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[136] Assay of catalases and peroxidases
edited_book
Author(s):
Britton Chance
,
A.C. Maehly
Publication date
(Print):
1955
Publisher:
Elsevier
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Author and book information
Book Chapter
Publication date (Print):
1955
Pages
: 764-775
DOI:
10.1016/S0076-6879(55)02300-8
SO-VID:
34e1862c-e2ab-4e4f-9a3e-5f4f8d116732
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Book chapters
pp. iii
Editorial Board
pp. ix
Volume II Preparation and assay of enzymes
pp. v
Contributors to volume II
pp. xviii
Volume I preparation and assay of enzymes
pp. xx
Errata for Volume I
pp. 3
[1] Swine pepsin and pepsinogen
pp. 8
[2] Chymotrypsinogens and chymotrypsins
pp. 26
[3] Trypsinogen and trypsin
pp. 36
[4] Naturally occurring trypsin inhibitors
pp. 54
[5] Plant proteolytic enzymes
pp. 64
[6] Cathepsin C from beef spleen
pp. 69
[7] Purification and assay of rennin
pp. 77
[8] Carboxypeptidase and procarboxypeptidase
pp. 83
[9] Aminopeptidases
pp. 93
[10] Dipeptidases
pp. 109
[11] Dehydropeptidases from kidney
pp. 115
[12] Aminoacylase
pp. 120
[13] Penicillinase
pp. 124
[14] Renin from kidney
pp. 135
[15] Renin substrate (hypertensinogen) from hog serum
pp. 139
[16] Enzymes in blood clotting
pp. 167
[17] Enzymatic degradation of cytochrome C
pp. 170
[18] Transaminases in bacteria
pp. 178
[19] Estimation of animal transaminases
pp. 185
[20] Amino acid decarboxylases of bacteria
pp. 190
[21] Amino acid decarboxylases of plants
pp. 195
[22] Amino acid decarboxylases of animals
pp. 199
[23] d-Amino acid oxidase from kidney
pp. 204
[24] l-Amino acid oxidases (mammalian tissues and snake venom)
pp. 212
[25] Amino acid racemases
pp. 217
[26] Amino acid reductases
pp. 220
[27] l-Glutamic dehydrogenase from liver
pp. 225
[28] Glycine oxidase
pp. 228
[29] Histidase and urocanase
pp. 233
[30] Tryptophan synthetase from neurospora
pp. 238
[31] Tryptophan cleavage
pp. 242
[32] Tryptophan oxidation
pp. 254
[33] Methionine-activating enzyme, liver
pp. 257
[34] Methyl acceptor systems
pp. 263
[35] γ-Glutamyltransferase (plants)
pp. 267
[36] Glutamotransferase (γ-glutamyltransferase)
pp. 273
[37] Cleavage of aromatic rings with eventual formation of β-ketoadipic acid
pp. 287
[38] Enzymes involved in conversion of tyrosine to acetoacetate
pp. 300
[39] Enzymes of aromatic biosynthesis
pp. 311
[40] Cystathionine cleavage enzymes
pp. 315
[41] Desulfhydrases and dehydrases
pp. 324
[42] Sulfatases and desulfinases
pp. 334
[43] Rhodanese
pp. 337
[44] Glutamine synthesis
pp. 342
[45] Enzymatic synthesis of glutathione
pp. 346
[46] Hippuric acid synthesis
pp. 350
[47] Enzymatic citrulline synthesis
pp. 356
[48] Enzymatic synthesis of arginine (condensing and splitting enzymes)
pp. 368
[49] Arginase
pp. 374
[50] Arginine dihydrolase
pp. 378
[51] Urease
pp. 380
[52] Glutaminase, asparaginase, and α-keto acid-ω-amidase
pp. 386
[53] Aspartase
pp. 390
[54] Amine oxidases
pp. 397
[55] Amino acid amidase from hog kidney
pp. 400
[56] Nitroethane oxidase
pp. 403
[57] Organic nitrate reductase
pp. 406
[58] Nitroaryl reductase from Neutrospora crassa
pp. 411
[59] Nitrate reductase from Neurospora
pp. 416
[60] Hydroxylamine reductase from Neurospora crassa
pp. 420
[61] Nitrite metabolism
pp. 427
[62] Ribonucleases
pp. 437
[63] Deoxyribonucleases
pp. 448
[64] Preparation of nucleoside phosphorylase from calf spleen
pp. 454
[65] Nicotinamide riboside phosphorylase
pp. 456
[66] Hydrolytic nucleosidases
pp. 464
[67] Nucleoside transdeoxyribosidase from bacteria
pp. 469
[68] 5′-Adenylic acid deaminase from muscle
pp. 473
[69] Specific adenosine deaminase from intestine
pp. 475
[70] Nonspecific adenosine deaminase from takadiastase
pp. 478
[71] Cytosine nucleoside deaminase from Escherichia coli
pp. 480
[72] Guanase
pp. 482
[73] Xanthine oxidase from milk
pp. 485
[74] Uricase
pp. 490
[75] Pyrimidine oxidase and related enzymes
pp. 497
[76] Adenosine phosphokinase
pp. 501
[77] Nucleotide synthesis by tissue extracts
pp. 504
[78] Some methods for the study of de Novo synthesis of purine nucleotides
pp. 523
[79] Acid prostatic phosphatase
pp. 530
[80] Intestinal phosphomonoesterase
pp. 533
[81] Phosphomonoesterase of milk
pp. 539
[82] Phosphomonoesterase of bone
pp. 541
[83] Glucose-6-phosphatase from liver
pp. 543
[84] Fructose-1,6-diphosphatase from liver
pp. 546
[85] “5” nucleotidases
pp. 551
[86] 3′-Nucleotidase from rye grass
pp. 555
[87] Preparation and properties of acetyl phosphatase
pp. 556
[88] Transphosphorylation by phosphatases
pp. 561
[89] Phosphodiesterase from snake venom
pp. 565
[90] Spleen and intestinal phosphodiesterases
pp. 570
[91] Inorganic pyrophosphatase from yeast
pp. 577
[92] Metaphosphatase
pp. 580
[93] Triphosphatase
pp. 582
[94] Myosin adenosinetriphosphatase
pp. 588
[95] Mg-Activated muscle ATPases
pp. 591
[96] Potato apyrase
pp. 593
[97] Mitochondrial ATPase
pp. 595
[98] Insect ATPase
pp. 598
[99] Adenylate kinase (myokinase, ADP phosphomutase)
pp. 605
[100] ATP-Creatine transphosphorylase
pp. 610
[101] Coupling of phosphorylation with oxidation
pp. 619
[102] Pantothenate-synthesizing enzyme
pp. 622
[103] Thiaminase
pp. 629
[104] Folic acid conjugase
pp. 631
[105] d-Biotin oxidase
pp. 633
[106] Pantetheine kinase
pp. 636
[107] Thiaminokinase
pp. 640
[108] Flavokinase
pp. 646
[109] Pyridoxal kinase from brewer's yeast
pp. 649
[110] Dephospho-CoA kinase from pigeon liver
pp. 652
[111] DPN kinase from pigeon liver
pp. 655
[112] Nucleotide pyrophosphatase
pp. 660
[113] Animal tissue DPNase (pyridine transglycosidase)
pp. 664
[114] Neurospora DPNase
pp. 667
[115] Dephospho-CoA pyrophosphorylase
pp. 670
[116] DPN pyrophosphorylase
pp. 673
[117] FAD pyrophosphorylase
pp. 675
[118] UDPG pyrophosphorylase from yeast
pp. 681
[119] Pyridine nucleotide transhydrogenase
pp. 688
[120] DPNH cytochrome c reductase (animal)
pp. 693
[121] DPNH cytochrome c reductase (bacterial)
pp. 699
[122] TPNH cytochrome c reductase from yeast
pp. 704
[123] TPNH cytochrome c reductase (liver)
pp. 707
[124] Diaphorases
pp. 712
[125] Triphosphopyridine and diphosphopyridine nucleotide oxidases
pp. 719
[126] Glutathione reductase (plant)
pp. 722
[127] Glutathione reductase1 (liver and yeast)
pp. 725
[128] Pyridine nucleotide quinone reductase from pea seeds
pp. 729
[129] Hydrogenase from Clostridium Kluyveri
pp. 732
[130] Cytochromes a, a1, a2, and a3
pp. 740
[131] Cytochrome b (mammals)
pp. 744
[132] Cytochrome b group (bacteria)
pp. 749
[133] Cytochrome c (mammals)
pp. 755
[134] Cytochrome c (ustilago)
pp. 758
[135] Cytochrome c and cytochrome c peroxidase from Pseudomonas fluorescens
pp. 764
[136] Assay of catalases and peroxidases
pp. 775
[137] Liver catalase
pp. 781
[138] Blood catalase
pp. 784
[139] Catalase from bacteria (Micrococcus lysodeikticus)
pp. 789
[140] Plant catalase
pp. 791
[141] Peroxidase (liver)
pp. 794
[142] Myeloperoxidase
pp. 801
[143] Plant peroxidase
pp. 813
[144] Lactoperoxidase
pp. 817
[145] Plant tyrosinase (polyphenol oxidase)
pp. 827
[146] Mammalian tyrosinase
pp. 831
[147] Ascorbic acid oxidase
pp. 836
[148] Carbonic anhydrase (plant and animal)
pp. 847
[149] Dehydroascorbic reductase
pp. 851
[150] Cypridina and firefly Luciferase
pp. 857
[151] Bacterial luciferase
pp. 861
[152] Assay and properties of hydrogenases
pp. 871
List of abbreviations
pp. 875
Author index
pp. 895
Subject index
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