beverages, and biological samples; pp. 317-336
(Warnke and Armstrong, U.S.A.)
Chapter 4.4- Gas chromatographic determination of D-amino acids in food and beverages; pp. 337-352
(Pätzold and Brückner, Germany)
Section 5. Protein-bound D-amino acids
Chapter 5.1- Detection of the specific D-aspartic acid residues in protein; pp. 355-367
(Fujii, Japan)
Chapter 5.2- Detection of amyloid eta-peptides with L-isoaspartate in Alzheimer's disease; pp. 369-374
(Shimizu and Shirasawa, Japan)
Chapter 5.3- Detection of D-amino acid in peptides by RP-HPLC and mass spectrometry; pp. 375-378
(Ollivaux and Soyez, France)
Chapter 5.4- Determination of D-amino-acid residue in peptides from animal venom by NMR: application to playpus venom peptide CvCNPs; pp. 379-387
(Torres et al.)
Chapter 5.5- Protein L-isoaspartyl-O-methyltransferase catalyzes in situ formation of D-aspartate and D-isoaspartate in proteins; pp. 389-397
(Aswad, USA)
Chapter 5.6- Purification of a novel mammalian proteinase for D-aspartate-containing protein, D-aspartyl endopeptidase (DAEP); pp. 399-401
(Kinouchi, Japan)
Chapter 5.7- Micropurification and structural assay of poly gamma-glutamate, a D-amino acid-containing biopolymer; pp. 403-407 (Ashiuchi and Misono, Japan)
Chapter 5.8- Estimation of chronological age using the aspartic acid racemization method on dentin samples; pp. 409-414
(Ohtani, Japan)
Chapter 5.9- The use of D-amino acids in peptide design; pp. 415-430 (Mahalakshmi and Balaram, India)
Chapter 5.10- Cellular approach of the biogenesis of D-amino-acid containing peptides in eukaryotes: the crustacean model; pp. 431-440 (Soyez, France)
Section 6. Enzymes involved in synthesis and metabolism of D-amino acids
Chapter 6.1- Purification of alanine racemase from Helicobacter pylori; pp. 443-445
(Nishimura and Nagata, Japan)
Chapter 6.2- Disruption of alanine racemase gene of Schizosaccharomyces pombe; pp. 447-451
(Kazuoka et al., Japan)
Chapter 6.3- Assay method for aspartate racemase activity by HPLC; pp. 453-458
(Nimura and Homma, Japan)
Chapter 6.4- Serine racemase of sillworm, Bombyx mori; pp. 459-462 (Yoshimura, Japan)
Chapter 6.5- Recombinant serine racemase preparation; pp. 463-466 (Foltyn and Wolosker, Israel)
Chapter 6.6- D-Amino acid oxidase activity assays; pp. 467-476 (Vanoni and Curti, Italy)
Chapter 6.7- Histochemical detection of D-amino-acid oxidase activity in rat brain; pp. 477-480
(Tanaka et al., Japan)
Chapter 6.8- Evaluation of chiral inversion of D-amino acid by stable isotope methodology; pp. 481-490
(Hasegawa et al., Japan)
Chapter 6.9- Techniques for the engineering of D-amino acid oxidase substrate specificity; pp. 491-501
(Molla et al., Italy)
Chapter 6.10- Transformation of plants with D-amino resistance selectable markers; pp. 503-508
(Forsum and Näsholm, Sweden)
Chapter 6.11- Screening for mutant mice lacking D-amino-acid oxidase activity; pp. 509-512
(Konno, Japan)
Chapter 6.12- Astroglial expression of D-amino acid oxidase: regional and cell-type specific expression; pp. 513-521
(Park et al., Japan)
Chapter 6.13- D-Amino acid oxidase: a versatile tool to study the function of the glial-derived neuromodulator D-serine at glutamatergic synapses; pp. 523-533
(Mothet, France)
Chapter 6.14- Resonance Raman study on charge-transfer complexed of porcine D-amino acid oxidase; pp. 535-543
(Nishina and Shiga, Japan)
Chapter 6.15- Immunodetection of D-aspartate oxidase; pp. 545-548 (Tedeschi et al., Italy)
Chapter 6.16- High-performance liquid chromatographic determination of D-aspartate oxidase activity in rat tissues; pp. 549-553
(Yamamoto et al., Japan)
Chapter 6.17- Cloning of the human brain D-aspartate oxidase cDNA and its expression in Escherichia coli; pp. 555-560
(Setoyama and Miura, Japan)
Chapter 6.18- Methods for N-acyl- D-amino acid amidohydrolase research; pp. 561-571
(Wakayama et al., Japan)
Chapter 6.19- Activity measurement of hydantoin racemase enzyme: a key for the production of optically pure D-amino acids; pp. 573-577 (Martinez-Rodriguez et al., Spain)
Chapter 6.20- Enzymes acting on D-amino acid amides; pp. 579-589 (Asano, Japan)
Chapter 6.21- Role of ammonium phosphates in tryptophanase activity toward D-tryptophan; pp. 591-607
(Shimada, Japan)
Index |
