Purification and properties of human erythrocyte inosine triphosphate pyrophosphohydrolase
Inosine triphosphate pyrophosphohydrolase from human erythrocytes was purified and characterized. The enzyme is highly specific for ITP and shows optimal activity in glycine buffer pH 9.6 and 50 mM MgCl2. The Km of the enzyme is 1.3 × 10−4, the Vmax = 1.2 × 10−9 and the Keq = 3.8 × 104. Human erythr...
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| Veröffentlicht in: | Journal of cellular physiology 1979-01, Vol.98 (1), p.41-47 |
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| container_title | Journal of cellular physiology |
| container_volume | 98 |
| creator | Vanderheiden, Bernardo S. |
| description | Inosine triphosphate pyrophosphohydrolase from human erythrocytes was purified and characterized. The enzyme is highly specific for ITP and shows optimal activity in glycine buffer pH 9.6 and 50 mM MgCl2. The Km of the enzyme is 1.3 × 10−4, the Vmax = 1.2 × 10−9 and the Keq = 3.8 × 104. Human erythrocyte ITP pyrophosphohydrolase does not require SH compounds for activation. The enzyme is inhibited by Cd++, Co++, and Ca++ ions and by phydroxymercuribenzoate. |
| doi_str_mv | 10.1002/jcp.1040980106 |
| format | Article |
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The enzyme is highly specific for ITP and shows optimal activity in glycine buffer pH 9.6 and 50 mM MgCl2. The Km of the enzyme is 1.3 × 10−4, the Vmax = 1.2 × 10−9 and the Keq = 3.8 × 104. Human erythrocyte ITP pyrophosphohydrolase does not require SH compounds for activation. The enzyme is inhibited by Cd++, Co++, and Ca++ ions and by phydroxymercuribenzoate.</description><identifier>ISSN: 0021-9541</identifier><identifier>EISSN: 1097-4652</identifier><identifier>DOI: 10.1002/jcp.1040980106</identifier><identifier>PMID: 33191</identifier><language>eng</language><publisher>Hoboken: Wiley Subscription Services, Inc., A Wiley Company</publisher><subject>Cations, Divalent ; Erythrocytes - enzymology ; Humans ; Hydrogen-Ion Concentration ; Hydroxymercuribenzoates - pharmacology ; Inosine Nucleotides ; Inosine Triphosphatase ; Inosine Triphosphate ; Magnesium - pharmacology ; Methods ; Pyrophosphatases - isolation & purification ; Pyrophosphatases - metabolism ; Substrate Specificity</subject><ispartof>Journal of cellular physiology, 1979-01, Vol.98 (1), p.41-47</ispartof><rights>Copyright © 1979 Wiley‐Liss, Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3456-386946296c7437e984d23087f55da180a114229c5aa2821c0ec4dcb7268628663</citedby><cites>FETCH-LOGICAL-c3456-386946296c7437e984d23087f55da180a114229c5aa2821c0ec4dcb7268628663</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fjcp.1040980106$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fjcp.1040980106$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,777,781,1412,27905,27906,45555,45556</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/33191$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Vanderheiden, Bernardo S.</creatorcontrib><title>Purification and properties of human erythrocyte inosine triphosphate pyrophosphohydrolase</title><title>Journal of cellular physiology</title><addtitle>J. Cell. Physiol</addtitle><description>Inosine triphosphate pyrophosphohydrolase from human erythrocytes was purified and characterized. The enzyme is highly specific for ITP and shows optimal activity in glycine buffer pH 9.6 and 50 mM MgCl2. The Km of the enzyme is 1.3 × 10−4, the Vmax = 1.2 × 10−9 and the Keq = 3.8 × 104. Human erythrocyte ITP pyrophosphohydrolase does not require SH compounds for activation. The enzyme is inhibited by Cd++, Co++, and Ca++ ions and by phydroxymercuribenzoate.</description><subject>Cations, Divalent</subject><subject>Erythrocytes - enzymology</subject><subject>Humans</subject><subject>Hydrogen-Ion Concentration</subject><subject>Hydroxymercuribenzoates - pharmacology</subject><subject>Inosine Nucleotides</subject><subject>Inosine Triphosphatase</subject><subject>Inosine Triphosphate</subject><subject>Magnesium - pharmacology</subject><subject>Methods</subject><subject>Pyrophosphatases - isolation & purification</subject><subject>Pyrophosphatases - metabolism</subject><subject>Substrate Specificity</subject><issn>0021-9541</issn><issn>1097-4652</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1979</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1PwjAcxhsjUUSvXrzsCwz7tq49GiKoQSREY-KlKV2XFWFd2hHdt7eCwXjy9H95nt9zeAC4RHCIIMTXK93EhULBIYLsCPQRFHlKWYaPQT8aUCoyik7BWQgrCKEQhJyAHiFIoD54m2-9La1WrXV1ouoiabxrjG-tCYkrk2q7UXVifNdW3umuNYmtXbC1SVpvm8qFplLx2XSR2l2u6grv1iqYc9Ar1TqYi585AC_j2-fRXTp9mtyPbqapJjRjKeFMUIYF0zkluRGcFphAnpdZVijEoUKIYix0phTmGGloNC30MseMM8wZIwMw3Odq70LwppSNtxvlO4mg_G5Ixobkb0MRuNoDzXa5McXBvqskqmKvfti16f7Jkg-j-Z_kdM_a0JrPA6v8u2Q5yTP5OpvI8WI2mS5i1CP5AsC5gkk</recordid><startdate>197901</startdate><enddate>197901</enddate><creator>Vanderheiden, Bernardo S.</creator><general>Wiley Subscription Services, Inc., A Wiley Company</general><scope>BSCLL</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></search><sort><creationdate>197901</creationdate><title>Purification and properties of human erythrocyte inosine triphosphate pyrophosphohydrolase</title><author>Vanderheiden, Bernardo S.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3456-386946296c7437e984d23087f55da180a114229c5aa2821c0ec4dcb7268628663</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1979</creationdate><topic>Cations, Divalent</topic><topic>Erythrocytes - enzymology</topic><topic>Humans</topic><topic>Hydrogen-Ion Concentration</topic><topic>Hydroxymercuribenzoates - pharmacology</topic><topic>Inosine Nucleotides</topic><topic>Inosine Triphosphatase</topic><topic>Inosine Triphosphate</topic><topic>Magnesium - pharmacology</topic><topic>Methods</topic><topic>Pyrophosphatases - isolation & purification</topic><topic>Pyrophosphatases - metabolism</topic><topic>Substrate Specificity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Vanderheiden, Bernardo S.</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><jtitle>Journal of cellular physiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Vanderheiden, Bernardo S.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification and properties of human erythrocyte inosine triphosphate pyrophosphohydrolase</atitle><jtitle>Journal of cellular physiology</jtitle><addtitle>J. Cell. Physiol</addtitle><date>1979-01</date><risdate>1979</risdate><volume>98</volume><issue>1</issue><spage>41</spage><epage>47</epage><pages>41-47</pages><issn>0021-9541</issn><eissn>1097-4652</eissn><abstract>Inosine triphosphate pyrophosphohydrolase from human erythrocytes was purified and characterized. The enzyme is highly specific for ITP and shows optimal activity in glycine buffer pH 9.6 and 50 mM MgCl2. The Km of the enzyme is 1.3 × 10−4, the Vmax = 1.2 × 10−9 and the Keq = 3.8 × 104. Human erythrocyte ITP pyrophosphohydrolase does not require SH compounds for activation. The enzyme is inhibited by Cd++, Co++, and Ca++ ions and by phydroxymercuribenzoate.</abstract><cop>Hoboken</cop><pub>Wiley Subscription Services, Inc., A Wiley Company</pub><pmid>33191</pmid><doi>10.1002/jcp.1040980106</doi><tpages>7</tpages></addata></record> |
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| ispartof | Journal of cellular physiology, 1979-01, Vol.98 (1), p.41-47 |
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| language | eng |
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| source | MEDLINE; Wiley Online Library Journals Frontfile Complete |
| subjects | Cations, Divalent Erythrocytes - enzymology Humans Hydrogen-Ion Concentration Hydroxymercuribenzoates - pharmacology Inosine Nucleotides Inosine Triphosphatase Inosine Triphosphate Magnesium - pharmacology Methods Pyrophosphatases - isolation & purification Pyrophosphatases - metabolism Substrate Specificity |
| title | Purification and properties of human erythrocyte inosine triphosphate pyrophosphohydrolase |
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