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از ساعت 7 صبح تا 10 شب
ویرایش: 1st
نویسندگان: T. Fukui (Eds.)
سری:
ISBN (شابک) : 9780080408200
ناشر: Pergamon Pr
سال نشر: 1991
تعداد صفحات: 557
زبان:
فرمت فایل : PDF (درصورت درخواست کاربر به PDF، EPUB یا AZW3 تبدیل می شود)
حجم فایل: 21 مگابایت
در صورت تبدیل فایل کتاب Enzymes Dependent on Pyridoxal Phosphate and Other Carbonyl Compounds As Cofactors. Proceedings of the 8th International Symposium on Vitamin B6 and Carbonyl Catalysis, Held in Osaka, Japan, October 15 –19, 1990 به فرمت های PDF، EPUB، AZW3، MOBI و یا DJVU می توانید به پشتیبان اطلاع دهید تا فایل مورد نظر را تبدیل نمایند.
توجه داشته باشید کتاب آنزیم های وابسته به پیریدوکسال فسفات و سایر ترکیبات کربونیل به عنوان کوفاکتور. مجموعه مقالات هشتمین سمپوزیوم بین المللی در مورد ویتامین B6 و کاتالیز کربونیل، برگزار شده در اوزاکا، ژاپن، 15 تا 19 اکتبر 1990 نسخه زبان اصلی می باشد و کتاب ترجمه شده به فارسی نمی باشد. وبسایت اینترنشنال لایبرری ارائه دهنده کتاب های زبان اصلی می باشد و هیچ گونه کتاب ترجمه شده یا نوشته شده به فارسی را ارائه نمی دهد.
Content:
Pergamon titles of related interest, Page ii
Front Matter, Page iii
Copyright, Page iv
Preface, Page v
Introduction, Page vii, ESMOND E. SNELL
Biochemical Significance of Carbonyl Catalysis, Pages 1-9, HIROSHI WADE, HIDEYUKI HAYASHI
Pyridoxal-P, The Pyruvoyl Group, and Amino Acid Decarboxylases, Pages 11-20, ESMOND E. SNELL
On the Biochemistry of Glutamine and Glutathione, Pages 21-28, ALTON MEISTER
PLP-Dependent and Independent Amino Acid Racemases, Pages 29-34, KENJI SODA
Evolutionary Relationships among Pyridoxal Phosphate-Dependent Enzymes, Pages 35-42, P.K. MEHTA, T.I. HALE, P. CHRISTEN
Aspartate Aminotransferase from Sulfolobus Solfataricus: A Hyperthermophilic Enzyme, Pages 43-53, G. MARINO, M.I. ARNONE, L. BIROLO, M.V. CUBELLIS, F. ZAPPACOSTA, G. SANNIA, G. NITTI, P. PUKCCI
Molecular Cloning and Sequence Determination of Thermostable Aspartate Aminotransferase from Thermophilic Bacillus Species, Pages 55-57, M.-H. SUNG, K. TANIZAWA, H. TANAKA, K. SODA, S. KURAMITSU, H. KAGAMIYAMA
The Complete Amino Acid Sequence of Rat Liver Cytosolic Alanine Aminotransferase, Pages 59-61, TAKEO MATSUZAWA, MARIKO YAGAMI, MASAMI SUZUKI, KOJI TAKIO, KOITI TITANI
Isolation and Characterization of cDNA Coding for 4-Aminobutyrate Aminotransferase, Pages 63-65, YOUNG TAE KIM, JOO HONG PARK, OH SHIN KWON, SOO YOUNG CHOI, JORGE E. CHURCHIGH
Comparison of the Amino Acid Sequence of Rat Liver Serine Dehydratase with the Sequences of other Hydroxyamino Acid Dehydratases and Existence of Two Isoforms of mRNA Coded by the Serine Dehydratase Gene, Pages 67-69, HIROFUMI OCAWA, MOTOJI FUJIOKA, HENRY C. PITOT
Primary Structure of Glutamate Decarboxylase from E. coli, Pages 71-73, BRUNO MARAS, EVA DE LUCA, DONATELLA BARRA, FRANCESCO BOSSA, ROBERT A. JOHN
Molecular Cloning and Sequencing of cDNAs of Rat and Guinea-Pig Dopa Decarboxylases, Pages 75-77, TASTUYA TANAKA, MASAO KURODA, HORIO YOSHIYKI, TAKETOSHI MASATO, IMAMURA IKUO, FUKUI HIROYUKI, WADA HIROSHI
Isolation and Characterization of a cDNA Clone Encoding Human Aromatic L-Amino Acid Decarboxylase, Pages 79-81, HIROSHI ICHINOSE, CHIHO SIIMI, TOSHIHARU NAGATSU, YOSHIKAZU KUROSAWA, KOITI TITANI, KEISUKE FUJITA
Identification of Critical Regions on the Primary Structure of Pig Kidney Dopa Decarboxylase, Pages 83-85, PAOLA DOMINICI, CARLA BORRI VOLTATTORNI, BRUNO MARAS, DONATELLA BARRA, FRANCESCO BOSSA
Partial Purification and cDNA Cloning of Human Histidine Decarboxylase, Pages 87-89, R. SATO, Y. TANNO, K. YAMAUCHI, Y. OHKAWARA, S. SHIBAHARA, K. MAEYAMA, T. WATANABE, T. TAKISHIMA
L-Histidine Decarboxylase from Mouse Mastocytoma P-815 Cells: The Amino Acid Sequence as Derived from cDNA Sequence, Pages 91-93, J. YAMAMOTO, K. YATSUNAMI, E. OHMORI, T. FUKUI, A. ICHIKAWA
Pseudomonas Cepacia 2, 2-Dialkylglycine Decarboxylase. High-Level Expression in Escherichia coli and Sequence Alignment with Ornithine Aminotransferases, Pages 95-97, J.W. KELLER, R.A. REYNOLDS, M.K. WISE, R.A. PAREKH
The Structural Differences Between Chicken Cytosolic and Mitochondrial Aspartate Aminotransferases, Pages 99-105, V.N. MALASHKEVICH, Yu.M. TORCHINSKY, B.V. STROKOPYTOV, V.V. BORISOV, J.-C. GENOVESIO-TAVERNE, J.N. JANSONIUS
Three-dimensional Structure of Aspartate Aminotransferase from Escherichia coli, Pages 107-109, AKIHIRO OKAMOTO, KEN HIROTSU, TAIICHI HIGUCHI, SEIKI KURAMITSU, HIROYUKI KAGAMIYAMA
The Three-Dimensional Structure of Phosphoserine Aminotransferase from Escherichia coli, Pages 111-115, W. STARK, J. KALLEN, Z. MARKOVIC-HOUSLEY, B. FOL, M. KANIA, J.N. JANSONIUS
X-ray Crystallographic Studies on E. coli Aspartate Aminotransferase Wild Type and Mutants, Pages 117-119, J. JÄGER, M. MOSER, R.A. PAUPTIT, U. SAUDER, B. FOL, Z. HOUSLEY-MARKOVIC, J.N. JANSONIUS, E. KÖHLER, K. KIRSCHNER, M. ZIAK, PH. CHRISTEN
Crystal Structure of ω-Amino Acid:Pyruvate Aminotransferase, Pages 121-124, NOBUSHISA WATANABE, NORIYOSHI SAKABE, KAZUO YONAHA, KIWAKO SAKABE, SHIGEO AIBARA, YUHEI MORITA
X-ray Structure Investigation of some Pyridoxal-Containing Enzymes, Pages 125-127, E. HARUTYUNYAN, A. ANTSON, G. OBMOLOVA, A. TEPLYAKOV, G. CHENCHIK, T. DEMIDKINA, A. GABIBOV, K. SCHNACKERZ, G. WAHLER, K. WILSON, Z. DAUTER
Fluorine-19, Phosphorus-31, and Proton NMR Spectroscopy of Aspartate Aminotransferase Containing 6-Fluoropyridoxal Phosphate or 6-Fluoropyridoxamine Phosphate, Pages 129-143, R.D. SCOTT, P. JIN, R. MIURA, W.C. CHU, A. KINTANAR, C.M. METZLER, D.E. METZLER
15N NMR Studies on Aspartate Aminotransferase Reconstituted with [15N]PLP, Pages 145-147, H. KONDO, Y. OHAMA, H. TANAMACHI, S. TANASE, Y. MORINO
Phosphorus-31 Nuclear Magnetic Resonance Studies on Apoaspartate Aminotransferase with Inorganic Phosphate and Thiophosphate, Pages 149-152, K.D. SCHNACKERZ, G. WALDMANN
Cryo-Trapping of True Enzyme-Substrate Intermediates of Aspartate Aminotransferase, Pages 153-159, M. STERK, H. GEHRING
Genetic Engineering and Chemical Modification at the Position of Lysine 258 in Aspartate Aminotransferase, Pages 161-167, J.F. KIRSCH, A. PLANAS, M.D. TONEY
Analysis of the Conformational Change Accompanying Reactions of the E. coli L-Aspartate Amino Transferase, Pages 169-173, A.T. DANISHEFSKY, D. RINGE
Substitution of S-(β-aminoethyl)-cysteine for Active-site Lysine of Thermostable Aspartate Aminotransferase, Pages 175-177, TOHRU YOSHIMURA, YUTAKA MATSUSHIMA, NOBUYOSHI ESAKI, KENJI SODA, KATSUYUKI TANIZAWA, SUNG MOON-HEE
Asp222, His143, and Tyr70 in Escherichia coli Aspartate Aminotransferase, Pages 179-181, S. KURAMITSU, T. YANO, K. INOUE, H. KAGAMIYAMA, K. HIROMI, S. TANASE, Y. MORINO
Escherichia coli Aspartate Aminotransferase: Effects of Site-Specific Mutations on Substrate Binding and Catalysis, Pages 183-186, H. HAYASHI, Y. INOUE, S. KURAMITSU, H. KAGAMIYAMA
Functional Role of the Mobile Amino-Terminal Segment of Porcine Cytosolic Aspartate Aminotransferase, Pages 187-189, S. TANASE, Y. FUKUMOTO, Q-W. PAN, F. NAGASHIMA, Y. MORINO
Insight into “Induced Fit” Mechanism of Porcine Cytosolic Aspartate Aminotransferase through the Behavior of the Residue at Position 18, Pages 191-193, T. HIGAKI, S. TANASE, Y. FUKUMOTO, Y. MORINO, K. NISHIMURA, H. OKAMKURA
Probing a Functional Role of GLU141 in Porcine Cytosolic Aspartate Aminotransferase, Pages 195-197, K. SUGINOHARA, N. HAMASAKI, S. TANASE, Y. FUKUMOTO, Y. MORINO
Individual Components of the Beta Subform of Cytosolic Aspartate Aminotransferase, Pages 199-201, C.M. METZLER, D.E. METZLER, SUSANNA MEKLIN, PAUL ROGERS, ARTHUR ARNONE
Microspectrophotometry on Crystals of Cytosolic Aspartate Aminotransferase, Pages 203-205, M.N. JANAKIRAMAN, D.E. METZLER
Aspartate Aminotransferase in Crystals and in Solution: The Functional and Structural Non-Equivalence of its Subunits, Pages 207-209, V.M. KOCHKINA
The Functioning of Sulfolobus Solfataricus Aspartate Aminotransferase, Pages 211-214, LEILA BIROLO, M. IMMACOLATA ARNIONE, M. VITTORIA CUBELLIS, GENNARO MARINO, GIOVANNI SANNIA
Thermostable d-Amino Acid Aminotransferase: Substitution of Arginyl and Alanyl Residues for Lysine 145, Pages 215-216, KATSUSHI NISHIMURA, TOHRU YOSHIMURA, NOBUYOSHI ESAKI, KENJI SODA, KATSUYUKI TANIZAWA, JAMES M. MANNING
The Mechanisms of Inactivation of Ornithine- and Gaba-Transaminases by Gaba Analogs, Pages 217-219, D. DE BIASE, J.B. BOLTON, R.A. JOHN, F. BOSSA, D. BARRA
Purification and Characterization of Aspartate Aminotransferase Isozymes from Nad-Malic Enzyme-Type C4 Plants, Pages 221-223, M. TANIGUCHI, T. SUGIYAMA
Aspartate Aminotransferase of Methanobacterium Thermoformicicum SF-4 and FTF, Pages 225-227, T. TANAKA, S. YAMAMOTO, A. TACHIBANA, M. TANIGUCHI, S. OI
Characteristics of Alanine Aminotransferase from Candida Maltosa, Pages 229-231, ISAO UMEMURA, KOJI YANAGIYA, SABURO KOMATSUBARA, TADASHI SATO, TETSUYA TOSA
Birds are Classified into Two Groups on the Basis of Intraperoxisomal Form of Hepatic Alanine:Gloyoxylate Aminotransferase, Pages 233-235, H. SAKURABA, S. FUJIWARA, T. NOGUCHI
Dimethylarginine Aminotransferase in Rats, Pages 237-239, T. OGAWA, M. KIMOTO, K. SASAOKA
Purification and Properties of Ornithine and N-Acetylornithine Aminotransferases from Gramicidin S-Producing Bacillus Brevis, Pages 241-243, MASAYUKI KANDA, KAZUKO HORI, TOSHITSUGU KUROTSU, YOSHITAKA SAITO
Partial Purification and some Properties of L- and D-Tryptophan Aminotransferases from Maize Coleoptiles, Pages 245-247, T. KOSHIBA, N. MITO
Exploring the Tryptophan Synthase α2β2 Multienzyme Complex by X-Ray Crystallography and Site-Directed Mutagensis, Pages 249-256, EDITH WILSON MILES, S. ASHRAF AHMED, ARVIND M. KAYASTHA
Allosteric Interactions Coordinate Covalent Steps in Catalysis and Modulate Indole Transfer Between the α- and β-Sites of the Tryptophan Synthase Bienzyme Complex, Pages 257-264, MICHAEL F. DUNN, PETER BRZOVIC\', CATHERINE LEJA, KARL HOUBEN, MELINDA ROY, ALEN AGUILAR, WILLIAM F. DREWE JR
Role of Glutamic Acid 109 in the Active Site of the β Subunit of Tryptophan Synthase from Salmonella Typhimurium in Controlling the Reaction Specificity and Substrate Specificity of the α2β2 Complex, Pages 265-267, ARVIND M. KAYASTHA, EDITH WILSON MILES
Indole Propanol Phosphate as a Conformational Probe in Various Forms of E. Coli Tryptophan Synthase A Phosphorus-31 NMR Study, Pages 269-271, P. BARTHOLMES, G. LENTZEN, B. RECKMANN, T. SCHWARZ, K.D. SCHNACKERZ
Allosteric Regulation of Trytophan Synthase: A pKa Change at β-Active Site Induced by α-Subunit, Pages 273-275, ANDREA MOZZARELLI, ALESSIO PERACCHI, STEFANO BETTATI, GIAN LUIGI ROSSI
Interactions Between Heterologous Subunits Coordinates Catalytic Activity in the Tryptophan Suynthase Bienzyme Complex, Pages 277-279, PETER BRZOVLC\', EDITH W. MILES, MICHAEL F. DUNN
Reorientations of the Coenzyme in the Active Site of Tryptophanase, Pages 281-285, YU. M. TORCHINSKY, L.N. ZAKOMIRDINA, I.S. SAKHAROVA
Structure and Function of Tryptophanase from Escherichia Coli, Pages 287-289, YASUSHI KAWATA, SHUNSUKE TANI, TOMOHIRO MIZOBATA, NOBORU YUMOTO, MASANOBU TOKUSHIGE
Role of Tryptophan 248 in the Active Site of Tryptophanase from Escherichia Coli, Pages 291-292, YASUSHI KAWATA, NOBUHARU TSUJIMOTO, SHUNSUKE TANI, TOMOHIRO MIZOBATA, MASANOBU TOKUSHIGE
Equilibria and Absorption Spectra of Tryptophanase, Pages 293-295, C.M. METZLER, R. VISWANATH, D.E. METZLER
α-Proton Exchange in Amino Acids Catalyzed by Tryptophanase, Pages 297-299, N.G. FALEEV, S.B. RUVINOV, V.M. BELIKOV, L.N. ZAKOMYRDINA, I.S. SAKHAROVA, YU. M. TORCHINSKY
Crystallization of Tyrosine Phenol-Lyase from Citrobacter Intermidius. Electron Microscopy of Tubes, Pages 301-303, ALFRED A. ANTSON, OLGA N. ZOGRAF, ELENA V. ORLOVA, EMIL H. HARUTYUNYAN, MICHAEL B. SHERMAN, TATYANA V. DEMIDKINA
Contribution of a Glycine-Rich Loop to PLP Active Sites, Pages 305-311, M. MARCEAU, J.A. SHAFER
Modification of the AMP-Binding Site of Biodegradative Threonine Deaminase from Escherichia Coli W, Pages 313-315, KENJI HIROSE, YASUSHI KAWATA, NOBORU YUMOTO, MASANOBU TOKUSHIGE, MITSUO TAGAYA, TOSHIO FUKUI
D-Glucosaminate Aldolase Activity of D-Glucosaminate Dehydratase from Pseudomonas Fluorescens, Pages 317-319, R. IWAMOTO, H. TAMIKI, S. NAKURA
Mechanism of the Beta-Replacement Enzyme, O-Acetylserine Sulfhydrylase, Pages 321-323, P.F. COOK, S. NALABOLU, C.-H TAI
PLP-Dependent Enzymes of Sulfur Amino Acid Metabolism. Catalytic Activity of Fusion Proteins. Physico-Chemical Investigations, Pages 325-327, A.G. GABIBOV, A.M. SHUSTER, O.A. KVASHUK, A.R. KHOMUTOV, G.I. CHENCHIK, E.A. TOLOSA, E.V. GORYACHENKOVA
Characterization of 1-Aminocyclopropane-1-carboxylate (ACC) Synthase, A Key Enzyme in Ethylene Biosynthesis: Active Site Peptide Sequencing, Pages 329-336, S.F. YANG, W-K. YIP, J-G. DONG, S. SATOH
The Origin of Substrate and Reaction Specificity in Serine Hydroxymethyltransferase, Pages 337-339, V. SCHIRCH, S. ANGELACCIO, S. PASCARELLA, E. FATTORI, F. BOSSA, W. STRONG, K. SHOSTAK, M. ZAMORA
Role of the Serine Hydroxymethyltransferase Glycine Quinonoid Complex in Controlling One Carbon Metabolism in Eukaryotic and Prokaryotic Cells, Pages 341-343, PATRICK STOVER, VERNE SCHIRCH
Stereochemical Fidelity of the Aminomalonic Acid Decarboxylase Activity of Serine Hydroxymethyltransferase, Pages 345-347, NEIL R. THOMAS, DAVID GANI
Reaction-Dependent Structural Change of 1-Aminocyclopropane-1-Carboxylate Deaminase from Pseudomonas Species, Pages 349-351, M. HONMA, Y. SATOH, M. YAMADA
Thermostable Alanine Racemase of Bacillus Stearothermophilus: Interdependent Folding of Two Domains into an Active Complex, Pages 353-355, H. TOYAMA, T. YOSHIMURA, N. ESAKI, K. SODA, K. TANIZAWA
A Novel Mechanistic Role for Pyridoxal-5′-Phosphate, Pages 357-363, P.A. FREY, R.M. PETROVICH, K.B. SONG, O. HAN
Oxidative Deamination of Amino Acids by Molecular Oxygen with Pyridoxal Phosphate and Cu(II) Ion as Catalysts, Pages 365-369, V.M. SHANBHAG, ARTHUR E. MARTELL
Intermediate Species Absorbing in the 500-nm Region in Nonenzymatic Pyridoxal Catalysis, Pages 371-372, YOSHIKAZU MATSUSHIMA, MISA KOJIMA, YOSHIKO NAGATA
Peculiarities of Spectroscopicsl Behavior of PLP Aldimines with Amino Acids, Pages 373-375, YU.V. MOROZOV, N.P. BAZHULINA, V.A. BOKOVOY, L.I. FIODOROVA, V.O. CHEKHOV
Mechanism and Error Rate in Phosphorylase Catalysis, Pages 377-384, DIETER PALM, STEFAN BECKER, REINHARD SCHINZEL
Design and Variation of Allosteric Regulation in Glycogen Phosphorylase, Pages 385-392, PETER K. HWANG, MICHELLE BROWNER, VIRGINIA L. RATH, STUART TUGENDREICH, PETER RASOR, ROBERT J. FLETTERICK
The Three-Dimensional Structure of Potato Phosphorylase at 2.6 Å Resolution, Pages 393-396, JOHANNES WILLNECKER, KARIN JAHNKE, MANFRED BUEHNER
X-Ray and Solution Studies on Glycogen Phosphorylase Reconstituted with Pyridoxal in Place of the Natural Coenzyme, Pages 397-400, N.G. OIKONOMAKOS, A.C. PAPAGEORGIOU, K.R. ACHARYA, D.D. LEONIDAS, L.N. JOHNSON, A.E. EVANGELOPOULOS
Structural Relationships in Higher Plant α-Glucan Phosphorylase Isozymes Differently Localized within Cells, Pages 401-403, H. MORI, K. NAKANO, K. TANIZAWA, T. FUKUI
Characterization of Potato Phosphorylase Modified Essential Lys Residue by O-Phthalaldehyde, Pages 405-407, MIKIHIKO KOBAYASHI, HIROBUMI AOKI, EIJI ICHISHIMA
Contribution of Individual Active Site Amino Acid Residues to Maltodextrin Phosphorylase Catalysis, Pages 409-411, R. SCHINZEL, D. PALM
Statistical Analysis of Steady-State Kinetics of Glycogen Phosphorylase b Reaction, Pages 413-415, B.I. KURGANOV, S.V. KLINOV
Synthesis of Pyridoxal-5’ Phosphate Analogs and their Interaction with Apoenzyme of Glycogen Phosphorylase b, Pages 417-419, V.I. GUNAR, N.P. SUGROBOVA, S.V. STEPANOVA, N.A. CHEBOTARIVA, A.A. POZNAKSKAJA, B.I. KURGANOV
Interaction of Phosphorylase and Phosphorylase Kinase with Calmodulin and Troponin C, Pages 421-423, NATALIJA B. LIVANOVA, IRAIDA E. ANDREEVA, VALENTINA F. MAKEEVA, ALEXANDER D. VERIN, OKSANA E. FALENDYSH, NIKOLAI B. GUSEV
Structures of Histidine and Ornithine Decarboxylases from Lactobacillus 30a, Pages 425-427, M.L. HACKERT, S.R. ERNST, D.T. GALLAGHER, C. MOMANY, P. KOLATKAR, C-K.C. WONG
Mechanism of Formation of the Pyruvate Prosthetic Group of Phosphatidylserine Decarboxylase of Escherichia Coli, Pages 429-436, W. DOWHAM, Q.-X. LI
Serine Hydroxymethyltransferase from Mung Bean Seedlings (Vigna Radiata): A New Pyruvoyl Enzyme, Pages 437-444, N. SUKANYA, H.S. SAVITHRI, A.N. RADHAKRISHNAN, N. APPAJI RAO
Enzyme-Activated Irreversible Inhibitors of S-Adenosylmethionine Decarboxylase, A Pyruvoyl Enzyme, Pages 445-447, C. DANZIN, P. MARCHAL, P. CASARA
PLP and/or PQQ?, Pages 449-456, J.A. DUINE
Chemical Behavior of Coenzyme PQQ Toward Amino Acids, Pages 457-464, YOSHIKI OHSHIRO, SHINOBU ITOH
Biochemical and Physiological Functions of Pyrroloquinoline Quinone, Pages 465-473, MINORU AMEYAMA, OSAO ADACHI
Studies on the Properties and Role of the Organic Cofactor in Lysyl Oxidase, Pages 475-482, H.M. KAGAN, M.A. SHAH, A. BOAK, P.M. GALLOP, P.C. TRACKMAN
Evidence that Glutamate Decarboxylase and Ornithine Aminotransferase are not Quinoproteins, Pages 483-485, R.A. JOHN, D. DE BIASE, B. MARAS
Expression of Recombinant Rat Liver Dopa Decarboxylase and Absence of Pyrroloquinoline Quinone in the Holo-Enzyme, Pages 487-489, TAKAGISHI TADASHI, IMAMURA IKUO, MIZUGUCHI HIROYUKI, FUKUI HIROYUKI, WADA HIROSHI, MASAO KURODA, TATSUYA TANAKA
A Cofactor of Nitroalkane Oxidase, Pages 491-493, KUMIO YOKOIGAWA, JEONG WEON HUH, TAKEO MORIYA, NOBUYOSHI ESAKI, KENJI SODA, KATSUYUKI TANIZAWA
Study on Active Site, PQQ, of Fungal Amine Oxidase, Pages 495-497, H. KAMAGAI, Y. SHIMADA, H. TSUCHIYAMA, T. TOCHIKURA, H. YAMADA, C-S. KIM, T. UENO, O. ADACHI, M. AMEYAMA
A Copper Containing Domain in Amine Oxidase, Pages 499-501, A. GIARTOSIO, E. AGOSTINELLI, S. D\'ALESSIO, A.M. ALBERTINI, B. MONDOVI\'
Trials to Detect Pyrroloquinoline Quinone (PQQ) in Bovine Plasma Amine Oxidase and Tissues of the Rat and Human by Gas Chromatography/Mass Spectrometry, Pages 503-505, T. KUMAZAWA, O. SUZUKI, H. SENO, T. URAKAMI, T. MATSUMOTO
Fluorescence Spectroscopy of Free and Bound PQQ, Pages 507-509, L.S. KHEMLANI, J.E. CHURCHICH
PQQ as a Generator and a Scavenger of Oxygen Radicals : Determination with ESR Spectroscopy using a Spin Trap Agent, Pages 511-513, T. AKAIKE, K. SATO, H. MAEDA, M. KOHNO
Preventive Effects of PQQ on Glucocorticoid-Induced Cataract Formation and Hepatic Pigmentation in Developing Chick Embryo, Pages 515-517, HIDEO NISHIGORI, OSAMU ISHIDA, IZUMI O. UMEDA
Precursor of Mitochondrial Aspartate Transaminase: Properties and Interactions with Membranes, Pages 519-526, M. MARTINEZ-CARRION, A. IRIARTE, J. MATTINGLY, T. WU
Lipid Dependency of the Binding of a Mitochondrial Precursor Protein to Model Membranes, Pages 527-529, A. IRIARTE, F. ALTIERI, J. DEL SOLAR, J.R. MATTINGLY Jr., M. MARTINEZ-CARRION
Hormonal Regulation of Cytosolic Aspartate Aminotransferase, Pages 531-536, J. HANOUNE, M. AGGERBECK, M. GARLATTI, S. FEILLEUX, M. DAHESHIA, R. BAROUKI
Characterization and Expression of the Serine Dehydratase Gene: Regulation by Glucocorticoids and Cyclic Amp, Pages 537-539, C. NODA, K. MATSUDA, A. ICHIHARA
Synthesis and Organelle Localization of Serine: Pyruvate Aminotransferase in Rat and Human Liver, Pages 541-543, A. ICHIYAMA, T. ODA, T. FUNAI, K. NISHIYAMA
Vitamin B6 and Nervous System Function, Pages 545-553, KRISHNAMURTI DAKSHINAMURTI, S.K. SHARMA, K.J. LAL
Immno-Cross-Reactivity of Histidine and Dopa Decarboxylases, Pages 555-557, HIROYUKI MIZUGUCHI, MASAMI YABUMOTO, IKUO IMAMURA, HIROYUKI FUKUI, HIROSHI WADA
Ornithine Decarboxylase and Neoplastic Growth, Pages 559-561, T.T. BEREZOV
Ornithine Decarboxylase Activity in Psoriatic Epidermis as Biochemical Feature of Hyperproliferative Process, Pages 563-565, A.T. KAGRAMANOVA, L.D. TISHENKO, T.T. BEREZOV, A.A. MANDEL
Chemical Regulation of Polyamine Biosynthesis in Cell Cultures by Polyfunctional O-Substituted Hydroxylamines, Pages 567-569, A.R. KHOMUTOV, R.M. KHOMUTOV, T.O. ELORANTA, L. PERSSON, C.W. PORTER, V.G. DZAVAKHIA
Glycine Induced Lysis and Accumulation of UDP-N-Acetylmuramyl-Peptide Peptoglycan Precursors in B. Subtilis with Reduced Alanine Racemase Activity, Pages 571-573, M.P. HEATON, T.L. THOMPSON, R.B. JOHNSTON
The Conversion of (R)-β-Aminoisobutyrate to the (S)-Enantiomer In Vitro, Pages 575-577, N. TAMAKI, M. KANEKO
Aromatic Amino Acid Aminotransferase of Escherichia Coli: Cloning and Expression of the tyrB Gene, Pages 579-581, CHICHI C. LIU, LI-PING TU, JIN-TANN CHEN, HSIN TSAI
Inactivation of Cytosolic Aspartate Aminotransferase: Effects of the Substrates and Some Low-Molecular Compounds, Pages 583-585, M. OKADA, H. HARIMA
Molecular Characterization of Apo-Ornithine Aminotransferase Subforms, Pages 587-588, MASATOSHI NISHII, TAKEO MATSUZAWA
Kynurenine Aminotransferase Activity at Low Concentration of Kynurenine and Immunohistochemical Localization of the Enzyme in Rat Brain, Pages 589-591, M. NAKAMURA, E. OKUNO, R. KIDO
On V.B.6 Effect to Diabetes Mellitus and Other Diseases, Pages 593-595, Y. SHIBATA, T. OHTA, M. NAKATSUKA, F. TAKEUCHI, M. HANEDA, T. TANAKA, T. TOKURA, T. TAMAI, S. OHTAWARA, K. SATO, Y. HACHINO
Vitamin B6 as an Inhibitor of Eukaryotic DNA Topoisomerase I, Pages 597-599, P. ARSENE DER GARABEDIAN, JACQUELINE J. VERMEERSCH
Inhibition of Aminotransferases in Human Serum by Amino-Guanidine: Role of Pyridoxine/Pyridoxal Phosphate in Diabetes, Pages 601-603, MAHIN KHATAMI, JEFFREY C. HONG, GEORGE A. HERMANN, ANTONY TURSI
Vitamin B6 Requirement for Yeast Cell Aggregation Caused by Inositol Deficiency and its Mechanism, Pages 605-607, T. KAMIHARA, T. FUJIMURA, H. NISHIHARA, K. NISHIMURA
Characteristics of a Transporter for Uptake of Vitamin B6 into Mammalian Cells: Isolation of B6 -Binding Proteins from Brush-Border Membranes of Rat Renal Proximal Tubular Epithelial Cells, Pages 609-611, D.B. McCORMICK, D.M. BOWERS-KOMRO, J.L. BONKOSVKSY, C. LARSEN, Z. ZHANG
CHARACTERIZATION OF THE PROTEOLYSIS ACTIVATED PYDIDOXINE 5 PHOSPHATE OXIDASE AND PURIFIED PYRIDOXAL DEHYROGENASE Characterization of the Proteolysis Activated Pydidoxine 5 Phosphate Oxidase and Purified Pyridoxal Dehyrogenase, Pages 613-615, FRANCIS KWOK, JORGE E. CHURCHICH
Pyridoxal Kinase: Inhibitors Bound to the Pyridoxal Binding Site, Pages 617-619, GLEN SCHOLZ, FRANCIS KWOK, JORGE E. CHURCHICH
Effect of Extracellularly Added Vitamin B-6 Compounds and Antagonists on Intracellular Pyridoxal 5’-Phosphate Form of Aspartate Aminotransferase in Rabbit Erythrocytes, Pages 621-623, T. YAGI, S. YAMAMOTO, K. MATSUOKA
Highly Sensitive and Simple Determination of Vitamin B-6 Derivatives Using a Reversed-Phase HPLC, Pages 625-627, H. TSUGE, N. HIROSE, T. TOUKAIRIN-ODA, T. HAYAKAWA
Probing the Active Site in Glycogen Synthase by Affinity Labeling with Nucleotidyl Derivatives of Pyridoxal Phosphate, Pages 629-631, TOSHIO FUKUI, MITSUO TAGAYA, KOJI FURUKAWA
Reaction of Pyridoxamine with Carboxylic Residues of Protein, Pages 633-635, OH-SHIN KWON, JORGE E. CHURCHICH
Structure Reaction and Molecular Evolution of Biotin Carboxylase, Pages 637-639, T. TANABE, A. MIYATA, C. YOKOYAMA, H. IHARA, T. TAKAI, H. TOH, M. ANAI, H. KONDO
Conversion of Nitriles into Useful Amides by Nitrile Hydratase, Ferric-Carbonyl Enzyme, Pages 641-648, T. NAGASAWA, H. YAMADA
Pyridoxal Phosphate Containing β-Lyases in the Synthesis of Labelled Biochemicals, Pages 649-656, P. HERMANN, I. WILLHARDT