Myoglobin and hemoglobin rotational diffusion in the cell
The detection of the 1H NMR signal of myoglobin (Mb) in tissue opens an opportunity to examine its cellular diffusion property, which is central to its purported role in facilitating oxygen transport. In perfused myocardium the field-dependent transverse relaxation analysis of the deoxy Mb proximal...
Gespeichert in:
| Veröffentlicht in: | Biophysical journal 1997-11, Vol.73 (5), p.2764-2770 |
|---|---|
| Hauptverfasser: | , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 2770 |
|---|---|
| container_issue | 5 |
| container_start_page | 2764 |
| container_title | Biophysical journal |
| container_volume | 73 |
| creator | Wang, D. Kreutzer, U. Chung, Y. Jue, T. |
| description | The detection of the 1H NMR signal of myoglobin (Mb) in tissue opens an opportunity to examine its cellular diffusion property, which is central to its purported role in facilitating oxygen transport. In perfused myocardium the field-dependent transverse relaxation analysis of the deoxy Mb proximal histidyl NdeltaH indicates that the Mb rotational correlation time in the cell is only approximately 1.4 times longer than it is in solution. Such a mobility is consistent with the theory that Mb facilitates oxygen diffusion from the sarcoplasm to the mitochondria. The microviscosities of the erythrocyte and myocyte environment are different. The hemoglobin (Hb) rotational correlation time is 2.2 longer in the cell than in solution. Because both the overlapping Hb and Mb signals are visible in vivo, a relaxation-based NMR strategy has been developed to discriminate between them. |
| doi_str_mv | 10.1016/S0006-3495(97)78305-X |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_1181178</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S000634959778305X</els_id><sourcerecordid>79427314</sourcerecordid><originalsourceid>FETCH-LOGICAL-c462t-7d7d1307d43064a688652bf30b358ef62355e56cc5a916f106f8d245fc2323a23</originalsourceid><addsrcrecordid>eNqFkEtLAzEUhYMotVZ_gjAr0cXozXtmo4j4AsWFCt2FNA8bmU40mQr-e6e2Fl25SnLPuefefAjtYzjGgMXJIwCIkrKaH9bySFYUeDneQEPMGSkBKrGJhmvLNtrJ-RUAEw54gAY1lcAkDFF9_xlfmjgJbaFbW0zd7OeZYqe7EFvdFDZ4P8_9vejr3dQVxjXNLtryuslub3WO0PPV5dPFTXn3cH17cX5XGiZIV0orLaYgLaMgmBZVJTiZeAoTyivnBaGcOy6M4brGwmMQvrKEcW8IJVQTOkKny9y3-WTmrHFtl3Sj3lKY6fSpog7qr9KGqXqJHwrjCuOeywgdrAJSfJ-73KlZyIsf6NbFeVayZkRSzHojXxpNijkn59dDMKgFc_XNXC2Aqlqqb-Zq3Pft_95w3bWC3OtnS931mD6CSyqb4FrjbEjOdMrG8M-EL1eckWE</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>79427314</pqid></control><display><type>article</type><title>Myoglobin and hemoglobin rotational diffusion in the cell</title><source>MEDLINE</source><source>Elsevier ScienceDirect Journals Complete</source><source>Cell Press Free Archives</source><source>Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals</source><source>PubMed Central</source><creator>Wang, D. ; Kreutzer, U. ; Chung, Y. ; Jue, T.</creator><creatorcontrib>Wang, D. ; Kreutzer, U. ; Chung, Y. ; Jue, T.</creatorcontrib><description>The detection of the 1H NMR signal of myoglobin (Mb) in tissue opens an opportunity to examine its cellular diffusion property, which is central to its purported role in facilitating oxygen transport. In perfused myocardium the field-dependent transverse relaxation analysis of the deoxy Mb proximal histidyl NdeltaH indicates that the Mb rotational correlation time in the cell is only approximately 1.4 times longer than it is in solution. Such a mobility is consistent with the theory that Mb facilitates oxygen diffusion from the sarcoplasm to the mitochondria. The microviscosities of the erythrocyte and myocyte environment are different. The hemoglobin (Hb) rotational correlation time is 2.2 longer in the cell than in solution. Because both the overlapping Hb and Mb signals are visible in vivo, a relaxation-based NMR strategy has been developed to discriminate between them.</description><identifier>ISSN: 0006-3495</identifier><identifier>EISSN: 1542-0086</identifier><identifier>DOI: 10.1016/S0006-3495(97)78305-X</identifier><identifier>PMID: 9370470</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Animals ; Diffusion ; Erythrocytes - chemistry ; Erythrocytes - metabolism ; Hemoglobins - analysis ; Hemoglobins - chemistry ; Hemoglobins - metabolism ; Histidine - chemistry ; Histidine - metabolism ; Horses ; Humans ; Myocardium - chemistry ; Myocardium - metabolism ; Myoglobin - analysis ; Myoglobin - chemistry ; Myoglobin - metabolism ; Nuclear Magnetic Resonance, Biomolecular ; Oxygen - metabolism ; Viscosity</subject><ispartof>Biophysical journal, 1997-11, Vol.73 (5), p.2764-2770</ispartof><rights>1997 The Biophysical Society</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c462t-7d7d1307d43064a688652bf30b358ef62355e56cc5a916f106f8d245fc2323a23</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1181178/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://dx.doi.org/10.1016/S0006-3495(97)78305-X$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,885,3550,27924,27925,45995,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9370470$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Wang, D.</creatorcontrib><creatorcontrib>Kreutzer, U.</creatorcontrib><creatorcontrib>Chung, Y.</creatorcontrib><creatorcontrib>Jue, T.</creatorcontrib><title>Myoglobin and hemoglobin rotational diffusion in the cell</title><title>Biophysical journal</title><addtitle>Biophys J</addtitle><description>The detection of the 1H NMR signal of myoglobin (Mb) in tissue opens an opportunity to examine its cellular diffusion property, which is central to its purported role in facilitating oxygen transport. In perfused myocardium the field-dependent transverse relaxation analysis of the deoxy Mb proximal histidyl NdeltaH indicates that the Mb rotational correlation time in the cell is only approximately 1.4 times longer than it is in solution. Such a mobility is consistent with the theory that Mb facilitates oxygen diffusion from the sarcoplasm to the mitochondria. The microviscosities of the erythrocyte and myocyte environment are different. The hemoglobin (Hb) rotational correlation time is 2.2 longer in the cell than in solution. Because both the overlapping Hb and Mb signals are visible in vivo, a relaxation-based NMR strategy has been developed to discriminate between them.</description><subject>Animals</subject><subject>Diffusion</subject><subject>Erythrocytes - chemistry</subject><subject>Erythrocytes - metabolism</subject><subject>Hemoglobins - analysis</subject><subject>Hemoglobins - chemistry</subject><subject>Hemoglobins - metabolism</subject><subject>Histidine - chemistry</subject><subject>Histidine - metabolism</subject><subject>Horses</subject><subject>Humans</subject><subject>Myocardium - chemistry</subject><subject>Myocardium - metabolism</subject><subject>Myoglobin - analysis</subject><subject>Myoglobin - chemistry</subject><subject>Myoglobin - metabolism</subject><subject>Nuclear Magnetic Resonance, Biomolecular</subject><subject>Oxygen - metabolism</subject><subject>Viscosity</subject><issn>0006-3495</issn><issn>1542-0086</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1997</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkEtLAzEUhYMotVZ_gjAr0cXozXtmo4j4AsWFCt2FNA8bmU40mQr-e6e2Fl25SnLPuefefAjtYzjGgMXJIwCIkrKaH9bySFYUeDneQEPMGSkBKrGJhmvLNtrJ-RUAEw54gAY1lcAkDFF9_xlfmjgJbaFbW0zd7OeZYqe7EFvdFDZ4P8_9vejr3dQVxjXNLtryuslub3WO0PPV5dPFTXn3cH17cX5XGiZIV0orLaYgLaMgmBZVJTiZeAoTyivnBaGcOy6M4brGwmMQvrKEcW8IJVQTOkKny9y3-WTmrHFtl3Sj3lKY6fSpog7qr9KGqXqJHwrjCuOeywgdrAJSfJ-73KlZyIsf6NbFeVayZkRSzHojXxpNijkn59dDMKgFc_XNXC2Aqlqqb-Zq3Pft_95w3bWC3OtnS931mD6CSyqb4FrjbEjOdMrG8M-EL1eckWE</recordid><startdate>19971101</startdate><enddate>19971101</enddate><creator>Wang, D.</creator><creator>Kreutzer, U.</creator><creator>Chung, Y.</creator><creator>Jue, T.</creator><general>Elsevier Inc</general><scope>6I.</scope><scope>AAFTH</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19971101</creationdate><title>Myoglobin and hemoglobin rotational diffusion in the cell</title><author>Wang, D. ; Kreutzer, U. ; Chung, Y. ; Jue, T.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c462t-7d7d1307d43064a688652bf30b358ef62355e56cc5a916f106f8d245fc2323a23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1997</creationdate><topic>Animals</topic><topic>Diffusion</topic><topic>Erythrocytes - chemistry</topic><topic>Erythrocytes - metabolism</topic><topic>Hemoglobins - analysis</topic><topic>Hemoglobins - chemistry</topic><topic>Hemoglobins - metabolism</topic><topic>Histidine - chemistry</topic><topic>Histidine - metabolism</topic><topic>Horses</topic><topic>Humans</topic><topic>Myocardium - chemistry</topic><topic>Myocardium - metabolism</topic><topic>Myoglobin - analysis</topic><topic>Myoglobin - chemistry</topic><topic>Myoglobin - metabolism</topic><topic>Nuclear Magnetic Resonance, Biomolecular</topic><topic>Oxygen - metabolism</topic><topic>Viscosity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wang, D.</creatorcontrib><creatorcontrib>Kreutzer, U.</creatorcontrib><creatorcontrib>Chung, Y.</creatorcontrib><creatorcontrib>Jue, T.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Biophysical journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wang, D.</au><au>Kreutzer, U.</au><au>Chung, Y.</au><au>Jue, T.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Myoglobin and hemoglobin rotational diffusion in the cell</atitle><jtitle>Biophysical journal</jtitle><addtitle>Biophys J</addtitle><date>1997-11-01</date><risdate>1997</risdate><volume>73</volume><issue>5</issue><spage>2764</spage><epage>2770</epage><pages>2764-2770</pages><issn>0006-3495</issn><eissn>1542-0086</eissn><abstract>The detection of the 1H NMR signal of myoglobin (Mb) in tissue opens an opportunity to examine its cellular diffusion property, which is central to its purported role in facilitating oxygen transport. In perfused myocardium the field-dependent transverse relaxation analysis of the deoxy Mb proximal histidyl NdeltaH indicates that the Mb rotational correlation time in the cell is only approximately 1.4 times longer than it is in solution. Such a mobility is consistent with the theory that Mb facilitates oxygen diffusion from the sarcoplasm to the mitochondria. The microviscosities of the erythrocyte and myocyte environment are different. The hemoglobin (Hb) rotational correlation time is 2.2 longer in the cell than in solution. Because both the overlapping Hb and Mb signals are visible in vivo, a relaxation-based NMR strategy has been developed to discriminate between them.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>9370470</pmid><doi>10.1016/S0006-3495(97)78305-X</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0006-3495 |
| ispartof | Biophysical journal, 1997-11, Vol.73 (5), p.2764-2770 |
| issn | 0006-3495 1542-0086 |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_1181178 |
| source | MEDLINE; Elsevier ScienceDirect Journals Complete; Cell Press Free Archives; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central |
| subjects | Animals Diffusion Erythrocytes - chemistry Erythrocytes - metabolism Hemoglobins - analysis Hemoglobins - chemistry Hemoglobins - metabolism Histidine - chemistry Histidine - metabolism Horses Humans Myocardium - chemistry Myocardium - metabolism Myoglobin - analysis Myoglobin - chemistry Myoglobin - metabolism Nuclear Magnetic Resonance, Biomolecular Oxygen - metabolism Viscosity |
| title | Myoglobin and hemoglobin rotational diffusion in the cell |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-04T02%3A46%3A55IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Myoglobin%20and%20hemoglobin%20rotational%20diffusion%20in%20the%20cell&rft.jtitle=Biophysical%20journal&rft.au=Wang,%20D.&rft.date=1997-11-01&rft.volume=73&rft.issue=5&rft.spage=2764&rft.epage=2770&rft.pages=2764-2770&rft.issn=0006-3495&rft.eissn=1542-0086&rft_id=info:doi/10.1016/S0006-3495(97)78305-X&rft_dat=%3Cproquest_pubme%3E79427314%3C/proquest_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=79427314&rft_id=info:pmid/9370470&rft_els_id=S000634959778305X&rfr_iscdi=true |