Cerium-based cytochemical method for detection of ouabain-sensitive, potassium-dependent p-nitrophenylphosphatase activity at physiological pH
We have developed a new cytochemical method for detecting the ouabain-sensitive, potassium-dependent p-nitrophenylphosphatase (K-NPPase) activity of the sodium-potassium-activated adenosine triphosphatase (Na-K ATPase) complex. The incubation medium contains p-nitrophenylphosphate (p-NPP) as substra...
Gespeichert in:
| Veröffentlicht in: | The journal of histochemistry and cytochemistry 1987-05, Vol.35 (5), p.601-611 |
|---|---|
| Hauptverfasser: | , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 611 |
|---|---|
| container_issue | 5 |
| container_start_page | 601 |
| container_title | The journal of histochemistry and cytochemistry |
| container_volume | 35 |
| creator | Kobayashi, T Okada, T Seguchi, H |
| description | We have developed a new cytochemical method for detecting the ouabain-sensitive, potassium-dependent p-nitrophenylphosphatase (K-NPPase) activity of the sodium-potassium-activated adenosine triphosphatase (Na-K ATPase) complex. The incubation medium contains p-nitrophenylphosphate (p-NPP) as substrate, cerium chloride as capture agent, Tricine buffer, MgCl2, and KCl. Tricine buffer protected against the medium turbidity caused by non-enzymatic reaction at pH 7.5. Biochemically, the accumulation of p-nitrophenol and phosphate in the reaction precipitate was proportionally related to the enzyme concentration. Ultracytochemically, the reaction products of the K-NPPase activity were localized as fine and uniform electron-dense deposits in the cytoplasmic side of specialized basolateral plasma membranes of cells of kidney distal convoluted tubules, secretory cells of salt gland, and marginal cells of stria vascularis. This method has the advantage of being useful at physiological pH. |
| doi_str_mv | 10.1177/35.5.3031156 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_77445028</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sage_id>10.1177_35.5.3031156</sage_id><sourcerecordid>77445028</sourcerecordid><originalsourceid>FETCH-LOGICAL-c3326-be2d075a03d4a6b19608ff167fdf743e445118f14d2bd7271f1cdc3c7267a75b3</originalsourceid><addsrcrecordid>eNp10MFu1DAQBmALgcpSuHFF8gEqITWLHcdxeqxWhSJV4gJny7HHG1eJHWynq7wEz4zbXZUTJ0szn_7xDELvKdlSKsQXxrd8ywijlLcv0IZyTitOmuYl2hBS11UpNK_Rm5TuCaFNw7szdHbiG_RnB9EtU9WrBAbrNQc9wOS0GvEEeQgG2xCxgQw6u-BxsDgsqlfOVwl8ctk9wCWeQ1YpPeYYmMEb8BnPlXc5hnkAv47zENI8qKIAq5L04PKKVUHDmlwYw_5p4nz7Fr2yakzw7vSeo19fb37ubqu7H9--767vKs1Y3VY91IYIrggzjWp7etWSzlraCmusaBiULSntLG1M3RtRC2qpNpppUbdCCd6zc3RxzJ1j-L1AynJyScM4Kg9hSVKIEkHqrsDLI9QxpBTByjm6ScVVUiIfzy8Zl1ye7ln4h1Pu0k9gnvG__sdTX6WysY3Ka5eeWcfaq6YThX0-sqT2IO_DEn25xv9Gfjrawe2Hg4sg06TGsXyAysPh8GRbQtlf-NGpOw</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>77445028</pqid></control><display><type>article</type><title>Cerium-based cytochemical method for detection of ouabain-sensitive, potassium-dependent p-nitrophenylphosphatase activity at physiological pH</title><source>MEDLINE</source><source>EZB Free E-Journals</source><source>SAGE Journals</source><source>Free Full-Text Journals in Chemistry</source><creator>Kobayashi, T ; Okada, T ; Seguchi, H</creator><creatorcontrib>Kobayashi, T ; Okada, T ; Seguchi, H</creatorcontrib><description>We have developed a new cytochemical method for detecting the ouabain-sensitive, potassium-dependent p-nitrophenylphosphatase (K-NPPase) activity of the sodium-potassium-activated adenosine triphosphatase (Na-K ATPase) complex. The incubation medium contains p-nitrophenylphosphate (p-NPP) as substrate, cerium chloride as capture agent, Tricine buffer, MgCl2, and KCl. Tricine buffer protected against the medium turbidity caused by non-enzymatic reaction at pH 7.5. Biochemically, the accumulation of p-nitrophenol and phosphate in the reaction precipitate was proportionally related to the enzyme concentration. Ultracytochemically, the reaction products of the K-NPPase activity were localized as fine and uniform electron-dense deposits in the cytoplasmic side of specialized basolateral plasma membranes of cells of kidney distal convoluted tubules, secretory cells of salt gland, and marginal cells of stria vascularis. This method has the advantage of being useful at physiological pH.</description><identifier>ISSN: 0022-1554</identifier><identifier>EISSN: 1551-5044</identifier><identifier>DOI: 10.1177/35.5.3031156</identifier><identifier>PMID: 3031156</identifier><identifier>CODEN: JHCYAS</identifier><language>eng</language><publisher>Los Angeles, CA: Histochemical Soc</publisher><subject>4-Nitrophenylphosphatase - metabolism ; Animals ; Biological and medical sciences ; Buffers ; Cell physiology ; Cerium ; Ducks ; Fundamental and applied biological sciences. Psychology ; Guinea Pigs ; Histocytochemistry ; Hydrogen-Ion Concentration ; Kidney Tubules, Distal - enzymology ; Membrane and intracellular transports ; Microscopy, Electron ; Molecular and cellular biology ; Nitrophenols - metabolism ; Organophosphorus Compounds - metabolism ; Ouabain - pharmacology ; Phosphoric Monoester Hydrolases - metabolism ; Potassium - pharmacology ; Rats ; Rats, Inbred Strains ; Salt Gland - enzymology ; Sodium-Potassium-Exchanging ATPase - metabolism ; Stria Vascularis - enzymology</subject><ispartof>The journal of histochemistry and cytochemistry, 1987-05, Vol.35 (5), p.601-611</ispartof><rights>1987 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3326-be2d075a03d4a6b19608ff167fdf743e445118f14d2bd7271f1cdc3c7267a75b3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://journals.sagepub.com/doi/pdf/10.1177/35.5.3031156$$EPDF$$P50$$Gsage$$H</linktopdf><linktohtml>$$Uhttps://journals.sagepub.com/doi/10.1177/35.5.3031156$$EHTML$$P50$$Gsage$$H</linktohtml><link.rule.ids>314,780,784,21819,27924,27925,43621,43622</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=8369487$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/3031156$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kobayashi, T</creatorcontrib><creatorcontrib>Okada, T</creatorcontrib><creatorcontrib>Seguchi, H</creatorcontrib><title>Cerium-based cytochemical method for detection of ouabain-sensitive, potassium-dependent p-nitrophenylphosphatase activity at physiological pH</title><title>The journal of histochemistry and cytochemistry</title><addtitle>J Histochem Cytochem</addtitle><description>We have developed a new cytochemical method for detecting the ouabain-sensitive, potassium-dependent p-nitrophenylphosphatase (K-NPPase) activity of the sodium-potassium-activated adenosine triphosphatase (Na-K ATPase) complex. The incubation medium contains p-nitrophenylphosphate (p-NPP) as substrate, cerium chloride as capture agent, Tricine buffer, MgCl2, and KCl. Tricine buffer protected against the medium turbidity caused by non-enzymatic reaction at pH 7.5. Biochemically, the accumulation of p-nitrophenol and phosphate in the reaction precipitate was proportionally related to the enzyme concentration. Ultracytochemically, the reaction products of the K-NPPase activity were localized as fine and uniform electron-dense deposits in the cytoplasmic side of specialized basolateral plasma membranes of cells of kidney distal convoluted tubules, secretory cells of salt gland, and marginal cells of stria vascularis. This method has the advantage of being useful at physiological pH.</description><subject>4-Nitrophenylphosphatase - metabolism</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Buffers</subject><subject>Cell physiology</subject><subject>Cerium</subject><subject>Ducks</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Guinea Pigs</subject><subject>Histocytochemistry</subject><subject>Hydrogen-Ion Concentration</subject><subject>Kidney Tubules, Distal - enzymology</subject><subject>Membrane and intracellular transports</subject><subject>Microscopy, Electron</subject><subject>Molecular and cellular biology</subject><subject>Nitrophenols - metabolism</subject><subject>Organophosphorus Compounds - metabolism</subject><subject>Ouabain - pharmacology</subject><subject>Phosphoric Monoester Hydrolases - metabolism</subject><subject>Potassium - pharmacology</subject><subject>Rats</subject><subject>Rats, Inbred Strains</subject><subject>Salt Gland - enzymology</subject><subject>Sodium-Potassium-Exchanging ATPase - metabolism</subject><subject>Stria Vascularis - enzymology</subject><issn>0022-1554</issn><issn>1551-5044</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1987</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp10MFu1DAQBmALgcpSuHFF8gEqITWLHcdxeqxWhSJV4gJny7HHG1eJHWynq7wEz4zbXZUTJ0szn_7xDELvKdlSKsQXxrd8ywijlLcv0IZyTitOmuYl2hBS11UpNK_Rm5TuCaFNw7szdHbiG_RnB9EtU9WrBAbrNQc9wOS0GvEEeQgG2xCxgQw6u-BxsDgsqlfOVwl8ctk9wCWeQ1YpPeYYmMEb8BnPlXc5hnkAv47zENI8qKIAq5L04PKKVUHDmlwYw_5p4nz7Fr2yakzw7vSeo19fb37ubqu7H9--767vKs1Y3VY91IYIrggzjWp7etWSzlraCmusaBiULSntLG1M3RtRC2qpNpppUbdCCd6zc3RxzJ1j-L1AynJyScM4Kg9hSVKIEkHqrsDLI9QxpBTByjm6ScVVUiIfzy8Zl1ye7ln4h1Pu0k9gnvG__sdTX6WysY3Ka5eeWcfaq6YThX0-sqT2IO_DEn25xv9Gfjrawe2Hg4sg06TGsXyAysPh8GRbQtlf-NGpOw</recordid><startdate>198705</startdate><enddate>198705</enddate><creator>Kobayashi, T</creator><creator>Okada, T</creator><creator>Seguchi, H</creator><general>Histochemical Soc</general><general>SAGE Publications</general><general>Histochemical Society</general><scope>IQODW</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></search><sort><creationdate>198705</creationdate><title>Cerium-based cytochemical method for detection of ouabain-sensitive, potassium-dependent p-nitrophenylphosphatase activity at physiological pH</title><author>Kobayashi, T ; Okada, T ; Seguchi, H</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3326-be2d075a03d4a6b19608ff167fdf743e445118f14d2bd7271f1cdc3c7267a75b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1987</creationdate><topic>4-Nitrophenylphosphatase - metabolism</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Buffers</topic><topic>Cell physiology</topic><topic>Cerium</topic><topic>Ducks</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Guinea Pigs</topic><topic>Histocytochemistry</topic><topic>Hydrogen-Ion Concentration</topic><topic>Kidney Tubules, Distal - enzymology</topic><topic>Membrane and intracellular transports</topic><topic>Microscopy, Electron</topic><topic>Molecular and cellular biology</topic><topic>Nitrophenols - metabolism</topic><topic>Organophosphorus Compounds - metabolism</topic><topic>Ouabain - pharmacology</topic><topic>Phosphoric Monoester Hydrolases - metabolism</topic><topic>Potassium - pharmacology</topic><topic>Rats</topic><topic>Rats, Inbred Strains</topic><topic>Salt Gland - enzymology</topic><topic>Sodium-Potassium-Exchanging ATPase - metabolism</topic><topic>Stria Vascularis - enzymology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kobayashi, T</creatorcontrib><creatorcontrib>Okada, T</creatorcontrib><creatorcontrib>Seguchi, H</creatorcontrib><collection>Pascal-Francis</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><jtitle>The journal of histochemistry and cytochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kobayashi, T</au><au>Okada, T</au><au>Seguchi, H</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cerium-based cytochemical method for detection of ouabain-sensitive, potassium-dependent p-nitrophenylphosphatase activity at physiological pH</atitle><jtitle>The journal of histochemistry and cytochemistry</jtitle><addtitle>J Histochem Cytochem</addtitle><date>1987-05</date><risdate>1987</risdate><volume>35</volume><issue>5</issue><spage>601</spage><epage>611</epage><pages>601-611</pages><issn>0022-1554</issn><eissn>1551-5044</eissn><coden>JHCYAS</coden><abstract>We have developed a new cytochemical method for detecting the ouabain-sensitive, potassium-dependent p-nitrophenylphosphatase (K-NPPase) activity of the sodium-potassium-activated adenosine triphosphatase (Na-K ATPase) complex. The incubation medium contains p-nitrophenylphosphate (p-NPP) as substrate, cerium chloride as capture agent, Tricine buffer, MgCl2, and KCl. Tricine buffer protected against the medium turbidity caused by non-enzymatic reaction at pH 7.5. Biochemically, the accumulation of p-nitrophenol and phosphate in the reaction precipitate was proportionally related to the enzyme concentration. Ultracytochemically, the reaction products of the K-NPPase activity were localized as fine and uniform electron-dense deposits in the cytoplasmic side of specialized basolateral plasma membranes of cells of kidney distal convoluted tubules, secretory cells of salt gland, and marginal cells of stria vascularis. This method has the advantage of being useful at physiological pH.</abstract><cop>Los Angeles, CA</cop><pub>Histochemical Soc</pub><pmid>3031156</pmid><doi>10.1177/35.5.3031156</doi><tpages>11</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0022-1554 |
| ispartof | The journal of histochemistry and cytochemistry, 1987-05, Vol.35 (5), p.601-611 |
| issn | 0022-1554 1551-5044 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_77445028 |
| source | MEDLINE; EZB Free E-Journals; SAGE Journals; Free Full-Text Journals in Chemistry |
| subjects | 4-Nitrophenylphosphatase - metabolism Animals Biological and medical sciences Buffers Cell physiology Cerium Ducks Fundamental and applied biological sciences. Psychology Guinea Pigs Histocytochemistry Hydrogen-Ion Concentration Kidney Tubules, Distal - enzymology Membrane and intracellular transports Microscopy, Electron Molecular and cellular biology Nitrophenols - metabolism Organophosphorus Compounds - metabolism Ouabain - pharmacology Phosphoric Monoester Hydrolases - metabolism Potassium - pharmacology Rats Rats, Inbred Strains Salt Gland - enzymology Sodium-Potassium-Exchanging ATPase - metabolism Stria Vascularis - enzymology |
| title | Cerium-based cytochemical method for detection of ouabain-sensitive, potassium-dependent p-nitrophenylphosphatase activity at physiological pH |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-03T13%3A56%3A48IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Cerium-based%20cytochemical%20method%20for%20detection%20of%20ouabain-sensitive,%20potassium-dependent%20p-nitrophenylphosphatase%20activity%20at%20physiological%20pH&rft.jtitle=The%20journal%20of%20histochemistry%20and%20cytochemistry&rft.au=Kobayashi,%20T&rft.date=1987-05&rft.volume=35&rft.issue=5&rft.spage=601&rft.epage=611&rft.pages=601-611&rft.issn=0022-1554&rft.eissn=1551-5044&rft.coden=JHCYAS&rft_id=info:doi/10.1177/35.5.3031156&rft_dat=%3Cproquest_cross%3E77445028%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=77445028&rft_id=info:pmid/3031156&rft_sage_id=10.1177_35.5.3031156&rfr_iscdi=true |