Enzymatic properties of two calcium-stimulated ATPases in the neutral and acidic pH regions found in the membrane fraction of human milk
Two calcium-stimulated ATPases at optimal pH values of 5.0 and 7.0, which are designated as acid and neutral Ca 2+ -ATPase, respectively, were found in the membrane fraction of human milk, and their enzymatic properties were studied. For maximal activity, neutral Ca 2+ -ATPase required 0.45 mM Ca io...
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| Veröffentlicht in: | Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 1992, Vol.56 (6), p.900-905 |
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| creator | Kanno, C. (Utsunomiya Univ. (Japan)) Takeda, Y Cho, J.K |
| description | Two calcium-stimulated ATPases at optimal pH values of 5.0 and 7.0, which are designated as acid and neutral Ca
2+
-ATPase, respectively, were found in the membrane fraction of human milk, and their enzymatic properties were studied. For maximal activity, neutral Ca
2+
-ATPase required 0.45 mM Ca ion, while acid Ca
2+
-ATPase required 207 mM Ca ion. Neutral Ca
2+
-ATPase activity was not enhanced by adding the Mg ion at more than 0.1 mM. Among the nucleotides, neutral Ca
2+
-ATPase showed a higher substrate specificity to GTP, CTP, ITP, and UTP than to ATP, while ATP was the best substrate for acid Ca
2+
-ATPase. Neutral and acid Ca
2+
-ATPases had apparent K
m
values of 0.361 and 0.192 mM, and V
max
of 186 and 178 μmol ATP hydrolyzed/mg of protein per min, respectively. Both Ca
2+
-ATPases were potently inhibited by fluoride, lanthanide, vanadate, and p-chloromercuribenzoate, and inactivated by EDTA, EGTA, and CDTA, but were unaffected by N-ethylmaleimide, NaN
3
, ouabain, oxidized glutathione, or oligomycin, and were inactivated by heating at 60°C for 10 min. These enzymes were concentrated in the membrane fraction of the cream and skim milk membrane. |
| doi_str_mv | 10.1271/bbb.56.900 |
| format | Article |
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2+
-ATPase, respectively, were found in the membrane fraction of human milk, and their enzymatic properties were studied. For maximal activity, neutral Ca
2+
-ATPase required 0.45 mM Ca ion, while acid Ca
2+
-ATPase required 207 mM Ca ion. Neutral Ca
2+
-ATPase activity was not enhanced by adding the Mg ion at more than 0.1 mM. Among the nucleotides, neutral Ca
2+
-ATPase showed a higher substrate specificity to GTP, CTP, ITP, and UTP than to ATP, while ATP was the best substrate for acid Ca
2+
-ATPase. Neutral and acid Ca
2+
-ATPases had apparent K
m
values of 0.361 and 0.192 mM, and V
max
of 186 and 178 μmol ATP hydrolyzed/mg of protein per min, respectively. Both Ca
2+
-ATPases were potently inhibited by fluoride, lanthanide, vanadate, and p-chloromercuribenzoate, and inactivated by EDTA, EGTA, and CDTA, but were unaffected by N-ethylmaleimide, NaN
3
, ouabain, oxidized glutathione, or oligomycin, and were inactivated by heating at 60°C for 10 min. These enzymes were concentrated in the membrane fraction of the cream and skim milk membrane.</description><identifier>ISSN: 0916-8451</identifier><identifier>EISSN: 1347-6947</identifier><identifier>DOI: 10.1271/bbb.56.900</identifier><identifier>PMID: 27280811</identifier><language>eng</language><publisher>Tokyo: Taylor & Francis</publisher><subject>ACTIVIDAD ENZIMATICA ; ACTIVITE ENZYMATIQUE ; ADENOSINA TRIFOSFATASA ; ADENOSINE TRIPHOSPHATASE ; Analytical, structural and metabolic biochemistry ; Biological and medical sciences ; CALCIO ; CALCIUM ; Enzymes and enzyme inhibitors ; ENZYMIC ACTIVITY ; Fundamental and applied biological sciences. Psychology ; HUMAN MILK ; Hydrolases ; LAIT HUMAIN ; LECHE HUMANA ; MEMBRANA ; MEMBRANE ; MEMBRANES</subject><ispartof>Bioscience, biotechnology, and biochemistry, 1992, Vol.56 (6), p.900-905</ispartof><rights>Copyright 1992 Taylor and Francis Group LLC 1992</rights><rights>1993 INIST-CNRS</rights><rights>Copyright Japan Science and Technology Agency 1992</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c489t-3e822390c933eacdace1a152123652f1b2adc946ed283e9bdd653a7d80e77b6f3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,4010,27900,27901,27902</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4598287$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/27280811$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kanno, C. (Utsunomiya Univ. (Japan))</creatorcontrib><creatorcontrib>Takeda, Y</creatorcontrib><creatorcontrib>Cho, J.K</creatorcontrib><title>Enzymatic properties of two calcium-stimulated ATPases in the neutral and acidic pH regions found in the membrane fraction of human milk</title><title>Bioscience, biotechnology, and biochemistry</title><addtitle>Biosci Biotechnol Biochem</addtitle><description>Two calcium-stimulated ATPases at optimal pH values of 5.0 and 7.0, which are designated as acid and neutral Ca
2+
-ATPase, respectively, were found in the membrane fraction of human milk, and their enzymatic properties were studied. For maximal activity, neutral Ca
2+
-ATPase required 0.45 mM Ca ion, while acid Ca
2+
-ATPase required 207 mM Ca ion. Neutral Ca
2+
-ATPase activity was not enhanced by adding the Mg ion at more than 0.1 mM. Among the nucleotides, neutral Ca
2+
-ATPase showed a higher substrate specificity to GTP, CTP, ITP, and UTP than to ATP, while ATP was the best substrate for acid Ca
2+
-ATPase. Neutral and acid Ca
2+
-ATPases had apparent K
m
values of 0.361 and 0.192 mM, and V
max
of 186 and 178 μmol ATP hydrolyzed/mg of protein per min, respectively. Both Ca
2+
-ATPases were potently inhibited by fluoride, lanthanide, vanadate, and p-chloromercuribenzoate, and inactivated by EDTA, EGTA, and CDTA, but were unaffected by N-ethylmaleimide, NaN
3
, ouabain, oxidized glutathione, or oligomycin, and were inactivated by heating at 60°C for 10 min. These enzymes were concentrated in the membrane fraction of the cream and skim milk membrane.</description><subject>ACTIVIDAD ENZIMATICA</subject><subject>ACTIVITE ENZYMATIQUE</subject><subject>ADENOSINA TRIFOSFATASA</subject><subject>ADENOSINE TRIPHOSPHATASE</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Biological and medical sciences</subject><subject>CALCIO</subject><subject>CALCIUM</subject><subject>Enzymes and enzyme inhibitors</subject><subject>ENZYMIC ACTIVITY</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>HUMAN MILK</subject><subject>Hydrolases</subject><subject>LAIT HUMAIN</subject><subject>LECHE HUMANA</subject><subject>MEMBRANA</subject><subject>MEMBRANE</subject><subject>MEMBRANES</subject><issn>0916-8451</issn><issn>1347-6947</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><recordid>eNptkT1vFDEQhlcIRI5AQ0mBLEGBkPbw565dRlE-QJFIEWpr1vYmDuv1YXsVHb-An41Pd0mBqCyNn3nfmXmb5i3Ba0J78mUYhrXo1grjZ82KMN63neL982aFFelayQU5al7lfI9xLQjysjmiPZVYErJq_pzNv7cBijdok-LGpeJdRnFE5SEiA5PxS2hz8WGZoDiLTm6uIVfCz6jcOTS7pSSYEMwWgfF2J3OJkrv1cc5ojEutH9DgwpBgdmhMYEr937ncLQFmFPz083XzYoQpuzeH97j5cX52c3rZXn2_-Hp6ctUaLlVpmZOUMoWNYsyBsWAcASIooawTdCQDBWsU75ylkjk1WNsJBr2V2PX90I3suPm0163r_lpcLjr4bNw01dHikjXplZCdUhRX9MM_6H1c0lyn04RzxRTnrK_U5z1lUsw5uVFvkg-QtppgvctH13y06HTNp8LvD5LLEJx9Qh8DqcDHAwC5nr_eajY-P3FcKEnlzlTsMT-PMQV4iGmyusB2iumxh_3X_92-b4So4TZV7Nu1Yph1mLO_l-KzbA</recordid><startdate>1992</startdate><enddate>1992</enddate><creator>Kanno, C. (Utsunomiya Univ. (Japan))</creator><creator>Takeda, Y</creator><creator>Cho, J.K</creator><general>Taylor & Francis</general><general>Japan Society for Bioscience Biotechnology and Agrochemistry</general><general>Oxford University Press</general><scope>FBQ</scope><scope>IQODW</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>1992</creationdate><title>Enzymatic properties of two calcium-stimulated ATPases in the neutral and acidic pH regions found in the membrane fraction of human milk</title><author>Kanno, C. (Utsunomiya Univ. (Japan)) ; Takeda, Y ; Cho, J.K</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c489t-3e822390c933eacdace1a152123652f1b2adc946ed283e9bdd653a7d80e77b6f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>ACTIVIDAD ENZIMATICA</topic><topic>ACTIVITE ENZYMATIQUE</topic><topic>ADENOSINA TRIFOSFATASA</topic><topic>ADENOSINE TRIPHOSPHATASE</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Biological and medical sciences</topic><topic>CALCIO</topic><topic>CALCIUM</topic><topic>Enzymes and enzyme inhibitors</topic><topic>ENZYMIC ACTIVITY</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>HUMAN MILK</topic><topic>Hydrolases</topic><topic>LAIT HUMAIN</topic><topic>LECHE HUMANA</topic><topic>MEMBRANA</topic><topic>MEMBRANE</topic><topic>MEMBRANES</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kanno, C. (Utsunomiya Univ. (Japan))</creatorcontrib><creatorcontrib>Takeda, Y</creatorcontrib><creatorcontrib>Cho, J.K</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Bioscience, biotechnology, and biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kanno, C. (Utsunomiya Univ. (Japan))</au><au>Takeda, Y</au><au>Cho, J.K</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Enzymatic properties of two calcium-stimulated ATPases in the neutral and acidic pH regions found in the membrane fraction of human milk</atitle><jtitle>Bioscience, biotechnology, and biochemistry</jtitle><addtitle>Biosci Biotechnol Biochem</addtitle><date>1992</date><risdate>1992</risdate><volume>56</volume><issue>6</issue><spage>900</spage><epage>905</epage><pages>900-905</pages><issn>0916-8451</issn><eissn>1347-6947</eissn><abstract>Two calcium-stimulated ATPases at optimal pH values of 5.0 and 7.0, which are designated as acid and neutral Ca
2+
-ATPase, respectively, were found in the membrane fraction of human milk, and their enzymatic properties were studied. For maximal activity, neutral Ca
2+
-ATPase required 0.45 mM Ca ion, while acid Ca
2+
-ATPase required 207 mM Ca ion. Neutral Ca
2+
-ATPase activity was not enhanced by adding the Mg ion at more than 0.1 mM. Among the nucleotides, neutral Ca
2+
-ATPase showed a higher substrate specificity to GTP, CTP, ITP, and UTP than to ATP, while ATP was the best substrate for acid Ca
2+
-ATPase. Neutral and acid Ca
2+
-ATPases had apparent K
m
values of 0.361 and 0.192 mM, and V
max
of 186 and 178 μmol ATP hydrolyzed/mg of protein per min, respectively. Both Ca
2+
-ATPases were potently inhibited by fluoride, lanthanide, vanadate, and p-chloromercuribenzoate, and inactivated by EDTA, EGTA, and CDTA, but were unaffected by N-ethylmaleimide, NaN
3
, ouabain, oxidized glutathione, or oligomycin, and were inactivated by heating at 60°C for 10 min. These enzymes were concentrated in the membrane fraction of the cream and skim milk membrane.</abstract><cop>Tokyo</cop><pub>Taylor & Francis</pub><pmid>27280811</pmid><doi>10.1271/bbb.56.900</doi><tpages>6</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0916-8451 |
| ispartof | Bioscience, biotechnology, and biochemistry, 1992, Vol.56 (6), p.900-905 |
| issn | 0916-8451 1347-6947 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_1795869920 |
| source | Freely Accessible Japanese Titles - check A-Z of ejournals; Free Full-Text Journals in Chemistry; EZB Electronic Journals Library; J-STAGE |
| subjects | ACTIVIDAD ENZIMATICA ACTIVITE ENZYMATIQUE ADENOSINA TRIFOSFATASA ADENOSINE TRIPHOSPHATASE Analytical, structural and metabolic biochemistry Biological and medical sciences CALCIO CALCIUM Enzymes and enzyme inhibitors ENZYMIC ACTIVITY Fundamental and applied biological sciences. Psychology HUMAN MILK Hydrolases LAIT HUMAIN LECHE HUMANA MEMBRANA MEMBRANE MEMBRANES |
| title | Enzymatic properties of two calcium-stimulated ATPases in the neutral and acidic pH regions found in the membrane fraction of human milk |
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