894 research outputs found

    The Effect of Repeated Recycling at Different Levels of Addition (Virgin and Recycled Fiber) on the Surface Characteristic of Paper Before and After Calendering

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    Extensive work has been done on the physical properties of paper with recycling, however not much has been researched on the surface properties of paper. This thesis was intended to give more information on this fairly untouched area. An extra dimension was added with the inclusion of virgin fibers. Two loops were designed, one using the conventional 100% recycled fibers and the other, with an addition of virgin pulp. 100% never dried kraft hardwood, refined at 300 CSF, was used. All handsheets were made on the Nobel and Wood handsheet-maker and repeated reslushing was performed on the British Disintegrator. No additives, fillers, or sizing agents were used at any point, thus, recycling was only subjected to: slushing, sheet making, wet-pressing and drying. Calendering was also performed. The principal effect of recycling was the loss of the fiber bonding ability, noticeably in the first recycle for opacity and porosity (100% recycle). The addition of virgin fibers was interestingly seen to improve the brightness with recycling. This phenomena (an increase in brightness with the addition of virgin fibers in comparison to the original brightness) has to be further investigated. Calendering with its compacting and polishing action, decreased the opacity and increased the smoothness. Roughness and gloss did not show a significant change with recycling but with calendering a more smoother and glossier sheet was obtained, as expected

    Truncation of the Mrp20 Protein Reveals New Ribosome‐assembly Subcomplex in Mitochondria

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    Mitochondrial ribosomal protein 20 (Mrp20) is a component of the yeast mitochondrial large (54S) ribosomal subunit and is homologous to the bacterial L23 protein, located at the ribosomal tunnel exit site. The carboxy‐terminal mitochondrial‐specific domain of Mrp20 was found to have a crucial role in the assembly of the ribosomes. A new, membrane‐bound, ribosomal‐assembly subcomplex composed of known tunnel‐exit‐site proteins, an uncharacterized ribosomal protein, MrpL25, and the mitochondrial peroxiredoxin (Prx), Prx1, accumulates in an mrp20ΔC yeast mutant. Finally, data supporting the idea that the inner mitochondrial membrane acts as a platform for the ribosome assembly process are discussed

    Mapping of the saccharomyces cerevisiae oxa1-mitochondrial ribosome interface and identification of MrpL40, a ribosomal protein in close proximity to oxal and critical for oxidative phosphorylation complex assembly

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    The Oxa1 protein plays a central role in facilitating the cotranslational insertion of the nascent polypeptide chains into the mitochondrial inner membrane. Mitochondrially encoded proteins are synthesized on matrix-localized ribosomes which are tethered to the inner membrane and in physical association with the Oxa1 protein. In the present study we used a chemical cross-linking approach to map the Saccharomyces cerevisiae Oxa1-ribosome interface, and we demonstrate here a close association of Oxa1 and the large ribosomal subunit protein, MrpL40. Evidence to indicate that a close physical and functional relationship exists between MrpL40 and another large ribosomal protein, the Mrp20/L23 protein, is also provided. MrpL40 shares sequence features with the bacterial ribosomal protein L24, which like Mrp20/L23 is known to be located adjacent to the ribosomal polypeptide exit site. We propose therefore that MrpL40 represents the Saccharomyces cerevisiae L24 homolog. MrpL40, like many mitochondrial ribosomal proteins, contains a C-terminal extension region that bears no similarity to the bacterial counterpart. We show that this C-terminal mitochondria-specific region is important for MrpL40's ability to support the synthesis of the correct complement of mitochondrially encoded proteins and their subsequent assembly into oxidative phosphorylation complexes

    Mapping of the \u3cem\u3eSaccharomyces cerevisiae\u3c/em\u3e Oxa1-Mitochondrial Ribosome Interface and Identification of MrpL40, a Ribosomal Protein in Close Proximity to Oxa1 and Critical for Oxidative Phosphorylation Complex Assembly

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    The Oxa1 protein plays a central role in facilitating the cotranslational insertion of the nascent polypeptide chains into the mitochondrial inner membrane. Mitochondrially encoded proteins are synthesized on matrix-localized ribosomes which are tethered to the inner membrane and in physical association with the Oxa1 protein. In the present study we used a chemical cross-linking approach to map the Saccharomyces cerevisiae Oxa1-ribosome interface, and we demonstrate here a close association of Oxa1 and the large ribosomal subunit protein, MrpL40. Evidence to indicate that a close physical and functional relationship exists between MrpL40 and another large ribosomal protein, the Mrp20/L23 protein, is also provided. MrpL40 shares sequence features with the bacterial ribosomal protein L24, which like Mrp20/L23 is known to be located adjacent to the ribosomal polypeptide exit site. We propose therefore that MrpL40 represents the Saccharomyces cerevisiae L24 homolog. MrpL40, like many mitochondrial ribosomal proteins, contains a C-terminal extension region that bears no similarity to the bacterial counterpart. We show that this C-terminal mitochondria-specific region is important for MrpL40\u27s ability to support the synthesis of the correct complement of mitochondrially encoded proteins and their subsequent assembly into oxidative phosphorylation complexes

    Stepwise Approach to Myopathy in Systemic Disease

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    Muscle diseases can constitute a large variety of both acquired and hereditary disorders. Myopathies in systemic disease results from several different disease processes including endocrine, inflammatory, paraneoplastic, infectious, drug- and toxin-induced, critical illness myopathy, metabolic, and myopathies with other systemic disorders. Patients with systemic myopathies often present acutely or sub acutely. On the other hand, familial myopathies or dystrophies generally present in a chronic fashion with exceptions of metabolic myopathies where symptoms on occasion can be precipitated acutely. Most of the inflammatory myopathies can have a chance association with malignant lesions; the incidence appears to be specifically increased only in patients with dermatomyositis. In dealing with myopathies associated with systemic illnesses, the focus will be on the acquired causes. Management is beyond the scope of this chapter. Prognosis is based upon the underlying cause and, most of the time, carries a good prognosis. In order to approach a patient with suspected myopathy from systemic disease, a stepwise approach is utilized

    Mrpl35, A Mitospecific Component of Mitoribosomes, Plays A Key Role in Cytochrome \u3cem\u3eC\u3c/em\u3e Oxidase Assembly

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    Mitoribosomes perform the synthesis of the core components of the oxidative phosphorylation (OXPHOS) system encoded by the mitochondrial genome. We provide evidence that MrpL35 (mL38), a mitospecific component of the yeast mitoribosomal central protuberance, assembles into a subcomplex with MrpL7 (uL5), Mrp7 (bL27), and MrpL36 (bL31) and mitospecific proteins MrpL17 (mL46) and MrpL28 (mL40). We isolated respiratory defective mrpL35 mutant yeast strains, which do not display an overall inhibition in mitochondrial protein synthesis but rather have a problem in cytochrome coxidase complex (COX) assembly. Our findings indicate that MrpL35, with its partner Mrp7, play a key role in coordinating the synthesis of the Cox1 subunit with its assembly into the COX enzyme and in a manner that involves the Cox14 and Coa3 proteins. We propose that MrpL35 and Mrp7 are regulatory subunits of the mitoribosome acting to coordinate protein synthesis and OXPHOS assembly events and thus the bioenergetic capacity of the mitochondria

    The Mitospecific Region of Mrp20 and its Importance for the Assembly of Mitochondrial Ribosomes in Saccharomyces cerevisiae

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    Yeast mitochondrial ribosomes are composed of an rRNA scaffold, encoded by the mitochondrial genome and many different proteins, which, with the exception of one, are encoded by nuclear genes. These ribosomal proteins are imported into the mitochondrial matrix following their synthesis in the cytosol, however, little is known about the subsequent events which result in an assembled, translationally-competent ribosome. Many of the mitochondrial ribosomal proteins bear homology to bacterial ancestors. In addition to the acquisition of mitochondrial targeting signals, a number of these nuclearly-encoded ribosomal proteins have acquired additional domains, often at their C-termini, which are termed mitochondrial-specific domains . The function(s) of these domains is currently unknown and it is postulated that they may be involved in the process of ribosomal assembly or for ensuring the targeting of the ribosome to the mitochondrial inner membrane where they are translationally-active. Mrp20 protein is a nuclearly-encoded component of the mitochondrial large ribosomal subunit and shares homology with bacterial ribosomal protein L23, a protein located at the exit site of the ribosomal polypeptide tunnel. Mrp20 contains a C-terminal mitochondrial-specific domain of unknown function. In this study, we demonstrate that the C-terminal mitochondrial-specific region of Mrp20 is important to support the assembly of active mitochondrial ribosomes. It is proposed that the proteins at the exit site such as Mrp20 and MrpL40 are important for the assembly of mitochondrial ribosomes. Furthermore, the data presented here indicates that in the absence of the C-terminal region of the Mrp20 protein, the process of assembly of the ribosome becomes stalled, and the accumulation of a novel ribosome intermediate complex is observed. The characterization of this novel intermediate, which furthers our understanding of the assembly process of ribosomes in mitochondria, is presented

    ACTIVITY STUDY OF CU BASED CATALYTIC MATRIXES WITH ZNO AND/OR ZRO2 FOR ENHANCEMENT OF CATALYST ACTIVE LIFETIME AND METHANOL YIELD

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    A series of Cu/ZnO/Al2O3, Cu/ZnO/ZrO2/Al2O3 and Cu/ZrO2/Al2O3 catalysts were prepared for methanol synthesis study in Lurgi process. Apart from Cu and Al2O3, these catalysts would contain ZnO and/or ZrO2 as active Carbon monoxide (CO) hydrogenation sites. The preparation method was an alternative acid-alkali pH precipitation. The SEM-EDX data for the formulations with various atomic ratios showed high homogeneity, hence good intermixing of ingredients. TPR analysis was done on all prepared matrixes and industrial catalyst and showed the reduction temperature of 300 oC to 345 oC for all 3 types of catalysts prepared. Both Low and High Temperature peak obtained for Metal Surface Area (MSA) analysis showed that there is a general decreasing H2 adsorption trend with the increasing amount of Zirconia in the catalyst. Prepared catalyst sample A with no zirconia present showed highest low and High Temperature adsorption in comparison with commercial and prepared catalysts. This suggests that Cu-ZnO catalyst have higher activity as compared to Cu-Zirconia based catalysts. TGA analysis also reveals that prepared catalysts sample has higher thermal stability at Lurgi Operating Temperature of 250oC compared to Industrial catalysts sample. CO conversion study reveals that sample A with no Zr present has highest conversion of up to 4%. Also determined was that Zn offers higher activity in CO hydrogenation process in catalyst samples compared to Zr when present in the same atomic %. Also monoclinic Zr phase formed in catalyst type Cu/ZnO/ZrO2/Al2O3 gives higher MeOH Yield compared to catalyst sample where tetragonal Zr phase is formed. A consistent trend between CH4 formation during activity study and Carbon formation study by CHNS reveals the most likely route for Carbon formation was through CH4 decomposition to form Carbon on catalysts surface sample The analytical kinetic study conducted decided that coverage of O atoms should be 0.5 in the beginning of the reaction in order to maximize the initial rate of reaction.
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