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Chow, Cheung-ming. / Thesis submitted in: December 2002. / Thesis (M.Phil.)--Chinese University of Hong Kong, 2003. / Includes bibliographical references (leaves 149-155). / Abstracts in English and Chinese. / Thesis committee --- p.i / Statement --- p.ii / Abstract --- p.iii / Acknowledgement --- p.vi / General abbreviations --- p.viii / Abbreviations of chemicals --- p.ix / List of figures --- p.x / List of tables --- p.xiv / Table of contents --- p.xv / Chapter 1. --- Literature review --- p.1-26 / Chapter 1.1 --- General introduction of nitrogen metabolism in plants --- p.1 / Chapter 1.2 --- Interaction between nitrogen metabolism and other metabolic and developmental pathways in plants --- p.2 / Chapter 1.2.1 --- Carbon metabolism --- p.2 / Chapter 1.2.2 --- Development --- p.2 / Chapter 1.2.3 --- Flowering --- p.3 / Chapter 1.3 --- Metabolic signalling in plants --- p.5 / Chapter 1.3.1 --- Nitrogen signalling in plants --- p.5 / Chapter 1.3.1.1 --- Inorganic N signalling --- p.5 / Chapter 1.3.1.2 --- Organic N signalling --- p.6 / Chapter 1.3.2 --- Carbon signalling --- p.7 / Chapter 1.3.2.1 --- Signalling pathways --- p.7 / Chapter 1.3.2.2 --- Gene expression regulated by sugar --- p.8 / Chapter 1.3.2.3 --- Role of sugar signalling in growth and development --- p.9 / Chapter 1.4 --- Ways to elucidate a new signal transduction pathway --- p.10 / Chapter 1.4.1 --- Carbon signalling as a paradigm to provide hints for exploring nitrogen signalling in plants --- p.10 / Chapter 1.4.2 --- Designing long-term approach to tackle nitrogen signalling in plants --- p.14 / Chapter 1.5 --- "Molecular tools available to change the ""signal"" and the proposed ""sensor""" --- p.15 / Chapter 1.5.1 --- ASN1 overexpressing lines (35S-ASN1) --- p.15 / Chapter 1.5.2 --- PII overexpressing lines (PII ox) & PII truncated lines (PII trunc.) --- p.16 / Chapter 1.5.2.1 --- Plant PII and its possible role --- p.16 / Chapter 1.5.2.2 --- Nitrogen/carbon sensing as the proposed in vivo function of PII-like protein in Arabidopsis thaliana by the in planta bioassay of PII overexpressing (PII ox) lines --- p.17 / Chapter 1.5.2.3 --- Changes in physiological and transcriptional expression of nitrogen assimilatory genes in PII transgenic lines --- p.17 / Chapter 1.6 --- Review on nitrogen controls and sensing mechanism of microbial organism and higher plants --- p.21 / Chapter 1.6.1 --- Nitrogen sensing in enteric bacteria --- p.21 / Chapter 1.6.2 --- Nitrogen sensing in cyanobacteria --- p.21 / Chapter 1.6.3 --- Nitrogen sensing in fungi --- p.22 / Chapter 1.6.4 --- Implication of the nitrogen sensing mechanisms in microorganisms to nitrogen sensing in plants --- p.23 / Chapter 1.7 --- "Hypothesis, objectives and outlines of this thesis work" --- p.25 / Chapter 2 --- Materials and Methods --- p.27-50 / Chapter 2.1 --- Materials --- p.27 / Chapter 2.1.1 --- "Plants,bacterial strains and vectors" --- p.27 / Chapter 2.1.2 --- Chemicals and Regents --- p.28 / Chapter 2.1.3 --- "Buffer, solution and gel" --- p.28 / Chapter 2.1.4 --- Commercial kits --- p.28 / Chapter 2.1.5 --- Equipments and facilities used --- p.29 / Chapter 2.1.6 --- Growth medium --- p.29 / Chapter 2.1.7 --- Primers --- p.29 / Chapter 2.2 --- Methods --- p.29 / Chapter 2.2.1 --- Growth condition for plant materials --- p.29 / Chapter 2.2.1.1 --- General conditions --- p.29 / Chapter 2.2.1.2 --- Mature Arabidopsis for gene expression profile --- p.30 / Chapter 2.2.1.3 --- Arabidopsis seedlings for physiological experiment --- p.30 / Chapter 2.2.2 --- Molecular Techniques --- p.31 / Chapter 2.2.2.1 --- Bacterial cultures for recombinant DNA --- p.31 / Chapter 2.2.2.2 --- Preparation of pBluescript II KS(+) T-vector for cloning --- p.31 / Chapter 2.2.2.3 --- Cloning techniques --- p.32 / Chapter 2.2.2.4 --- Transformation of DH5a competent cell --- p.32 / Chapter 2.2.2.5 --- Gel electrophoresis --- p.33 / Chapter 2.2.2.6 --- DNA and RNA extractions from plant tissues --- p.34 / Chapter 2.2.2.7 --- First strand cDNA synthesis --- p.35 / Chapter 2.2.2.8 --- PCR techniques --- p.35 / Chapter 2.2.2.9 --- Sequencing --- p.37 / Chapter 2.2.3 --- Analysis of sequences and homology search --- p.37 / Chapter 2.2.4 --- Biochemical analysis --- p.41 / Chapter 2.2.4.1 --- Sugar content analysis --- p.41 / Chapter 2.2.4.2 --- Anthocyanin content analysis --- p.42 / Chapter 2.2.4.3 --- Fresh weight measurement --- p.43 / Chapter 2.2.4.4 --- Statistic analysis --- p.43 / Chapter 2.2.5 --- Generation of crossing progenies --- p.44 / Chapter 2.2.5.1 --- Artificial crossing of A. thaliana --- p.44 / Chapter 2.2.5.2 --- PCR screening for successful crossing --- p.44 / Chapter 2.2.6 --- Construction of subtractive libraries --- p.45 / Chapter 2.2.7 --- Reverse-dot blot screening --- p.45 / Chapter 2.2.7.1 --- in vitro transcription for making ampicillin cRNA --- p.46 / Chapter 2.2.7.2 --- PCR amplification --- p.47 / Chapter 2.2.7.3 --- Dot-blotting of PCR products on nylon membrane --- p.48 / Chapter 2.2.7.4 --- P probe preparation --- p.49 / Chapter 2.2.7.5 --- Hybridization --- p.49 / Chapter 2.2.7.6 --- Signal detection --- p.50 / Chapter 3 --- Results --- p.51-124 / Chapter 3.1 --- Differential growth behaviour and sugar content in 35S-ASNI lines --- p.51 / Chapter 3.1.1 --- Growth of the seedlings of 35S-ASN1 lines under different N and C supplementations --- p.51 / Chapter 3.1.2 --- Lowered reducing sugar content in 35S-ASN1 lines --- p.52 / Chapter 3.2 --- Development of markers for nitrogen signalling events related to altered N status in 35S-ASN1 lines --- p.60 / Chapter 3.2.1 --- Sugar-induced anthocyanin levels as common morphological marker shared by 35S-ASN1 lines and PII transgenic lines --- p.60 / Chapter 3.2.2 --- Expression markers related to altered N status in 35-ASN1 lines --- p.64 / Chapter 3.3 --- Generation of transgenic plants constitutively expressing ASN1 and GLB1 (or ASN1 and truncated GLB1) through crossing --- p.74 / Chapter 3.4 --- Search for homologs of well-known microbial nitrogen signalling components in Arabidopsis thaliana --- p.78 / Chapter 3.4.1 --- Homologs of yeast general amino acid control components --- p.80 / Chapter 3.4.1.1 --- Arabidopsis thaliana GCN2-like protein --- p.80 / Chapter 3.4.1.2 --- Arabidopsis thaliana GCN1 -like protein --- p.84 / Chapter 3.4.1.3 --- Arabidopsis thaliana GCN20-like protein --- p.84 / Chapter 3.4.1.4 --- Plant eIF2α --- p.86 / Chapter 3.4.1.5 --- Arabidopsis thaliana GCN4-CRE like sequences --- p.87 / Chapter 3.4.2 --- Homologs of fungi nitrogen sensing components: Globally acting factor in nitrogen control in fungi --- p.89 / Chapter 3.4.3 --- Homologs of cyanobacteria nitrogen control components: IF7 & IF 17 (Negative regulators of GS activity) --- p.89 / Chapter 4 --- Discussion --- p.125-147 / Chapter 4.1 --- Differential physiological and morphological behaviours found in the comparative studies between control lines and 35S-ASN1 lines --- p.125 / Chapter 4.1.1 --- in planta promotive effect of ASN1 overexpression on the seedlings growth under low nitrogen and in the absence of exogenous applied metabolizable sugar --- p.125 / Chapter 4.1.2 --- Modulation of sugar level in 35S-ASN1 lines --- p.126 / Chapter 4.2 --- Development of morphological marker and gene expression markers --- p.128 / Chapter 4.2.1 --- Anthocyanin accumulation as a morphological marker for epistatic analysis --- p.128 / Chapter 4.2.2 --- Differential expressed genes as candidates for gene expression markers of nitrogen signalling event --- p.131 / Chapter 4.3 --- Arabidopsis homolog search for well-known microbial signalling components --- p.132 / Chapter 4.3.1 --- "Possible amino acid sensing system in Arabidopsis constructed by homologs of yeast GCN2, GCN1, GCN20 and eIF2a" --- p.132 / Chapter 4.3.1.1 --- Arabidopsis GCN2-like (A. thaliana GCN2-like) protein --- p.132 / Chapter 4.3.1.2 --- Arabidopsis GCNl-like (A. thaliana GCNl-like) & GCN20-like (A. thaliana GCNl-like) proteins --- p.136 / Chapter 4.3.1.3 --- Plant eIF2a phosphorylation pathway --- p.139 / Chapter 4.3.1.4 --- GCN4 related transcriptional factors and GCN4-like motif (GLM) cis-element in plants --- p.140 / Chapter 4.3.1.5 --- Implication of the presence of plant homologs of fungi regulatory proteins involved in the general control of amino acid biosynthesis --- p.142 / Chapter 4.3.2 --- Failure in identifying homologs of nitrogen regulators responsible for switching of nitrogen source in Arabidopsis --- p.144 / Chapter 4.4 --- Overview of research platform construction --- p.146 / Chapter 5 --- Conclusion and Perspectives --- p.148 / Chapter 6 --- References --- p.149-155 / Chapter 7 --- Appendix --- p.156-167

It is known that the functional activity of the nervous system is associated with ammonia formation and that the administration of ammonium salts to experimental animals produces convulsions. Mechanisms, therefore, that control ammonia metabolism in the brain are of importance for brain cell function. The presence of ammonia utilizing mechanisms in the brain maintains the low free cerebral ammonia levels found in vivo. There is, however, a rapid formation of ammonia in the brain on the death of the animal and a further liberation of ammonia takes place when isolated brain cortex is incubated aerobically in the absence of glucose. Studies of these and other aspects of ammonia metabolism form the subject matter of this thesis. The estimation of ammonia in these studies is based on a modification of the diffusion technique of Conway. Ammonia and amino acid analyses have been carried out using the Beckman amino acid analyzer. The rapid rate of cerebral ammonia formation that takes place when the brain is removed from the animal is partially arrested by trichloracetic acid (TCA), presumably by the inactivation of cerebral enzymes. Our results rule out the possibility that glutamine, glutamate, taurine and ATP are significant contributors to the initial or pre-incubation levels of ammonia and the evidence favors the involvement of TCA-insoluble components as precursors of such ammonia. In the presence of glucose the pre-incubation levels of amino acids of cerebral cortex slices of the rat are maintained during subsequent aerobic incubation at 37°C for one hour. In the absence of glucose, however, we have found marked changes in the pre-incubation levels of amino acids of cerebral cortex slices under these experimental conditions. A considerable rise of ammonia also occurs in the absence of glucose and this can be largely accounted for by a net loss of –NH₂-groups of the amino acid pools of brain slices. The significant fall in the cerebral levels of glutamate and glutamine under these conditions indicates that for short periods of incubation (one hour), these amino acids may serve as major sources of ammonia formation by respiring brain cortex slices. Our findings of a marked suppression of ammonia formation by cerebral cortex slices incubated for one hour either anaerobically, or aerobically, in a glucose-free medium in the presence of amytal, D-glutamate or α-methylglutamate, implicate the oxidative deamination of cerebral glutamate as a major mechanism for ammonia liberation. D-glutamate also acts by inhibiting the hydrolysis of glutamine. In the presence of glucose aerobic incubation with 2, 4-dinitrophenol, iodoacetate, malonate, hydroxylamine or D-glutamate, increases the rate of ammonia formation by cerebral cortex slices. This is doubtless due to diminished activity of cerebral glutamine synthetase required for ammonia fixation to occur. We find that the level of ammonia in the brain tissue itself is not markedly affected by the presence of absence of glucose. The increased quantity of ammonia formed by cerebral cortex slices in the absence of glucose is found largely in the incubation medium. This fact points to the formation of ammonia in specific compartment(s), and the retention of ammonia within such compartment(s) up to a certain level. Above this level there is efflux of ammonia into the incubation medium. Such a conclusion helps to explain the apparent high concentration ratio (tissue:medium) of NH₄⁺ obtained either aerobically (viz. 42) or anaerobically (viz. 12) at the end of one hour incubation in the presence of glucose. There is some accumulation of NH₄⁺ ions in rat brain cortex slices against a concentration gradient. Our finding that ouabain stimulates ammonia formation in respiring cerebral cortex slices is in accord with the fact that ouabain inhibits the utilization-of NH₄⁺ for the biosynthesis of glutamine, presumably by affecting the transport of NH₄⁺ to the site of glutamine synthesis. Ouabain has no effect on the cerebral glutaminase of the rat. / Medicine, Faculty of / Biochemistry and Molecular Biology, Department of / Graduate

Dissertation (PhD)--University of Stellenbosch, 2002. / ENGLISH ABSTRACT: Saccharomyces cerevisiae uses the nitrogenous compounds in its environment selectively. The basis of this phenomenon is the transcriptional regulation of genes whose products are required for nitrogen catabolism. A rich nitrogen source represses the expression of genes required for the degradation of poor nitrogen sources via the action of the target of rapamyein (TOR) signaling cascade. If only a poor nitrogen source is available, these genes are derepressed. This process is known as nitrogen catabolite repression (NCR) or nitrogen regulation. The DALI and DAL4 genes of S. cerevisiae are transcribed divergently from the 829 bp intergenic region. The five known UASNTR elements (GATAI-5) were mutated in the full context of the intergenic promoter. All five elements are required for the transcriptional activation of DAL4. The two elements most proximal to DAL4 (GATA4 and GATA5) contributed the most and the one most distal (GATAI) contributed the least to its expression. In contrast, three of the five elements (GATA2-4) are required for DALI activation. In addition, analyses revealed that no single element is shared equally between these two genes. Predictions as to the function of known nitrogen-regulating elements based on their sequence and location proved to be inaccurate in some cases. Mutation analyses of the three UISALL elements present in the intergenic promoter region revealed that UIS8, which does not share a high degree of homology with the consensus UISALL sequence, is required the most for transcriptional induction of both DALI and DAL4. Also, UIS7, which shares the most similarity with the UISALL consensus sequence, has the phenotype of a repressor-like element when mutated. These observations therefore portray the opposite phenotypes of what was expected. We identified a regulator, Vid30p, which is required for the transcriptional response of S. cerevisiae in low ammonia conditions. Genetic analyses of the vid30/j, mutant indicate that Vid30p functions by regulating the expression of genes required for the production and degradation of glutamate. The transcription of VID30 is NCR-sensitive, highly induced by low concentrations of ammonia, and rapamycin-sensitive. In addition, the vid30/j, mutant is hypersensitive to rapamycin, indicating that this protein is, directly or indirectly, controlled by the TOR signaling pathway. / AFRIKAANSE OPSOMMING: Saccharomyces cerevisiae het die vermoeë om stikstofbronne vanuit die omgewing selektief te benut. Die basis van hierdie verskynsel is die transkripsionele regulering van gene wat vir proteïene kodeer wat stikstof katabolisme bemiddel. 'n Goeie stikstofbron onderdruk die transkripsie van gene wat met die degradering van swak stikstofbronne gemoeid is. Hierdie onderdrukking word deur die teiken-van-rapamisien (TVR)-seintransduksiepad bewerkstellig. Wanneer slegs 'n swak stikstofbron beskikbaar is, word hierdie gene geaktiveer. Hierdie verskynsel staan as stikstofkatabolietonderdrukking (SKR) of stikstofregulering bekend. Die DALI- en DAL4-gene van S. cerevisiae word divergent vanaf 'n 829 bp intergeniese area getranskribeer. Vyf UASNTR-elemente (GATAI-5) is in die volle konteks van die intergeniese promotor gemuteer. Al vyf elemente word vir DAL4 transkripsionele aktivering benodig. Die twee elemente mees proksimaal tot DAL4 (GATA4 en GATA5) lewer die grootste bydrae tot DAL4-geenuitdrukking, terwyl die mees distale element (GATAI) die kleinste bydrae lewer. In teenstelling hiermee lewer slegs drie van die vyf elemente (GATA2-4) 'n noemenswaardige bydrae tot DALI se uitdrukking. Nie een van die vyf elemente lewer 'n gelykwaardige bydrae tot die uitdrukking van DALI en DAL4 nie. Voorspellings betreffende die bydrae van die onderskeie UASNTR-elemente tot die uitdrukking van die DALI- en DAL4-gene, gebaseer op die sekwens en die posisie van die element in die promotor, was meestal onakkuraat. Die drie U/SALL-elemente in die intergeniese area is gemuteer en toon dat U/S8, wat nie 'n groot mate van homologie met die U/SALL konsensus sekwens deel nie, die mees kritiese element vir transkripsionele induksie van beide DALI en DAL4 is. UIS7, wat 'n hoër mate van homologie met die UISALL konsensus sekwens deel, toon die fenotipe van 'n onderdrukkingselement wanner dit gemuteer word. Hierdie waarnemings is dus die teenoorgestelde van wat verwag is. Ons het 'n reguleerder, Vid30p, geïdentifiseer wat benodig word VIr die transkripsionele response van stikstofgereguleerde gene in lae konsentrasie ammonium. Genetiese analises van die vid3011 mutant toon dat Vid30p funksioneer deur die transkripsie van gene gemoeid met die vorming en degradering van glutamaat te reguleer. Die transkripsie van V/D30 is SKO-sensitief, word sterk deur lae konsentrasies ammonium geïnduseer, en is rapamisien-sensitief. Die vid30t!. mutant is ook hipersensitief vir rapamisien, wat aandui dat Vid30p, direk of indirek, deur die TVR-seintransduksiepad gereguleer word.

No description available.

Thesis (Ph.D.) Department of Agronomy, University of Adelaide, 1981.

The purpose of the present study is to determine the nitrogen intake and output (in both urine and feces) of two groups of Texas college women living in the Home Management House at North Texas State College.

No description available.

by Deng Yu. / Thesis (M.Phil.)--Chinese University of Hong Kong, 1999. / Includes bibliographical references (leaves 111-120). / Abstract also in Chinese. / Acknowledgements --- p.i / Abstract --- p.ii / List of Abbreviations --- p.viii / List of Tables --- p.ix / List of Figures --- p.x / Chapter 1 --- Introduction / Chapter 1.1 --- Primary nitrogen metabolism in fungi --- p.1 / Chapter 1.1.1 --- Ammonium assimilation --- p.4 / Chapter 1.1.2 --- Regulation of ammonium assimilating enzymes --- p.8 / Chapter 1.2 --- Relevant central carbon metabolism in fungi --- p.11 / Chapter 1.2.1 --- Glyoxylate cycle and isocitrate metabolism --- p.11 / Chapter 1.2.2 --- GABA shunt --- p.15 / Chapter 1.3 --- Relationship between nitrogen metabolism and fungi morphogenesis --- p.15 / Chapter 1.4 --- General background of Volvariella volvacea --- p.17 / Chapter 1.5 --- Objectives of the study --- p.20 / Chapter 2 --- Materials and methods / Chapter 2.1 --- Organism --- p.22 / Chapter 2.2 --- Growth media --- p.22 / Chapter 2.2.1 --- Basal medium --- p.22 / Chapter 2.2.2 --- Solid-state cultivation --- p.23 / Chapter 2.3 --- Effect of different nitrogen sources on the mycelial growth of V volvacea in submerged culture --- p.26 / Chapter 2.4 --- Effect of different carbon and nitrogen sources and concentrations on the production of selected enzymes involved in central carbon and nitrogen metabolism --- p.27 / Chapter 2.5 --- Enzyme extraction --- p.28 / Chapter 2.6 --- Enzyme assays --- p.28 / Chapter 2.6.1 --- NAD-dependent glutamate dehydrogenase --- p.28 / Chapter 2.6.2 --- NADP-dependent glutamate dehydrogenase --- p.29 / Chapter 2.6.3 --- NAD- dependent isocitrate dehydrogenase --- p.29 / Chapter 2.6.4 --- Isocitrate lyase --- p.30 / Chapter 2.7 --- Protein determination --- p.30 / Chapter 2.8 --- Determination of optimum pH for enzyme assays --- p.31 / Chapter 2.9 --- Determination of optimum temperatures for enzyme assays --- p.31 / Chapter 2.10 --- Transfer experiments --- p.31 / Chapter 2.11 --- Enzyme stability --- p.32 / Chapter 2.12 --- Purification of NAD-dependent glutamate dehydrogenase --- p.33 / Chapter 2.12.1 --- Ammonium sulphate precipitation --- p.33 / Chapter 2.12.2 --- Ion exchange chromatography --- p.33 / Chapter 2.12.3 --- Ultrafiltrartion --- p.34 / Chapter 2.12.4 --- Gel filtration chromatography --- p.34 / Chapter 2.12.5 --- Affinity chromatography --- p.34 / Chapter 2.13 --- Electrophoresis --- p.35 / Chapter 2.13.1 --- SDS polyacrylamide gel electrophoresis --- p.35 / Chapter 2.13.2 --- Native polyacrylamide gel electrophoresis --- p.35 / Chapter 2.13.3 --- Activity staining for NAD-dependent glutamate dehydrogenase --- p.36 / Chapter 2.13.4 --- Protein staining --- p.36 / Chapter 2.14 --- NAD-dependent glutamate dehydrogenase characterization studies --- p.37 / Chapter 2.14.1 --- Effect of substrate concentration --- p.37 / Chapter 2.14.2 --- Molecular weight determination --- p.37 / Chapter 2.14.2.1 --- Molecular weight determination by gel filtration chromatography --- p.37 / Chapter 2.14.2.2 --- Molecular weight determination by native PAGE --- p.38 / Chapter 2.14.2.3 --- Protein subunit molecular weight determination by SDS- PAGE --- p.38 / Chapter 3 --- Results / Chapter 3.1 --- Effect of different nitrogen sources on the mycelial growth of V. volvacea in submerged culture --- p.39 / Chapter 3.2 --- Optimum assay conditions for NAD-dependent glutamate dehydrogenase --- p.42 / Chapter 3.3 --- Optimum assay conditions for NADP-dependent glutamate dehydrogenase --- p.46 / Chapter 3.4 --- Optimum assay conditions for NAD-dependent isocitrate dehydrogenase --- p.50 / Chapter 3.5 --- Optimum assay conditions for isocitrate lyase --- p.54 / Chapter 3.6 --- Biomass production and enzyme activities in extracts of in vegetative mycelia grown with different nitrogen and carbon sources provided at different concentrations --- p.58 / Chapter 3.6.1 --- Mycelia growth under different conditions --- p.58 / Chapter 3.6.2 --- NAD- and NADP-dependent glutamate dehydrogenases in extracts of vegetative mycelia grown with different nitrogen and carbon sources provided at different conditions --- p.58 / Chapter 3.6.3 --- NAD-dependent isocitrate dehydrogenase and isocitrate lyase in vegetative mycelia grown with different nitrogen and carbon sources provided at different conditions --- p.64 / Chapter 3.7 --- Transfer experiments --- p.67 / Chapter 3.7.1 --- Activities of glutamate dehydrogenases in extracts of myceila transferred to media containing different carbon sources --- p.67 / Chapter 3.7.2 --- Effect of different carbon sources on the glutamate dehydrogenases in submerged cultures --- p.67 / Chapter 3.8 --- Glutamate dehydrogenase activity in various parts of the fruit body during different stages of fruit body development --- p.70 / Chapter 3.9 --- Stabilization of NAD-dependent glutamate dehydrogenase activity --- p.75 / Chapter 3.10 --- Purification of NAD-dependent glutamate dehydrogenase --- p.77 / Chapter 3.10.1 --- Ammonium sulphate precipitation --- p.77 / Chapter 3.10.2 --- Partial purification by column chromatography --- p.78 / Chapter 3.10.3 --- Electrophoretic determination of the protein profiles of crude extract and partially purified samples --- p.83 / Chapter 3.11 --- Characterization of partially purified NAD-dependent glutamate dehydrogenase from V. volvacea --- p.86 / Chapter 3.11.1 --- Optimum pH and temperature --- p.86 / Chapter 3.11.2 --- Kinetic parameters --- p.86 / Chapter 3.11.3 --- Molecular weight --- p.92 / Chapter 3.11.3.1 --- Molecular weight determination by gel filtration chromatography --- p.92 / Chapter 3.11.3.2 --- Molecular weight determination by native PAGE --- p.92 / Chapter 3.11.3.3 --- Subunit molecular weight determination by SDS-PAGE --- p.92 / Chapter 4 --- Discussion / Chapter 4.1 --- Nutrient nitrogen for the growth of Volvariella volvacea --- p.97 / Chapter 4.1.1 --- Mycelial growth on simple nitrogen compounds --- p.97 / Chapter 4.1.2 --- Nutrient nitrogen in mushroom compost --- p.98 / Chapter 4.2 --- Production and regulation of selected enzymes in vegetative mycelia --- p.98 / Chapter 4.2.1 --- Production and regulation of glutamate dehydrogenases --- p.98 / Chapter 4.2.2 --- Production and regulation of isocitrate dehydrogenase and isocitrate lyase --- p.103 / Chapter 4.3 --- Glutamate dehydrogenases and fruit body development --- p.104 / Chapter 4.4 --- Purification and characterization of NAD-dependent glutamate dehydrogenase --- p.105 / Chapter 4.4.1 --- Enzyme purification --- p.105 / Chapter 4.4.2 --- Enzyme stability --- p.106 / Chapter 4.4.3 --- Enzyme properties --- p.107 / Chapter 4.5 --- Future works: nitrogen metabolism and the growth of Vohariella volvacea --- p.109 / References --- p.111

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