Enzymes of the glycolate pathway in plants without CO2-photorespiration

1970 ◽  
Vol 48 (6) ◽  
pp. 1219-1226 ◽  
Author(s):  
D. W. Rehfeld ◽  
D. D. Randall ◽  
N. E. Tolbert
Keyword(s):  
Specific Activity ◽  
Cell Types ◽  
Total Activity ◽  
Glycolate Oxidase ◽  
Mesophyll Cells ◽  
Hydroxypyruvate Reductase ◽  
Glycolate Metabolism ◽  
Wet Weight ◽  
Reduced Nicotinamide Adenine Dinucleotide ◽  
Sheath Cells

Extracts, mainly from mesophyll cells, were obtained by grinding cells in a Waring Blendor; then extracts of parenchyma sheath cells were obtained by exhaustive grinding of the blender residue in a roller mill or mortar with sand. The specific activities of P-glycolate phosphatase, glycolate oxidase, catalase and reduced nicotinamide adenine dinucleotide- (NADH-) hydroxypyruvate reductase were fourfold higher in extracts of the parenchyma sheath cells than in the mesophyll cells from corn, sugarcane, and Atriplex rosea. P-Glycerate phosphatase was mainly located in the mesophyll cells. The total activity of glycolate oxidase in plants without CO2-photorespiration averaged about one-third that found in other plants on a wet-weight basis. Glycolate oxidase activity in Atriplex rosea, without CO2-photorespiration, was about the same as in Atriplex patula, with CO2-photorespiration. It is concluded that enzymes for glycolate metabolism are present in all leaves in substantial amounts and are located in both cell types, although a higher specific activity is in the parenchyma sheath cells. Thus it is proposed that photorespiration occurs in all plants, but that CO2 evolution from glycolate metabolism is not manifested in plants which have high levels of activity for the C4-dicarboxylic acid cycle of CO2 fixation.

Glycolate metabolism in young and old tobacco leaves, and effects of α-hydroxy-2-pyridinemethanesulfonic acid

1973 ◽  
Vol 51 (10) ◽  
pp. 1857-1865 ◽  
Author(s):  
Marvin L. Salin ◽  
Peter H. Homann
Keyword(s):  
Gas Exchange ◽  
Leaf Tissue ◽  
Glycolate Oxidase ◽  
Low Permeability ◽  
Mesophyll Cells ◽  
Tobacco Leaves ◽  
Young Leaves ◽  
Glycolate Metabolism ◽  
Lower Ability ◽  
Compensation Concentration

Young tobacco leaves photorespire less than older leaves. This difference is reflected by lower activities of photorespiratory enzymes in young leaves, and by an apparent inability to synthesize glycolate, the substrate of photorespiration.It is shown in this paper that young tobacco leaves differ from old ones in the following, additional respects: (1) extracts have a much lower ability to decarboxylate glycine; (2) the transient burst of CO2 after lowering of the light intensity is nearly absent; (3) photosynthesis is much less inhibited when leaves are floated on solutions of the inhibitor of glycolate oxidase α-hydroxy-2-pyridinemethanesulfonic acid (HPMS); (4) the CO2 compensation concentration is higher; and (5) the mesophyll cells are much more densely packed.It is concluded that the small photorespiratory gas exchange of young leaves is due to deficiencies in enzymes of glycolate metabolism and perhaps to a slow synthesis of glycolate. The latter may be explained by a relatively high internal CO2 concentration resulting from large physical resistances to gas exchange in the tissue. However, the rate of glycolate formation possibly is underestimated because of a low permeability of young leaf tissue to HPMS.Other results provide evidence that HPMS alters the biochemical pattern of CO2 photoassimilation in old tobacco leaves under certain conditions. Hence, this poison ought to be used with caution in studies on photorespiration and glycolate metabolism.

scholarly journals Electron Probe Microanalysis of Potassium and Chloride in Freeze-Substituted Leaf Sections of Zea Mays

1973 ◽  
Vol 26 (5) ◽  
pp. 1015 ◽  
Author(s):  
CK Pallaghy
Keyword(s):  
Potassium Concentration ◽  
Cell Types ◽  
Bundle Sheath ◽  
Concentration Gradients ◽  
Mesophyll Cells ◽  
Transmission Electron ◽  
Bundle Sheath Cells ◽  
Scanning Transmission ◽  
Diamond Knife ◽  
Sheath Cells

Small sections of leaves were floated on distilled water under either light or dark conditions, and were freeze-substituted in a 1 % solution of osmium tetroxide in acetone at -78�C followed by embedding in an epoxy resin. Approximately I-11m-thick sections were cut using a dry diamond knife and examined by scanning transmission electron microscopy. The relative concentrations of potassium and chloride in subcellular compartments were determined using an energy dispersive X-ray analyser. The concentration of sodium in the leaf (1�7 m-equivjkg of wet tissue) was too low to be detected by this method. The spatial resolution of this technique was sufficient to distinguish between concentrations in the chloroplasts, cytoplasm, vacuole, and nuclei. The concentration of chloride in stomata and some other epidermal cells was very much higher than in either mesophyll or bundle sheath cells. The potassium concentration in some vascular cells was at least two- to threefold higher than that in mesophyll or bundle sheath cells. The Cl : K ratio in mesophyll and bundle sheath cells resembled that in the solution (0 �10) used for growing the plants. The concentration of chloride in the "free" cytoplasm of mesophyll cells was always very low. Significant differences were found in the "ion" relations of mesophyll and bundle sheath cells. Whereas the ratio of potassium concentration between the vacuole and chloroplasts of mesophyll cells was high (1 �19) in the light and low (0�65) in the dark, the opposite was true for bundle sheath cells-O� 65 and 0�86 respectively. The ratio of potassium concentration between the vacuo les of mesophyll and those of bundle sheath cells was 1 �48 in the light, but only 0�76 in the dark. These concentration gradients are discussed in relation to a possible transfer of organic acid salts of potassium between these two cell types.

bundle sheath defective, a mutation that disrupts cellular differentiation in maize leaves

Development ◽  
1994 ◽  
Vol 120 (3) ◽  
pp. 673-681 ◽  
Author(s):  
J. A. Langdale ◽  
C. A. Kidner
Keyword(s):  
Gene Action ◽  
Morphological Differentiation ◽  
Cell Types ◽  
Bundle Sheath ◽  
Sheath Cell ◽  
Mesophyll Cells ◽  
Bundle Sheath Cell ◽  
Bundle Sheath Cells ◽  
Maize Leaves ◽  
Sheath Cells

Post-primordial differentiation events in developing maize leaves produce two photosynthetic cell types (bundle sheath and mesophyll) that are morphologically and biochemically distinct. We have isolated a mutation that disrupts the differentiation of one of these cell types in light-grown leaves. bundle sheath defective 1-mutable 1 (bsd1-m1) is an unstable allele that was induced by transposon mutagenesis. In the bundle sheath cells of bsd1-m1 leaves, chloroplasts differentiate aberrantly and C4 photosynthetic enzymes are absent. The development of mesophyll cells is unaffected. In dark-grown bsd1-m1 seedlings, morphological differentiation of etioplasts is only disrupted in bundle sheath cells but photosynthetic enzyme accumulation patterns are altered in both cell types. These data suggest that, during normal development, the Bsd1 gene directs the morphological differentiation of chloroplasts in a light-independent and bundle sheath cell-specific fashion. In contrast, Bsd1 gene action on photosynthetic gene expression patterns is cell-type independent in the dark (C3 state) but bundle sheath cell-specific in the light (C4 state). Current models hypothesize that C4 photosynthetic differentiation is achieved through a light-induced interaction between bundle sheath and mesophyll cells (J. A. Langdale and T. Nelson (1991) Trends in Genetics 7, 191–196). Based on the data shown in this paper, we propose that induction of the C4 state restricts Bsd1 gene action to bundle sheath cells.

scholarly journals Four Mutant Alleles Elucidate the Role of the G2 Protein in the Development of C4 and C3 Photosynthesizing Maize Tissues

Genetics ◽  
2001 ◽  
Vol 159 (2) ◽  
pp. 787-797
Author(s):  
Lizzie Cribb ◽  
Lisa N Hall ◽  
Jane A Langdale
Keyword(s):  
Cell Types ◽  
Bundle Sheath ◽  
Primary Role ◽  
Ribulose Bisphosphate Carboxylase ◽  
Sheath Cell ◽  
Mesophyll Cells ◽  
Phenotypic Data ◽  
Bisphosphate Carboxylase ◽  
Bundle Sheath Cell

Abstract Maize leaf blades differentiate dimorphic photosynthetic cell types, the bundle sheath and mesophyll, between which the reactions of C4 photosynthesis are partitioned. Leaf-like organs of maize such as husk leaves, however, develop a C3 pattern of differentiation whereby ribulose bisphosphate carboxylase (RuBPCase) accumulates in all photosynthetic cell types. The Golden2 (G2) gene has previously been shown to play a role in bundle sheath cell differentiation in C4 leaf blades and to play a less well-defined role in C3 maize tissues. To further analyze G2 gene function in maize, four g2 mutations have been characterized. Three of these mutations were induced by the transposable element Spm. In g2-bsd1-m1 and g2-bsd1-s1, the element is inserted in the second intron and in g2-pg14 the element is inserted in the promoter. In the fourth case, g2-R, four amino acid changes and premature polyadenylation of the G2 transcript are observed. The phenotypes conditioned by these four mutations demonstrate that the primary role of G2 in C4 leaf blades is to promote bundle sheath cell chloroplast development. C4 photosynthetic enzymes can accumulate in both bundle sheath and mesophyll cells in the absence of G2. In C3 tissue, however, G2 influences both chloroplast differentiation and photosynthetic enzyme accumulation patterns. On the basis of the phenotypic data obtained, a model that postulates how G2 acts to facilitate C4 and C3 patterns of tissue development is proposed.

Nitrate metabolism in relation to the aspartate-type C-4 pathway of photosynthesis in Eleusine coracana

1974 ◽  
Vol 52 (12) ◽  
pp. 2599-2605 ◽  
Author(s):  
C. K. M. Rathnam ◽  
V. S. R. Das
Keyword(s):  
Glutamate Dehydrogenase ◽  
Eleusine Coracana ◽  
Bundle Sheath ◽  
Chloroplast Envelope ◽  
Mesophyll Cells ◽  
Bundle Sheath Cells ◽  
Nitrate Metabolism ◽  
Type C ◽  
Envelope Membranes ◽  
Sheath Cells

The intercellular and intracellular distributions of nitrate assimilating enzymes were studied. Nitrate reductase was found to be localized on the chloroplast envelope membranes. The chloroplastic NADPH – glutamate dehydrogenase was concentrated in the mesophyll cells. The extrachloroplastic NADH – glutamate dehydrogenase was localized in the bundle sheath cells. Glutamate synthesized in the mesophyll chloroplasts was interpreted to be utilized exclusively in the synthesis of aspartate, while in the bundle sheath cells it was thought to be consumed in other cellular metabolic processes. Based on the results, a scheme is proposed to account for the nitrate metabolism in the leaves of Eleusine coracana Gaertn. in relation to its aspartate-type C-4 pathway of photosynthesis.

5α-Reductase activity in stroma and epithelium of rat prostate and epididymis. A contribution to elucidation of the mechanism for development of hyperplastic growth of prostatic tissue

1983 ◽  
Vol 103 (2) ◽  
pp. 273-281 ◽  
Author(s):  
Ole Djøseland ◽  
Nicholas Bruchovsky ◽  
Paul S. Rennie ◽  
Navdeep Otal ◽  
Sian Høglo
Keyword(s):  
Enzyme Activity ◽  
Specific Activity ◽  
Reductase Activity ◽  
Major Change ◽  
Growth Stimulation ◽  
Total Activity ◽  
Prostatic Tissue ◽  
Ventral Prostate ◽  
Total Enzyme Activity ◽  
Abnormal Growth

Abstract. The 5α-reductase activity was assayed in homogenates of stroma and epithelium in the rat ventral prostate and epididymis. Samples consisting of 0.3 mg/ml tissue protein in TES buffer, pH 7.0 were incubated at 37°C for 30 min in the presence of 50 nm [1,2-3H]testosterone and a NADPH-generating system started with 5 × 10−4 m NADP. The yield of 5α-reduced metabolites, as established by using thin-layer chromatography, gave an estimate of enzyme activity. Whereas the specific activity of 5α-reductase was highest in prostatic stroma and epididymal epithelium, most of the total enzyme activity was associated with the epithelium in both the prostate and epididymis. The effect of dihydrotestosterone on specific activity of 5α-reductase was studied by administering the hormone to 7-day castrated rats. In prostate, the specific activity of both stromal and epithelium forms of the enzyme reached a maximum after 4 days of treatment. In epididymis only the epithelial form of 5α-reductase underwent a major change in specific activity, the latter peaking after 8–12 days of treatment. Furthermore, while the total activity of 5α-reductase in the prostatic tissue fractions could be induced by as much as 4-fold the normal control values, the epididymal enzyme could not be induced above the normal level either in the stroma or the epithelium. This may explain the relative resistance of epididymis to abnormal growth stimulation under the influence of hormones.

Quantitative Evaluation of Allelopathic Potentials in Soils: Total Activity Approach

Weed Science ◽  
2010 ◽  
Vol 58 (3) ◽  
pp. 258-264 ◽  
Author(s):  
Syuntaro Hiradate ◽  
Kenji Ohse ◽  
Akihiro Furubayashi ◽  
Yoshiharu Fujii
Keyword(s):  
Cinnamic Acid ◽  
Specific Activity ◽  
Quantitative Estimation ◽  
Alluvial Soil ◽  
Total Activity ◽  
Mucuna Pruriens ◽  
Maximum Effect ◽  
Published Data ◽  
Plant Materials ◽  
Allelopathic Potential

The allelopathic potential of a plant has been evaluated on the basis of two indicators: specific activity, which is the specific concentration of the allelochemical to exert a half-maximum effect on a receiver plant (EC50), and total activity in a plant, which is the ratio of the concentration of an allelochemical in the producing plant to its EC50. In the present study, a new indicator, total activity in a soil, which takes into account the effects of a soil on the allelopathy activity, is proposed because allelopathic activity is affected by the presence of soils. The total activity in a soil was calculated by multiplying the “total activity in a plant” with a “soil factor.” In this calculation, we assumed simplified cases for comparison, such that the allelopathic plant materials are evenly incorporated in the soils and the allelochemicals are released from the plant materials to the soils at a constant rate. We conducted bioassay experiments in the presence and absence of soils and cited some published data to calculate the specific activities and total activities in a plant and in a soil. The results indicated that the allelopathies of buckwheat caused by (+)-catechin, Leucaena leucocephala by L-mimosine, Xanthium occidentale by trans-cinnamic acid, and Brassica parachinensis by cis-cinnamic acid were not significant in a volcanic ash soil, an alluvial soil, and a calcareous soil, but the allelopathy of sweet vernalgrass caused by coumarin and Spiraea thunbergii by cis-cinnamoyl glucosides was highly effective in those soils. The allelopathies of Juglans species caused by juglone plus juglone precursors and Mucuna pruriens by L-DOPA would depend highly on the soil types. Although some limitations exist for this approach, the total activity approach would allow for a better quantitative estimation of the allelopathic potential of plant materials in soils.

scholarly journals Covalent Immobilization of Thiol Proteinases on Chitosan

2020 ◽  
Vol 2 (1) ◽  
pp. 7
Author(s):  
Svetlana Olshannikova ◽  
Victoria Koroleva ◽  
Marina Holyavka ◽  
Alexander Pashkov ◽  
Valeriy Artyukhov
Keyword(s):  
Specific Activity ◽  
Crosslinking Agent ◽  
Total Activity ◽  
Covalent Immobilization ◽  
Tropical Plants ◽  
Chitosan Matrix ◽  
Plant Enzymes ◽  
Thiol Proteases ◽  
Thiol Proteinases ◽  
Wide Substrate Specificity

Plant enzymes such as ficin (EC 3.4.22.3), papain (EC 3.4.22.2) and bromelain (EC 3.4.22.4) are obtained from tropical plants. These biocatalysts belong to thiol proteases, in the active center of which cysteine is contained. Ficin, papain and bromelain have a wide substrate specificity, which provides a demand for their use in various industries. Enzymes in the free state are less commonly used; immobilized biocatalysts are the preferred form. The aim of this work was to determine the optimal concentration of a crosslinking agent in the covalent immobilization of ficin, papain and bromelain on a chitosan matrix. Ficin, papain and bromelain (Sigma) were chosen as objects of study. An acid-soluble chitosan (350 kDa, Bioprogress CJSC) was used as an immobilization carrier. The concentration range of glutaraldehyde (crosslinking agent) ranged from 1 to 25%. Suitable concentrations of glutaraldehyde for covalent immobilization were identified by the optimal ratio of protein content (mg per g of carrier), total activity (in units per ml of solution) and specific activity (in units per mg of protein). It was shown that for covalent immobilization of ficin and bromelain on a chitosan matrix, it is most promising to use 10% glutaraldehyde. For immobilization of papain on chitosan by covalent means, the concentration of glutaraldehyde equal to 20% is optimal.

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