{"response":{"docs":[{"system_create_dtsi":"2017-10-27T02:52:14Z","system_modified_dtsi":"2018-08-01T18:40:10Z","has_model_ssim":["Article"],"id":"bc3870915","accessControl_ssim":["6e921eb2-b145-449c-9688-1a9eeb96b36a"],"hasRelatedMediaFragment_ssim":["bc387092f"],"hasRelatedImage_ssim":["bc387092f"],"depositor_ssim":["greiskd@ucmail.uc.edu"],"depositor_tesim":["greiskd@ucmail.uc.edu"],"title_tesim":["Cardiac myosin binding protein-C is a potential diagnostic biomarker for myocardial infarction"],"date_uploaded_dtsi":"2017-03-03T00:00:00Z","date_modified_dtsi":"2017-04-07T00:00:00Z","isPartOf_ssim":["admin_set/default"],"proxy_depositor_ssim":["dungavjk@mail.uc.edu"],"doi_tesim":["10.1016/j.yjmcc.2011.09.011"],"journal_title_tesim":["Journal of Molecular and Cellular Cardiology"],"college_tesim":["Medicine"],"department_tesim":["Cancer \u0026 Cell Biology"],"note_tesim":["This work was part of a pilot \"mediated-deposit model\" where library staff found potential works, later submitted for faculty review"],"creator_tesim":["Muthusamy, Saminathan","Nair, Nandini","McElligott, Andrew","Martin, Jody L.","Govindan, Suresh","Gongora, Enrique","henderson, Kyle K.","Greis, Kenneth D.","Barefield, David","Luther, Pradeep K.","Sadayappan, Sakthivel","Winegrad, Saul"],"subject_tesim":["Cardiology","Cancer Biology"],"language_tesim":["English"],"description_tesim":["Cardiac myosin binding protein-C (cMyBP-C) is a thick filament assembly protein that stabilizes sarcomeric structure and regulates cardiac function; however, the profile of cMyBP-C degradation after myocardial infarction (MI) is unknown. We hypothesized that cMyBP-C is sensitive to proteolysis and is specifically increased in the bloodstream post-MI in rats and humans. Under these circumstances, elevated levels of degraded cMyBP-C could be used as a diagnostic tool to confirm MI. To test this hypothesis, we first established that cMyBP-C dephosphorylation is directly associated with increased degradation of this myofilament protein, leading to its release in vitro. Using neonatal rat ventricular cardiomyocytes in vitro, we were able to correlate the induction of hypoxic stress with increased cMyBP-C dephosphorylation, degradation, and the specific release of N′-fragments. Next, to define the proteolytic pattern of cMyBP-C post-MI, the left anterior descending coronary artery was ligated in adult male rats. Degradation of cMyBP-C was confirmed by a reduction in total cMyBP-C and the presence of degradation products in the infarct tissue. Phosphorylation levels of cMyBP-C were greatly reduced in ischemic areas of the MI heart compared to non-ischemic regions and sham control hearts. Post-MI plasma samples from these rats, as well as humans, were assayed for cMyBP-C and its fragments by sandwich ELISA and immunoprecipitation analyses. Results showed significantly elevated levels of cMyBP-C in the plasma of all post-MI samples. Overall, this study suggests that cMyBP-C is an easily releasable myofilament protein that is dephosphorylated, degraded and released into the circulation post-MI. The presence of elevated levels of cMyBP-C in the blood provides a promising novel biomarker able to accurately rule in MI, thus aiding in the further assessment of ischemic heart disease."],"license_tesim":["http://rightsstatements.org/vocab/InC/1.0/"],"date_created_tesim":["2012-01"],"source_tesim":["Journal of Molecular and Cellular Cardiology"],"thumbnail_path_ss":"/downloads/bc387092f?file=thumbnail","suppressed_bsi":false,"actionable_workflow_roles_ssim":["admin_set/default-default-depositing"],"workflow_state_name_ssim":["deposited"],"member_ids_ssim":["bc387092f"],"file_set_ids_ssim":["bc387092f"],"visibility_ssi":"open","admin_set_tesim":["Default Admin Set"],"sort_title_ssi":"CARDIAC MYOSIN BINDING PROTEINC IS A POTENTIAL DIAGNOSTIC BIOMARKER FOR MYOCARDIAL INFARCTION","human_readable_type_tesim":["Article"],"read_access_group_ssim":["public"],"read_access_person_ssim":["konecnmc@ucmail.uc.edu"],"edit_access_person_ssim":["greiskd@ucmail.uc.edu"],"nesting_collection__pathnames_ssim":["bc3870915"],"nesting_collection__deepest_nested_depth_isi":1,"_version_":1697114871270735872,"timestamp":"2021-04-15T13:54:24.722Z","score":0.00049999997},{"system_create_dtsi":"2017-10-27T02:52:10Z","system_modified_dtsi":"2018-08-01T18:40:11Z","has_model_ssim":["Article"],"id":"bc3870894","accessControl_ssim":["a26ae815-4a1d-44f2-a752-795d411711dd"],"hasRelatedMediaFragment_ssim":["bc387090w"],"hasRelatedImage_ssim":["bc387090w"],"depositor_ssim":["greiskd@ucmail.uc.edu"],"depositor_tesim":["greiskd@ucmail.uc.edu"],"title_tesim":["Cardiac Metabolic Pathways Affected in the Mouse Model of Barth Syndrome"],"date_uploaded_dtsi":"2017-03-03T00:00:00Z","date_modified_dtsi":"2017-04-07T00:00:00Z","isPartOf_ssim":["admin_set/default"],"proxy_depositor_ssim":["dungavjk@mail.uc.edu"],"doi_tesim":["10.1371/journal.pone.0128561"],"journal_title_tesim":["PLoS ONE"],"college_tesim":["Medicine"],"department_tesim":["Cancer \u0026 Cell Biology"],"note_tesim":["This work was part of a pilot \"mediated-deposit model\" where library staff found potential works, later submitted for faculty review"],"creator_tesim":["Haffey, Wendy D.","Mandala, Satish K.","Purevjav, Enkhsalkhan","Huang, Yan","Javadov, Sabzali","Greis, Kenneth D.","Powers, Corey","Strauss, Arnold W.","Towbin, Jeffrey A.","Khuchua, Zaza"],"subject_tesim":["Cancer Biology"],"language_tesim":["English"],"description_tesim":["Cardiolipin (CL) is a mitochondrial phospholipid essential for electron transport chain (ETC) integrity. CL-deficiency in humans is caused by mutations in the tafazzin (Taz) gene and results in a multisystem pediatric disorder, Barth syndrome (BTHS). It has been reported that tafazzin deficiency destabilizes mitochondrial respiratory chain complexes and affects supercomplex assembly. The aim of this study was to investigate the impact of Taz-knockdown on the mitochondrial proteomic landscape and metabolic processes, such as stability of respiratory chain supercomplexes and their interactions with fatty acid oxidation enzymes in cardiac muscle. Proteomic analysis demonstrated reduction of several polypeptides of the mitochondrial respiratory chain, including Rieske and cytochrome c1 subunits of complex III, NADH dehydrogenase alpha subunit 5 of complex I and the catalytic core-forming subunit of F0F1-ATP synthase. Taz gene knockdown resulted in upregulation of enzymes of folate and amino acid metabolic pathways in heart mitochondria, demonstrating that Tazdeficiency causes substantive metabolic remodeling in cardiac muscle. Mitochondrial respiratory chain supercomplexes are destabilized in CL-depleted mitochondria from Taz knockdown hearts resulting in disruption of the interactions between ETC and the fatty acid oxidation enzymes, very long-chain acyl-CoA dehydrogenase and long-chain 3-hydroxyacylCoA dehydrogenase, potentially affecting the metabolic channeling of reducing equivalents between these two metabolic pathways. Mitochondria-bound myoglobin was significantly reduced in Taz-knockdown hearts, potentially disrupting intracellular oxygen delivery to the oxidative phosphorylation system. Our results identify the critical pathways affected by the Taz-deficiency in mitochondria and establish a future framework for development of therapeutic options for BTHS."],"license_tesim":["http://rightsstatements.org/vocab/InC/1.0/"],"date_created_tesim":["2015-06"],"source_tesim":["PLoS ONE"],"thumbnail_path_ss":"/downloads/bc387090w?file=thumbnail","suppressed_bsi":false,"actionable_workflow_roles_ssim":["admin_set/default-default-depositing"],"workflow_state_name_ssim":["deposited"],"member_ids_ssim":["bc387090w"],"file_set_ids_ssim":["bc387090w"],"visibility_ssi":"open","admin_set_tesim":["Default Admin Set"],"sort_title_ssi":"CARDIAC METABOLIC PATHWAYS AFFECTED IN THE MOUSE MODEL OF BARTH SYNDROME","human_readable_type_tesim":["Article"],"read_access_group_ssim":["public"],"read_access_person_ssim":["konecnmc@ucmail.uc.edu"],"edit_access_person_ssim":["greiskd@ucmail.uc.edu"],"nesting_collection__pathnames_ssim":["bc3870894"],"nesting_collection__deepest_nested_depth_isi":1,"_version_":1697122167359012864,"timestamp":"2021-04-15T15:50:22.814Z","score":0.00049999997},{"system_create_dtsi":"2017-10-27T02:52:05Z","system_modified_dtsi":"2018-08-01T18:40:07Z","has_model_ssim":["Article"],"id":"bc387087k","accessControl_ssim":["5b824e71-18ef-430f-89d9-6ab268c5b92e"],"hasRelatedMediaFragment_ssim":["bc387088v"],"hasRelatedImage_ssim":["bc387088v"],"depositor_ssim":["greiskd@ucmail.uc.edu"],"depositor_tesim":["greiskd@ucmail.uc.edu"],"title_tesim":["Mechanism of insulin sensitization by BMOV (bis maltolato oxo vanadium); unliganded vanadium (VO4) as the active component"],"date_uploaded_dtsi":"2017-03-01T00:00:00Z","date_modified_dtsi":"2017-04-07T00:00:00Z","isPartOf_ssim":["admin_set/default"],"proxy_depositor_ssim":["dungavjk@mail.uc.edu"],"doi_tesim":["10.1016/S0162-0134(03)00236-8"],"journal_title_tesim":["Journal of Inorganic Biochemistry"],"college_tesim":["Medicine"],"department_tesim":["Cancer \u0026 Cell Biology"],"note_tesim":["This work was part of a pilot \"mediated-deposit model\" where library staff found potential works, later submitted for faculty review"],"creator_tesim":["Diven, Conrad","Peters, Kevin G.","Evdokimov, Artem","Howard, Brian W.","Soper, Shari","Genbauffe, Frank","Greis, Kenneth D.","Rastogi, Vinit","Eby-Wilkens, Elaine","Pokross, Matthew","Maier, Matthew"],"subject_tesim":["Biology","Biochemistry"],"language_tesim":["English"],"description_tesim":["Organovanadium compounds have been shown to be insulin sensitizers in vitro and in vivo. One potential biochemical mechanism for insulin sensitization by these compounds is that they inhibit protein tyrosine phosphatases (PTPs) that negatively regulate insulin receptor activation and signaling. In this study, bismaltolato oxovanadium (BMOV), a potent insulin sensitizer, was shown to be a reversible, competitive phosphatase inhibitor that inhibited phosphatase activity in cultured cells and enhanced insulin receptor activation in vivo. NMR and X-ray crystallographic studies of the interaction of BMOV with two different phosphatases, HCPTPA (human low molecular weight cytoplasmic protein tyrosine phosphatase) and PTP1B (protein tyrosine phosphatase 1B), demonstrated uncomplexed vanadium (VO ) in the active site. Taken together, these findings support phosphatase inhibition as a mechanism for insulin sensitization by BMOV 4 and other organovanadium compounds and strongly suggest that uncomplexed vanadium is the active component of these compounds."],"license_tesim":["http://rightsstatements.org/vocab/InC/1.0/"],"date_created_tesim":["2003-09"],"source_tesim":["Journal of Inorganic Biochemistry"],"thumbnail_path_ss":"/downloads/bc387088v?file=thumbnail","suppressed_bsi":false,"actionable_workflow_roles_ssim":["admin_set/default-default-depositing"],"workflow_state_name_ssim":["deposited"],"member_ids_ssim":["bc387088v"],"file_set_ids_ssim":["bc387088v"],"visibility_ssi":"open","admin_set_tesim":["Default Admin Set"],"sort_title_ssi":"MECHANISM OF INSULIN SENSITIZATION BY BMOV BIS MALTOLATO OXO VANADIUM UNLIGANDED VANADIUM VO4 AS THE ACTIVE COMPONENT","human_readable_type_tesim":["Article"],"read_access_group_ssim":["public"],"read_access_person_ssim":["konecnmc@ucmail.uc.edu"],"edit_access_person_ssim":["greiskd@ucmail.uc.edu"],"nesting_collection__pathnames_ssim":["bc387087k"],"nesting_collection__deepest_nested_depth_isi":1,"_version_":1697102503580008448,"timestamp":"2021-04-15T10:37:49.973Z","score":0.00049999997},{"system_create_dtsi":"2017-10-27T02:52:01Z","system_modified_dtsi":"2018-08-01T18:40:10Z","has_model_ssim":["Article"],"id":"bc3870851","accessControl_ssim":["57e582d4-c063-4af3-bfca-dc5c034433bc"],"hasRelatedMediaFragment_ssim":["bc3870869"],"hasRelatedImage_ssim":["bc3870869"],"depositor_ssim":["greiskd@ucmail.uc.edu"],"depositor_tesim":["greiskd@ucmail.uc.edu"],"title_tesim":["Apolipoprotein A-II-mediated Conformational Changes of Apolipoprotein A-I in Discoidal High Density Lipoproteins"],"date_uploaded_dtsi":"2017-03-01T00:00:00Z","date_modified_dtsi":"2017-04-07T00:00:00Z","isPartOf_ssim":["admin_set/default"],"proxy_depositor_ssim":["dungavjk@mail.uc.edu"],"doi_tesim":["DOI 10.1074/jbc.M111.291070"],"journal_title_tesim":["Journal of Biological Chemistry"],"college_tesim":["Medicine"],"department_tesim":["Cancer \u0026 Cell Biology"],"note_tesim":["This work was part of a pilot \"mediated-deposit model\" where library staff found potential works, later submitted for faculty review"],"creator_tesim":["Gauthamadasa, Kekulawalage","Vaitinadin, Nataraja Sarma","Homan, Reyn","Macha, Stephen","Dresman, James L.","D. Silva, R. A. Gangani","Greis, Kenneth D."],"subject_tesim":["Biological Chemistry"],"language_tesim":["English"],"description_tesim":["Background: Role of apolipoprotein (apo) A-II on metabolism of high density lipoproteins (HDLs) is unknown.\n\nResults: Conformational changes of apoA-I, the major apolipoprotein of HDL, caused by apoA-II in discoidal HDL are confined to two regions of apoA-I.\n\nConclusion: Interactions between the two major apolipoproteins in discoidal HDL are site specific.\n\nSignificance: Functional implications of HDL complexes will significantly benefit from such structural information."],"license_tesim":["http://rightsstatements.org/vocab/InC/1.0/"],"date_created_tesim":["2012-03"],"source_tesim":["Journal of Biological Chemistry"],"thumbnail_path_ss":"/downloads/bc3870869?file=thumbnail","suppressed_bsi":false,"actionable_workflow_roles_ssim":["admin_set/default-default-depositing"],"workflow_state_name_ssim":["deposited"],"member_ids_ssim":["bc3870869"],"file_set_ids_ssim":["bc3870869"],"visibility_ssi":"open","admin_set_tesim":["Default Admin Set"],"sort_title_ssi":"APOLIPOPROTEIN AIIMEDIATED CONFORMATIONAL CHANGES OF APOLIPOPROTEIN AI IN DISCOIDAL HIGH DENSITY LIPOPROTEINS","human_readable_type_tesim":["Article"],"read_access_group_ssim":["public"],"read_access_person_ssim":["konecnmc@ucmail.uc.edu"],"edit_access_person_ssim":["greiskd@ucmail.uc.edu"],"nesting_collection__pathnames_ssim":["bc3870851"],"nesting_collection__deepest_nested_depth_isi":1,"_version_":1697097727010144256,"timestamp":"2021-04-15T09:21:54.681Z","score":0.00049999997},{"system_create_dtsi":"2017-10-27T02:51:57Z","system_modified_dtsi":"2018-08-01T18:40:11Z","has_model_ssim":["Article"],"id":"bc387083g","accessControl_ssim":["dcde149e-28a4-44b8-8619-4b9bc785fbde"],"hasRelatedMediaFragment_ssim":["bc387084r"],"hasRelatedImage_ssim":["bc387084r"],"depositor_ssim":["greiskd@ucmail.uc.edu"],"depositor_tesim":["greiskd@ucmail.uc.edu"],"title_tesim":["Refined Structure of the Lipophosphoglycan of Leishmania donovani"],"date_uploaded_dtsi":"2017-03-01T00:00:00Z","date_modified_dtsi":"2017-04-07T00:00:00Z","isPartOf_ssim":["admin_set/default"],"proxy_depositor_ssim":["dungavjk@mail.uc.edu"],"journal_title_tesim":["Journal of Biological Chemistry"],"college_tesim":["Medicine"],"department_tesim":["Cancer \u0026 Cell Biology"],"note_tesim":["This work was part of a pilot \"mediated-deposit model\" where library staff found potential works, later submitted for faculty review"],"creator_tesim":["Ferguson, Michael A. J.","Turco, Salvatore J.","Thomas, Jerry R.","Gorin, Philip A. J.","Homans, Steven W.","McConville, Malcom J.","Greis, Kenneth D.","Thomas-Oates, Jane E."],"subject_tesim":["Biological Chemistry","Biology"],"language_tesim":["English"],"description_tesim":["The primary structure of the major surface glycoconjugate of Leishmania donovani parasites, a lipophosphoglycan, has been further characterized. The repeating PO4-6Galp beta 1-4Man disaccharide units, which are a salient feature of the molecule, are shown to terminate with one of several neutral structures, the most abundant of which is the branched trisaccharide Galp beta 1-4(Manp alpha 1-2)Man. The phosphosaccharide core of lipophosphoglycan, which links the disaccharide repeats to a lipid anchor, contains 2 phosphate residues. One of the core phosphates has previously been localized on O-6 of the galactosyl residue distal to the lipid anchor; the second phosphate is now shown to be on O-6 of the mannosyl residue distal to the anchor and to bear an alpha-linked glucopyranosyl residue. Also, the anomeric configuration of the unusual 3-substituted Galf residue in the phosphosaccharide core is established as beta. The complete structure of the core is thus PO4-6Galp alpha 1-6Galp alpha 1-3Galf beta 1-3[Glcp alpha 1-PO4-6]Manp alpha 1-3Manp alpha 1-4GlcN alpha 1-. This further clarification of the structure of lipophosphoglycan may prove beneficial in determining the structure-function relationships of this highly unusual glycoconjugate."],"license_tesim":["http://rightsstatements.org/vocab/InC/1.0/"],"date_created_tesim":["1992-05"],"source_tesim":["Journal of Biological Chemistry"],"thumbnail_path_ss":"/downloads/bc387084r?file=thumbnail","suppressed_bsi":false,"actionable_workflow_roles_ssim":["admin_set/default-default-depositing"],"workflow_state_name_ssim":["deposited"],"member_ids_ssim":["bc387084r"],"file_set_ids_ssim":["bc387084r"],"visibility_ssi":"open","admin_set_tesim":["Default Admin Set"],"sort_title_ssi":"REFINED STRUCTURE OF THE LIPOPHOSPHOGLYCAN OF LEISHMANIA DONOVANI","human_readable_type_tesim":["Article"],"read_access_group_ssim":["public"],"read_access_person_ssim":["konecnmc@ucmail.uc.edu"],"edit_access_person_ssim":["greiskd@ucmail.uc.edu"],"nesting_collection__pathnames_ssim":["bc387083g"],"nesting_collection__deepest_nested_depth_isi":1,"_version_":1697115499946573824,"timestamp":"2021-04-15T14:04:24.274Z","score":0.00049999997},{"system_create_dtsi":"2017-10-27T02:51:52Z","system_modified_dtsi":"2018-08-01T18:40:09Z","has_model_ssim":["Article"],"id":"bc387081x","accessControl_ssim":["add9072d-1ff4-4d50-a075-c58b872a6fc5"],"hasRelatedMediaFragment_ssim":["bc3870826"],"hasRelatedImage_ssim":["bc3870826"],"depositor_ssim":["greiskd@ucmail.uc.edu"],"depositor_tesim":["greiskd@ucmail.uc.edu"],"title_tesim":["Purification and Characterization an Extracellular Phosphoglycan from Leishmania donovani"],"date_uploaded_dtsi":"2017-03-01T00:00:00Z","date_modified_dtsi":"2017-04-07T00:00:00Z","isPartOf_ssim":["admin_set/default"],"proxy_depositor_ssim":["dungavjk@mail.uc.edu"],"journal_title_tesim":["Journal of Biological Chemistry"],"college_tesim":["Medicine"],"department_tesim":["Cancer \u0026 Cell Biology"],"note_tesim":["This work was part of a pilot \"mediated-deposit model\" where library staff found potential works, later submitted for faculty review"],"creator_tesim":["Turco, Salvatore J.","Thomas, Jerry R.","Homans, Steven W.","Ferguson, Michael A.","McConville, Malcolm J.","Greis, Kenneth D."],"subject_tesim":["Biological Chemistry","Biology"],"language_tesim":["English"],"description_tesim":["An extracellular phosphoglycan (exPG), present in the culturem edium of the promastigote form L oefi shmania donovani, was purified and structurally characterized. The purification scheme included ethanol precipitation of the culture medium, anion exchange chromatography, hydrophobic chromatography on phenyl-Sepharose, and preparative polyacrylamgeild e electrophoresis. Structural analysis by ‘H-’H NMR, methylation linkage analysis, and glycosidase digestion revealed that the exPG consisted of thfoel lowing structure: (CAP)+[P04-6Galp@1-4Manpal]lo-11-POr6GalpB1-4Man. The capw as found to be ones eovf eral small, neutral oligosaccharides, the most abundant of which was the trisaccharide Galp@l-4(Manpal-2)Man. The results indicated structural analogy to the cellular-derived lipophosphoglycan (LPG) from L. donovani. The important exceptions are a lacko f the lipid anchor, the entire phosphosaccharide core, and several of the repeating disaccharide units. Although the function of exPGis presently unknowni,t may play a protective role for the promastigote in the insect vector or during infection of a mammalian host "],"license_tesim":["http://rightsstatements.org/vocab/InC/1.0/"],"date_created_tesim":["1992-04"],"source_tesim":["Journal of Biological Chemistry"],"thumbnail_path_ss":"/downloads/bc3870826?file=thumbnail","suppressed_bsi":false,"actionable_workflow_roles_ssim":["admin_set/default-default-depositing"],"workflow_state_name_ssim":["deposited"],"member_ids_ssim":["bc3870826"],"file_set_ids_ssim":["bc3870826"],"visibility_ssi":"open","admin_set_tesim":["Default Admin Set"],"sort_title_ssi":"PURIFICATION AND CHARACTERIZATION AN EXTRACELLULAR PHOSPHOGLYCAN FROM LEISHMANIA DONOVANI","human_readable_type_tesim":["Article"],"read_access_group_ssim":["public"],"read_access_person_ssim":["konecnmc@ucmail.uc.edu"],"edit_access_person_ssim":["greiskd@ucmail.uc.edu"],"nesting_collection__pathnames_ssim":["bc387081x"],"nesting_collection__deepest_nested_depth_isi":1,"_version_":1697096093120069632,"timestamp":"2021-04-15T08:55:56.482Z","score":0.00049999997},{"system_create_dtsi":"2017-10-27T02:51:48Z","system_modified_dtsi":"2018-08-01T18:40:06Z","has_model_ssim":["Article"],"id":"bc387079w","accessControl_ssim":["256fdb9c-cabe-4e51-b0f9-34f56c617458"],"hasRelatedMediaFragment_ssim":["bc387080n"],"hasRelatedImage_ssim":["bc387080n"],"depositor_ssim":["greiskd@ucmail.uc.edu"],"depositor_tesim":["greiskd@ucmail.uc.edu"],"title_tesim":["An effective skeletal muscle prefractionation method to remove abundant structural proteins for optimized two-dimensional gel electrophoresis"],"date_uploaded_dtsi":"2017-03-01T00:00:00Z","date_modified_dtsi":"2017-04-07T00:00:00Z","isPartOf_ssim":["admin_set/default"],"proxy_depositor_ssim":["dungavjk@mail.uc.edu"],"doi_tesim":["10.1002/elps.200410367"],"journal_title_tesim":["Electrophoresis"],"college_tesim":["Medicine"],"department_tesim":["Cancer \u0026 Cell Biology"],"note_tesim":["This work was part of a pilot \"mediated-deposit model\" where library staff found potential works, later submitted for faculty review"],"creator_tesim":["Wang, Feng","Jarrold, Bradley","Burt, Thomas","DeMuth, Jeffrey","Greis, Kenneth D."],"subject_tesim":["Biology","Electrophoresis"],"language_tesim":["English"],"description_tesim":["Proteomic analysis of biological samples in disease models or therapeutic intervention studies requires the ability to detect and identify biologically relevant proteins present in relatively low concentrations. The detection and analysis of these low-level proteins is hindered by the presence of a few proteins that are expressed in relatively high concentrations. In the case of muscle tissue, highly abundant structural proteins, such as actin, myosin, and tropomyosin, compromise the detection and analysis of more biologically relevant proteins. We have developed a practical protocol which exploits high-pH extraction to reduce or remove abundant structural proteins from skeletal muscle crude membrane preparations in a manner suitable for two dimensional gel electrophoresis. An initial whole-cell muscle lysate is generated by homogenization of powdered tissue in Tris-base. This lysate is subsequently partitioned into a supernatant and pellet containing the majority of structural proteins. Treatment of the pellet with high-pH conditions effectively releases structural proteins from membrane compartments which are then removed through ultracentrifugation. 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