The Experts below are selected from a list of 270 Experts worldwide ranked by ideXlab platform
Koichi Chikuni - One of the best experts on this subject based on the ideXlab platform.
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Postmortem Changes in bovine troponin t isoforms on two dimensional electrophoretic gel analyzed using mass spectrometry and western blotting the limited fragmentation into basic polypeptides
Meat Science, 2007Co-Authors: Susumu Muroya, Ikuyo Nakajima, Mayumi Ohnishikameyama, Koichi ChikuniAbstract:To comprehend Postmortem Changes in troponin T (TnT), whole beef proteins were developed on a two-dimensional electrophoretic gel. Multiple TnT-related spots were identified by both western blotting and MALDI-TOF MS utilizing bovine TnT isoform mRNA sequences. More than 10 TnT fast-type isoform spots (pI 5.7-9.6<) and the two slow-type isoform spots (pI 5.6-5.7) were observed at slaughter. All the isoforms were degraded exclusively into basic spots (pI 9.6<) at day 14 Postmortem. Some TnT-related phosphorylated spots present at slaughter had disappeared by day 14, suggesting that the phosphorylated N-terminal region was cut off during beef aging. The intact isoforms and the fragments were identified by the MS with sequence coverage of 20.8-62.7%, and two of the fragments included the cutting site peptide of a conventional 30kDa or of a slow TnT-derived fragment. These results revealed that all of the TnT isoforms are cut exclusively in the glutamic acid-rich amino-terminal region during Postmortem aging.
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Postmortem Changes in bovine troponin T isoforms on two-dimensional electrophoretic gel analyzed using mass spectrometry and western blotting: The limited fragmentation into basic polypeptides.
Meat science, 2006Co-Authors: Susumu Muroya, Mayumi Ohnishi-kameyama, Ikuyo Nakajima, Koichi ChikuniAbstract:To comprehend Postmortem Changes in troponin T (TnT), whole beef proteins were developed on a two-dimensional electrophoretic gel. Multiple TnT-related spots were identified by both western blotting and MALDI-TOF MS utilizing bovine TnT isoform mRNA sequences. More than 10 TnT fast-type isoform spots (pI 5.7-9.6
Susumu Muroya - One of the best experts on this subject based on the ideXlab platform.
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Postmortem Changes in bovine troponin t isoforms on two dimensional electrophoretic gel analyzed using mass spectrometry and western blotting the limited fragmentation into basic polypeptides
Meat Science, 2007Co-Authors: Susumu Muroya, Ikuyo Nakajima, Mayumi Ohnishikameyama, Koichi ChikuniAbstract:To comprehend Postmortem Changes in troponin T (TnT), whole beef proteins were developed on a two-dimensional electrophoretic gel. Multiple TnT-related spots were identified by both western blotting and MALDI-TOF MS utilizing bovine TnT isoform mRNA sequences. More than 10 TnT fast-type isoform spots (pI 5.7-9.6<) and the two slow-type isoform spots (pI 5.6-5.7) were observed at slaughter. All the isoforms were degraded exclusively into basic spots (pI 9.6<) at day 14 Postmortem. Some TnT-related phosphorylated spots present at slaughter had disappeared by day 14, suggesting that the phosphorylated N-terminal region was cut off during beef aging. The intact isoforms and the fragments were identified by the MS with sequence coverage of 20.8-62.7%, and two of the fragments included the cutting site peptide of a conventional 30kDa or of a slow TnT-derived fragment. These results revealed that all of the TnT isoforms are cut exclusively in the glutamic acid-rich amino-terminal region during Postmortem aging.
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Postmortem Changes in bovine troponin T isoforms on two-dimensional electrophoretic gel analyzed using mass spectrometry and western blotting: The limited fragmentation into basic polypeptides.
Meat science, 2006Co-Authors: Susumu Muroya, Mayumi Ohnishi-kameyama, Ikuyo Nakajima, Koichi ChikuniAbstract:To comprehend Postmortem Changes in troponin T (TnT), whole beef proteins were developed on a two-dimensional electrophoretic gel. Multiple TnT-related spots were identified by both western blotting and MALDI-TOF MS utilizing bovine TnT isoform mRNA sequences. More than 10 TnT fast-type isoform spots (pI 5.7-9.6
Gert Lubec - One of the best experts on this subject based on the ideXlab platform.
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Postmortem Changes in the Level of Brain Proteins
Experimental neurology, 2001Co-Authors: Michael Fountoulakis, Rosmarie Hardmeier, Harald Höger, Gert LubecAbstract:Abstract A systematic study on Postmortem Changes of brain proteins has not been performed so far and information is limited to basic principles of specific or nonspecific proteolysis or proteolysis of individual proteins. We studied protein level alterations in rat brain of animals kept at 23°C for several Postmortem times up to 72 h. Brain tissue protein extracts were analyzed by two-dimensional electrophoresis and the proteins with different levels were identified by matrix-assisted laser desorption ionization mass spectrometry. The Changes observed mainly concerned structural proteins and enzymes. The levels of dihydropyrimidinase-related protein-2 decreased within 6 h and two new spots were detected representing shorter forms of the protein. Most of the other alterations appeared about 48 h Postmortem. The most significant were reduced levels of neurofilament, α-internexin, synaptosomal-associated protein 25, glial fibrillary acidic protein, heat shock proteins, and dynamin-1; increased levels of 14-3-3 proteins and spectrin; and generation of shorter forms of certain proteins, such as tubulins, actin, and serum albumin. The results may be useful in neuropathology and brain protein studies.
Chaisiri Wongkham - One of the best experts on this subject based on the ideXlab platform.
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serial analyses of Postmortem Changes in human skeletal muscle a case study of alterations in proteome profile histology electrolyte contents water composition and enzyme activity
Proteomics Clinical Applications, 2008Co-Authors: Ratree Tavichakorntrakool, Vitoon Prasongwattana, Pote Sriboonlue, Anucha Puapairoj, Jongruk Pongskul, Narong Khuntikeo, Wattana Hanpanich, Pathai Yenchitsomanus, Chaisiri WongkhamAbstract:Postmortem tissues are frequently used in forensic investigation, clinical studies, and biomedical research. It is well known that the shorter period from death to analyses provides the more accurate results. However, the longest Postmortem interval that still provides the reliable data remains unclear. We performed serial analyses of Postmortem Changes in proteome profile, histology, electrolyte contents, water composition, and enzyme activity in human vastus lateralis muscle from a male cadaver (died from a motorcycle accident). This uninjured muscle was sectioned into several 1-cm(3 ) cubes and stored in individual closed tubes at 4 or 25°C for 0, 2, 4, 6, 12, 24 or 48 h prior to proteomic, histological, chemical and biochemical analyses. At 4°C, the 2-DE proteome profile remained unchanged until 24 h, when some poorly focused protein spots and significant decrease in the total number of visualized spots were observed. These Changes were detectable earlier (12 h) in the samples stored at 25°C. Profound vacuolization and autolysis started at 24 and 6 h for the samples stored at 4oC and 25°C, respectively. K and Mg contents began to increase at 12 and 48 h, respectively, for both temperatures. However, the increase in Na and Ca contents began at 24 h in the samples stored at 4°C, but started earlier (12 h) in those stored at 25°C. Water content started to decline at 48 and 24 h in the samples stored at 4 and 25°C, respectively. Muscle lactate dehydrogenase activity began to be out of range at 12 h for both temperatures. These findings demonstrate that storing the samples at 4°C could delay some of the aforementioned Changes, which occurred more rapidly at 25°C. Our results also suggest that muscle proteome profile, histology, electrolyte contents, water composition, and enzyme activity should be analyzed within the optimal Postmortem intervals, which vary among individual analyses, to obtain the most reliable data.
Pathai Yenchitsomanus - One of the best experts on this subject based on the ideXlab platform.
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serial analyses of Postmortem Changes in human skeletal muscle a case study of alterations in proteome profile histology electrolyte contents water composition and enzyme activity
Proteomics Clinical Applications, 2008Co-Authors: Ratree Tavichakorntrakool, Vitoon Prasongwattana, Pote Sriboonlue, Anucha Puapairoj, Jongruk Pongskul, Narong Khuntikeo, Wattana Hanpanich, Pathai Yenchitsomanus, Chaisiri WongkhamAbstract:Postmortem tissues are frequently used in forensic investigation, clinical studies, and biomedical research. It is well known that the shorter period from death to analyses provides the more accurate results. However, the longest Postmortem interval that still provides the reliable data remains unclear. We performed serial analyses of Postmortem Changes in proteome profile, histology, electrolyte contents, water composition, and enzyme activity in human vastus lateralis muscle from a male cadaver (died from a motorcycle accident). This uninjured muscle was sectioned into several 1-cm(3 ) cubes and stored in individual closed tubes at 4 or 25°C for 0, 2, 4, 6, 12, 24 or 48 h prior to proteomic, histological, chemical and biochemical analyses. At 4°C, the 2-DE proteome profile remained unchanged until 24 h, when some poorly focused protein spots and significant decrease in the total number of visualized spots were observed. These Changes were detectable earlier (12 h) in the samples stored at 25°C. Profound vacuolization and autolysis started at 24 and 6 h for the samples stored at 4oC and 25°C, respectively. K and Mg contents began to increase at 12 and 48 h, respectively, for both temperatures. However, the increase in Na and Ca contents began at 24 h in the samples stored at 4°C, but started earlier (12 h) in those stored at 25°C. Water content started to decline at 48 and 24 h in the samples stored at 4 and 25°C, respectively. Muscle lactate dehydrogenase activity began to be out of range at 12 h for both temperatures. These findings demonstrate that storing the samples at 4°C could delay some of the aforementioned Changes, which occurred more rapidly at 25°C. Our results also suggest that muscle proteome profile, histology, electrolyte contents, water composition, and enzyme activity should be analyzed within the optimal Postmortem intervals, which vary among individual analyses, to obtain the most reliable data.