Interaction of ouabain with (Na + + K +)ATPase from human heart and from guinea-pig heart
(Na + + K +)ATPase (ATP phosphohydrolase, EC 3.6.1.3.) has been prepared from human heart and guinea-pig heart, with respective specific activities of 10–15 μmol P i · mg −1 · h −1 and of 25–30 μmol P i · mg −1 · h −1. Residual Mg 2+—ATPase activities were about 5 per cent. The parameters of (Na + +...
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creator | De Pover, Alain Godfraind, Theophile |
description | (Na
+ + K
+)ATPase (ATP phosphohydrolase, EC 3.6.1.3.) has been prepared from human heart and guinea-pig heart, with respective specific activities of 10–15 μmol P
i · mg
−1 · h
−1 and of 25–30 μmol P
i · mg
−1 · h
−1. Residual Mg
2+—ATPase activities were about 5 per cent. The parameters of (Na
+ + K
+)ATPase activity and of ouabain-interaction have been compared: (1) Half-maximal activity concentrations and Hill coefficients of Na
+, K
+, Mg
2+ and ATP were similar for the two species. The apparent activation energies calculated from Arrhenius plots were also similar. A transition was observed at about 23°C. (2) Human heart (Na
+ + K
+)ATPase was 10 times more sensitive to ouabain-inhibition than that of guinea-pig. Hunter-Downs plots showed a competitive inhibition for K
+ at low K
+ concentration and noncompetitive inhibition at high concentration. (3) The Scatchard plot for [
3H]ouabain binding was upward-concave with human heart and linear with guinea-pig heart. (4) The dissociation kinetics of [
3H]ouabain from human preparations studied by an isotopic dilution technique indicated two classes of binding sites with
k
d of 0.058 min
−1 and 0.0092 min
−1. The dissociation kinetics with guinea-pig heart indicated one single class of binding sites with a
k
d
of 0.43 min
−1. (5) The time-course of 0.2 μM [
3H]ouabain binding showed pseudo-first order association kinetics in man and in guinea-pig.
k
a
for the two classes of binding sites in man were therefore similar, respectively equal to 3.4 × 10
6 min
−1 · M
−1 and to 3.7 × 10
6 min
−1 · M
−1 ·
k
a
for guinea-pig heart was equal to 2.3.10
6 min
−1 · M
−1. (6) In guinea-pig heart,
K
D
c from Scatchard plot and from
k
d
/
k
a
ratio were equal to the inhibition constant
K
i
calculated from Hunter-Downs plot indicating that the binding sites were closely related to (Na
+ + K
+)ATPase inhibition. (7) In human heart,
K
D
of the low affinity binding sites was close to
K
i
, whereas
K
D
of the high affinity binding sites was several times lower. This suggests that only low affinity binding sites might be involved in (Na
+ + K
+)ATPase inhibition by ouabain. |
doi_str_mv | 10.1016/0006-2952(79)90612-9 |
format | Article |
fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_74854117</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>0006295279906129</els_id><sourcerecordid>74854117</sourcerecordid><originalsourceid>FETCH-LOGICAL-c356t-255f0a18413a706519e1eeeadc8d624f18c5569c22bc6cf6ee938596b98517e03</originalsourceid><addsrcrecordid>eNp9kMtOwzAQRS3EqxT-oAuvUKsqYDuxY2-QqopHRQUsyoKV5TqT1qhJip2A-HtSgrpEsxjN3DtXmoPQgJIrSqi4JoSIiCnOhqkaKSIoi9QB6lGZxu1ayEPU21tO0VkI77tRCnqCjhlTUogeepuVNXhja1eVuMpx1ZilcSX-cvUaD58MHrf1iMejyeLFBMC5rwq8bgpT4jUYX2NTZt1y1bgSTLR1q045R0e52QS4-Ot99Hp3u5g-RPPn-9l0Mo9szEUdMc5zYqhMaGxSIjhVQAHAZFZmgiU5lZZzoSxjSytsLgBULLkSSyU5TYHEfXTZ5W599dFAqHXhgoXNxpRQNUGnieQJpWlrTDqj9VUIHnK99a4w_ltTondA9Q6P3tHSqdK_QLVqzwZ_-c2ygGx_1BFs5ZtOhvbHTwdeB-ugtJA5D7bWWeX-z_8B1seCBA</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>74854117</pqid></control><display><type>article</type><title>Interaction of ouabain with (Na + + K +)ATPase from human heart and from guinea-pig heart</title><source>MEDLINE</source><source>ScienceDirect Journals (5 years ago - present)</source><creator>De Pover, Alain ; Godfraind, Theophile</creator><creatorcontrib>De Pover, Alain ; Godfraind, Theophile</creatorcontrib><description>(Na
+ + K
+)ATPase (ATP phosphohydrolase, EC 3.6.1.3.) has been prepared from human heart and guinea-pig heart, with respective specific activities of 10–15 μmol P
i · mg
−1 · h
−1 and of 25–30 μmol P
i · mg
−1 · h
−1. Residual Mg
2+—ATPase activities were about 5 per cent. The parameters of (Na
+ + K
+)ATPase activity and of ouabain-interaction have been compared: (1) Half-maximal activity concentrations and Hill coefficients of Na
+, K
+, Mg
2+ and ATP were similar for the two species. The apparent activation energies calculated from Arrhenius plots were also similar. A transition was observed at about 23°C. (2) Human heart (Na
+ + K
+)ATPase was 10 times more sensitive to ouabain-inhibition than that of guinea-pig. Hunter-Downs plots showed a competitive inhibition for K
+ at low K
+ concentration and noncompetitive inhibition at high concentration. (3) The Scatchard plot for [
3H]ouabain binding was upward-concave with human heart and linear with guinea-pig heart. (4) The dissociation kinetics of [
3H]ouabain from human preparations studied by an isotopic dilution technique indicated two classes of binding sites with
k
d of 0.058 min
−1 and 0.0092 min
−1. The dissociation kinetics with guinea-pig heart indicated one single class of binding sites with a
k
d
of 0.43 min
−1. (5) The time-course of 0.2 μM [
3H]ouabain binding showed pseudo-first order association kinetics in man and in guinea-pig.
k
a
for the two classes of binding sites in man were therefore similar, respectively equal to 3.4 × 10
6 min
−1 · M
−1 and to 3.7 × 10
6 min
−1 · M
−1 ·
k
a
for guinea-pig heart was equal to 2.3.10
6 min
−1 · M
−1. (6) In guinea-pig heart,
K
D
c from Scatchard plot and from
k
d
/
k
a
ratio were equal to the inhibition constant
K
i
calculated from Hunter-Downs plot indicating that the binding sites were closely related to (Na
+ + K
+)ATPase inhibition. (7) In human heart,
K
D
of the low affinity binding sites was close to
K
i
, whereas
K
D
of the high affinity binding sites was several times lower. This suggests that only low affinity binding sites might be involved in (Na
+ + K
+)ATPase inhibition by ouabain.</description><identifier>ISSN: 0006-2952</identifier><identifier>EISSN: 1873-2968</identifier><identifier>DOI: 10.1016/0006-2952(79)90612-9</identifier><identifier>PMID: 229866</identifier><language>eng</language><publisher>England: Elsevier Inc</publisher><subject>Animals ; Enzyme Activation ; Guinea Pigs ; Humans ; Kinetics ; Magnesium - pharmacology ; Myocardium - enzymology ; Ouabain - pharmacology ; Potassium - pharmacology ; Protein Binding ; Sodium - pharmacology ; Sodium-Potassium-Exchanging ATPase - metabolism ; Thermodynamics</subject><ispartof>Biochemical pharmacology, 1979-10, Vol.28 (20), p.3051-3056</ispartof><rights>1979</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c356t-255f0a18413a706519e1eeeadc8d624f18c5569c22bc6cf6ee938596b98517e03</citedby><cites>FETCH-LOGICAL-c356t-255f0a18413a706519e1eeeadc8d624f18c5569c22bc6cf6ee938596b98517e03</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/0006295279906129$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27903,27904,65309</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/229866$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>De Pover, Alain</creatorcontrib><creatorcontrib>Godfraind, Theophile</creatorcontrib><title>Interaction of ouabain with (Na + + K +)ATPase from human heart and from guinea-pig heart</title><title>Biochemical pharmacology</title><addtitle>Biochem Pharmacol</addtitle><description>(Na
+ + K
+)ATPase (ATP phosphohydrolase, EC 3.6.1.3.) has been prepared from human heart and guinea-pig heart, with respective specific activities of 10–15 μmol P
i · mg
−1 · h
−1 and of 25–30 μmol P
i · mg
−1 · h
−1. Residual Mg
2+—ATPase activities were about 5 per cent. The parameters of (Na
+ + K
+)ATPase activity and of ouabain-interaction have been compared: (1) Half-maximal activity concentrations and Hill coefficients of Na
+, K
+, Mg
2+ and ATP were similar for the two species. The apparent activation energies calculated from Arrhenius plots were also similar. A transition was observed at about 23°C. (2) Human heart (Na
+ + K
+)ATPase was 10 times more sensitive to ouabain-inhibition than that of guinea-pig. Hunter-Downs plots showed a competitive inhibition for K
+ at low K
+ concentration and noncompetitive inhibition at high concentration. (3) The Scatchard plot for [
3H]ouabain binding was upward-concave with human heart and linear with guinea-pig heart. (4) The dissociation kinetics of [
3H]ouabain from human preparations studied by an isotopic dilution technique indicated two classes of binding sites with
k
d of 0.058 min
−1 and 0.0092 min
−1. The dissociation kinetics with guinea-pig heart indicated one single class of binding sites with a
k
d
of 0.43 min
−1. (5) The time-course of 0.2 μM [
3H]ouabain binding showed pseudo-first order association kinetics in man and in guinea-pig.
k
a
for the two classes of binding sites in man were therefore similar, respectively equal to 3.4 × 10
6 min
−1 · M
−1 and to 3.7 × 10
6 min
−1 · M
−1 ·
k
a
for guinea-pig heart was equal to 2.3.10
6 min
−1 · M
−1. (6) In guinea-pig heart,
K
D
c from Scatchard plot and from
k
d
/
k
a
ratio were equal to the inhibition constant
K
i
calculated from Hunter-Downs plot indicating that the binding sites were closely related to (Na
+ + K
+)ATPase inhibition. (7) In human heart,
K
D
of the low affinity binding sites was close to
K
i
, whereas
K
D
of the high affinity binding sites was several times lower. This suggests that only low affinity binding sites might be involved in (Na
+ + K
+)ATPase inhibition by ouabain.</description><subject>Animals</subject><subject>Enzyme Activation</subject><subject>Guinea Pigs</subject><subject>Humans</subject><subject>Kinetics</subject><subject>Magnesium - pharmacology</subject><subject>Myocardium - enzymology</subject><subject>Ouabain - pharmacology</subject><subject>Potassium - pharmacology</subject><subject>Protein Binding</subject><subject>Sodium - pharmacology</subject><subject>Sodium-Potassium-Exchanging ATPase - metabolism</subject><subject>Thermodynamics</subject><issn>0006-2952</issn><issn>1873-2968</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1979</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kMtOwzAQRS3EqxT-oAuvUKsqYDuxY2-QqopHRQUsyoKV5TqT1qhJip2A-HtSgrpEsxjN3DtXmoPQgJIrSqi4JoSIiCnOhqkaKSIoi9QB6lGZxu1ayEPU21tO0VkI77tRCnqCjhlTUogeepuVNXhja1eVuMpx1ZilcSX-cvUaD58MHrf1iMejyeLFBMC5rwq8bgpT4jUYX2NTZt1y1bgSTLR1q045R0e52QS4-Ot99Hp3u5g-RPPn-9l0Mo9szEUdMc5zYqhMaGxSIjhVQAHAZFZmgiU5lZZzoSxjSytsLgBULLkSSyU5TYHEfXTZ5W599dFAqHXhgoXNxpRQNUGnieQJpWlrTDqj9VUIHnK99a4w_ltTondA9Q6P3tHSqdK_QLVqzwZ_-c2ygGx_1BFs5ZtOhvbHTwdeB-ugtJA5D7bWWeX-z_8B1seCBA</recordid><startdate>19791015</startdate><enddate>19791015</enddate><creator>De Pover, Alain</creator><creator>Godfraind, Theophile</creator><general>Elsevier Inc</general><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>19791015</creationdate><title>Interaction of ouabain with (Na + + K +)ATPase from human heart and from guinea-pig heart</title><author>De Pover, Alain ; Godfraind, Theophile</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c356t-255f0a18413a706519e1eeeadc8d624f18c5569c22bc6cf6ee938596b98517e03</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1979</creationdate><topic>Animals</topic><topic>Enzyme Activation</topic><topic>Guinea Pigs</topic><topic>Humans</topic><topic>Kinetics</topic><topic>Magnesium - pharmacology</topic><topic>Myocardium - enzymology</topic><topic>Ouabain - pharmacology</topic><topic>Potassium - pharmacology</topic><topic>Protein Binding</topic><topic>Sodium - pharmacology</topic><topic>Sodium-Potassium-Exchanging ATPase - metabolism</topic><topic>Thermodynamics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>De Pover, Alain</creatorcontrib><creatorcontrib>Godfraind, Theophile</creatorcontrib><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>Biochemical pharmacology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>De Pover, Alain</au><au>Godfraind, Theophile</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Interaction of ouabain with (Na + + K +)ATPase from human heart and from guinea-pig heart</atitle><jtitle>Biochemical pharmacology</jtitle><addtitle>Biochem Pharmacol</addtitle><date>1979-10-15</date><risdate>1979</risdate><volume>28</volume><issue>20</issue><spage>3051</spage><epage>3056</epage><pages>3051-3056</pages><issn>0006-2952</issn><eissn>1873-2968</eissn><abstract>(Na
+ + K
+)ATPase (ATP phosphohydrolase, EC 3.6.1.3.) has been prepared from human heart and guinea-pig heart, with respective specific activities of 10–15 μmol P
i · mg
−1 · h
−1 and of 25–30 μmol P
i · mg
−1 · h
−1. Residual Mg
2+—ATPase activities were about 5 per cent. The parameters of (Na
+ + K
+)ATPase activity and of ouabain-interaction have been compared: (1) Half-maximal activity concentrations and Hill coefficients of Na
+, K
+, Mg
2+ and ATP were similar for the two species. The apparent activation energies calculated from Arrhenius plots were also similar. A transition was observed at about 23°C. (2) Human heart (Na
+ + K
+)ATPase was 10 times more sensitive to ouabain-inhibition than that of guinea-pig. Hunter-Downs plots showed a competitive inhibition for K
+ at low K
+ concentration and noncompetitive inhibition at high concentration. (3) The Scatchard plot for [
3H]ouabain binding was upward-concave with human heart and linear with guinea-pig heart. (4) The dissociation kinetics of [
3H]ouabain from human preparations studied by an isotopic dilution technique indicated two classes of binding sites with
k
d of 0.058 min
−1 and 0.0092 min
−1. The dissociation kinetics with guinea-pig heart indicated one single class of binding sites with a
k
d
of 0.43 min
−1. (5) The time-course of 0.2 μM [
3H]ouabain binding showed pseudo-first order association kinetics in man and in guinea-pig.
k
a
for the two classes of binding sites in man were therefore similar, respectively equal to 3.4 × 10
6 min
−1 · M
−1 and to 3.7 × 10
6 min
−1 · M
−1 ·
k
a
for guinea-pig heart was equal to 2.3.10
6 min
−1 · M
−1. (6) In guinea-pig heart,
K
D
c from Scatchard plot and from
k
d
/
k
a
ratio were equal to the inhibition constant
K
i
calculated from Hunter-Downs plot indicating that the binding sites were closely related to (Na
+ + K
+)ATPase inhibition. (7) In human heart,
K
D
of the low affinity binding sites was close to
K
i
, whereas
K
D
of the high affinity binding sites was several times lower. This suggests that only low affinity binding sites might be involved in (Na
+ + K
+)ATPase inhibition by ouabain.</abstract><cop>England</cop><pub>Elsevier Inc</pub><pmid>229866</pmid><doi>10.1016/0006-2952(79)90612-9</doi><tpages>6</tpages></addata></record> |
fulltext | fulltext |
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ispartof | Biochemical pharmacology, 1979-10, Vol.28 (20), p.3051-3056 |
issn | 0006-2952 1873-2968 |
language | eng |
recordid | cdi_proquest_miscellaneous_74854117 |
source | MEDLINE; ScienceDirect Journals (5 years ago - present) |
subjects | Animals Enzyme Activation Guinea Pigs Humans Kinetics Magnesium - pharmacology Myocardium - enzymology Ouabain - pharmacology Potassium - pharmacology Protein Binding Sodium - pharmacology Sodium-Potassium-Exchanging ATPase - metabolism Thermodynamics |
title | Interaction of ouabain with (Na + + K +)ATPase from human heart and from guinea-pig heart |
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