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(Na + + K + ) ATPase has one functioning phosphorylation site per α subunit
(Na + + K + )ATPase contains two different subunits, a catalytic subunit ( α ) and a subunit with uncertain function (β). The enzyme binds ATP, ouabain and vanadate, and can be phos-phorylated by ATP as well as by inorganic phosphate. From the previously reported maximal binding and phosphorylation...
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| Published in: | Nature (London) 1981-03, Vol.290 (5804), p.338-339 |
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| Main Authors: | , , , , |
| Format: | Article |
| Language: | English |
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| cited_by | cdi_FETCH-LOGICAL-c364t-9fd5137d21c5b329663fc808ef0905266bcc796bebc3569dac2dcc4ebd05134f3 |
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| cites | cdi_FETCH-LOGICAL-c364t-9fd5137d21c5b329663fc808ef0905266bcc796bebc3569dac2dcc4ebd05134f3 |
| container_end_page | 339 |
| container_issue | 5804 |
| container_start_page | 338 |
| container_title | Nature (London) |
| container_volume | 290 |
| creator | Peters, W. H. M Swarts, H. G. P de Pont, J. J. H. H. M Stekhoven, F. M. A. H. Schuurmans Bonting, S. L |
| description | (Na
+
+ K
+
)ATPase contains two different subunits, a catalytic subunit (
α
) and a subunit with uncertain function (β). The enzyme binds ATP, ouabain and vanadate, and can be phos-phorylated by ATP as well as by inorganic phosphate. From the previously reported maximal binding and phosphorylation capacities of 3.5–4.3 nmol P per mg protein
1–3
(based on Lowry protein determination) and the earlier molecular weight value of ∼250,000
1,2
, a molar binding and phosphorylation capacity of 0.87–1.07 mol per mol enzyme was derived. As it is generally agreed that the enzyme molecule contains two
α
subunits
1–6
or even a multiple of two
7,8
, it has been suggested that the enzyme operates by means of a so-called ‘half-of-the-sites mechanism’, whereby only one of the two
α
subunits can be phosphorylated at any one time
9,10
. We now present evidence that every
α
subunit can be phosphorylated simultaneously, which rules out the operation of such a mechanism. |
| doi_str_mv | 10.1038/290338a0 |
| format | article |
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+
+ K
+
)ATPase contains two different subunits, a catalytic subunit (
α
) and a subunit with uncertain function (β). The enzyme binds ATP, ouabain and vanadate, and can be phos-phorylated by ATP as well as by inorganic phosphate. From the previously reported maximal binding and phosphorylation capacities of 3.5–4.3 nmol P per mg protein
1–3
(based on Lowry protein determination) and the earlier molecular weight value of ∼250,000
1,2
, a molar binding and phosphorylation capacity of 0.87–1.07 mol per mol enzyme was derived. As it is generally agreed that the enzyme molecule contains two
α
subunits
1–6
or even a multiple of two
7,8
, it has been suggested that the enzyme operates by means of a so-called ‘half-of-the-sites mechanism’, whereby only one of the two
α
subunits can be phosphorylated at any one time
9,10
. We now present evidence that every
α
subunit can be phosphorylated simultaneously, which rules out the operation of such a mechanism.</description><identifier>ISSN: 0028-0836</identifier><identifier>EISSN: 1476-4687</identifier><identifier>DOI: 10.1038/290338a0</identifier><identifier>PMID: 6259540</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>Adenosine Triphosphate - metabolism ; Animals ; Binding Sites ; Humanities and Social Sciences ; Kidney - enzymology ; letter ; Macromolecular Substances ; multidisciplinary ; Phosphorylation ; Protein Conformation ; Rabbits ; Science ; Science (multidisciplinary) ; Sodium-Potassium-Exchanging ATPase - metabolism</subject><ispartof>Nature (London), 1981-03, Vol.290 (5804), p.338-339</ispartof><rights>Springer Nature Limited 1981</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c364t-9fd5137d21c5b329663fc808ef0905266bcc796bebc3569dac2dcc4ebd05134f3</citedby><cites>FETCH-LOGICAL-c364t-9fd5137d21c5b329663fc808ef0905266bcc796bebc3569dac2dcc4ebd05134f3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,2727,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/6259540$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Peters, W. H. M</creatorcontrib><creatorcontrib>Swarts, H. G. P</creatorcontrib><creatorcontrib>de Pont, J. J. H. H. M</creatorcontrib><creatorcontrib>Stekhoven, F. M. A. H. Schuurmans</creatorcontrib><creatorcontrib>Bonting, S. L</creatorcontrib><title>(Na + + K + ) ATPase has one functioning phosphorylation site per α subunit</title><title>Nature (London)</title><addtitle>Nature</addtitle><addtitle>Nature</addtitle><description>(Na
+
+ K
+
)ATPase contains two different subunits, a catalytic subunit (
α
) and a subunit with uncertain function (β). The enzyme binds ATP, ouabain and vanadate, and can be phos-phorylated by ATP as well as by inorganic phosphate. From the previously reported maximal binding and phosphorylation capacities of 3.5–4.3 nmol P per mg protein
1–3
(based on Lowry protein determination) and the earlier molecular weight value of ∼250,000
1,2
, a molar binding and phosphorylation capacity of 0.87–1.07 mol per mol enzyme was derived. As it is generally agreed that the enzyme molecule contains two
α
subunits
1–6
or even a multiple of two
7,8
, it has been suggested that the enzyme operates by means of a so-called ‘half-of-the-sites mechanism’, whereby only one of the two
α
subunits can be phosphorylated at any one time
9,10
. We now present evidence that every
α
subunit can be phosphorylated simultaneously, which rules out the operation of such a mechanism.</description><subject>Adenosine Triphosphate - metabolism</subject><subject>Animals</subject><subject>Binding Sites</subject><subject>Humanities and Social Sciences</subject><subject>Kidney - enzymology</subject><subject>letter</subject><subject>Macromolecular Substances</subject><subject>multidisciplinary</subject><subject>Phosphorylation</subject><subject>Protein Conformation</subject><subject>Rabbits</subject><subject>Science</subject><subject>Science (multidisciplinary)</subject><subject>Sodium-Potassium-Exchanging ATPase - metabolism</subject><issn>0028-0836</issn><issn>1476-4687</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1981</creationdate><recordtype>article</recordtype><recordid>eNptkN9KwzAUxoMoc07BF1ByJRtSTZMmTS7H8B8O9WJelzRNt44urUlzscfyRXwmMzp3JYfDgfP9-DjnA-AyRncxIvweC0QIl-gIDOMkZVHCeHoMhghhHiFO2Ck4c26NEKJxmgzAgGEqaIKGYD5-k_A21GvoCZwuPqTTcCUdbIyGpTeqqxpTmSVsV40Lbbe13K2gqzoNW23hzzd0Pvem6s7BSSlrpy_2cwQ-Hx8Ws-do_v70MpvOI0VY0kWiLGhM0gLHiuYEC8ZIqTjiukQCUcxYrlQqWK5zRSgThVS4UCrReRHOJ0lJRuCm921t8-W167JN5ZSua2l0412WUsoJTkkAxz2obOOc1WXW2moj7TaLUbYLLvsLLqBXe0-fb3RxAPdJBX3S6y4oZqlttm68NeHN_7yue9bIzlt98DoAv6fUfbQ</recordid><startdate>19810326</startdate><enddate>19810326</enddate><creator>Peters, W. H. M</creator><creator>Swarts, H. G. P</creator><creator>de Pont, J. J. H. H. M</creator><creator>Stekhoven, F. M. A. H. Schuurmans</creator><creator>Bonting, S. L</creator><general>Nature Publishing Group UK</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>19810326</creationdate><title>(Na + + K + ) ATPase has one functioning phosphorylation site per α subunit</title><author>Peters, W. H. M ; Swarts, H. G. P ; de Pont, J. J. H. H. M ; Stekhoven, F. M. A. H. Schuurmans ; Bonting, S. L</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c364t-9fd5137d21c5b329663fc808ef0905266bcc796bebc3569dac2dcc4ebd05134f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1981</creationdate><topic>Adenosine Triphosphate - metabolism</topic><topic>Animals</topic><topic>Binding Sites</topic><topic>Humanities and Social Sciences</topic><topic>Kidney - enzymology</topic><topic>letter</topic><topic>Macromolecular Substances</topic><topic>multidisciplinary</topic><topic>Phosphorylation</topic><topic>Protein Conformation</topic><topic>Rabbits</topic><topic>Science</topic><topic>Science (multidisciplinary)</topic><topic>Sodium-Potassium-Exchanging ATPase - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Peters, W. H. M</creatorcontrib><creatorcontrib>Swarts, H. G. P</creatorcontrib><creatorcontrib>de Pont, J. J. H. H. M</creatorcontrib><creatorcontrib>Stekhoven, F. M. A. H. Schuurmans</creatorcontrib><creatorcontrib>Bonting, S. L</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>Nature (London)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Peters, W. H. M</au><au>Swarts, H. G. P</au><au>de Pont, J. J. H. H. M</au><au>Stekhoven, F. M. A. H. Schuurmans</au><au>Bonting, S. L</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>(Na + + K + ) ATPase has one functioning phosphorylation site per α subunit</atitle><jtitle>Nature (London)</jtitle><stitle>Nature</stitle><addtitle>Nature</addtitle><date>1981-03-26</date><risdate>1981</risdate><volume>290</volume><issue>5804</issue><spage>338</spage><epage>339</epage><pages>338-339</pages><issn>0028-0836</issn><eissn>1476-4687</eissn><abstract>(Na
+
+ K
+
)ATPase contains two different subunits, a catalytic subunit (
α
) and a subunit with uncertain function (β). The enzyme binds ATP, ouabain and vanadate, and can be phos-phorylated by ATP as well as by inorganic phosphate. From the previously reported maximal binding and phosphorylation capacities of 3.5–4.3 nmol P per mg protein
1–3
(based on Lowry protein determination) and the earlier molecular weight value of ∼250,000
1,2
, a molar binding and phosphorylation capacity of 0.87–1.07 mol per mol enzyme was derived. As it is generally agreed that the enzyme molecule contains two
α
subunits
1–6
or even a multiple of two
7,8
, it has been suggested that the enzyme operates by means of a so-called ‘half-of-the-sites mechanism’, whereby only one of the two
α
subunits can be phosphorylated at any one time
9,10
. We now present evidence that every
α
subunit can be phosphorylated simultaneously, which rules out the operation of such a mechanism.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>6259540</pmid><doi>10.1038/290338a0</doi><tpages>2</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0028-0836 |
| ispartof | Nature (London), 1981-03, Vol.290 (5804), p.338-339 |
| issn | 0028-0836 1476-4687 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_75583273 |
| source | Nature |
| subjects | Adenosine Triphosphate - metabolism Animals Binding Sites Humanities and Social Sciences Kidney - enzymology letter Macromolecular Substances multidisciplinary Phosphorylation Protein Conformation Rabbits Science Science (multidisciplinary) Sodium-Potassium-Exchanging ATPase - metabolism |
| title | (Na + + K + ) ATPase has one functioning phosphorylation site per α subunit |
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