Purification and properties of trout gill AMP deaminase
The AMp deaminase has been purified 450-500 fold from 20,000 g supernatants from trout gill. The procedure comprised cellulose phosphate and DEAE-cellulose chromatography. The gill appeared to contain different isoenzymes as indicated by different chromatographic behavior on cellulose phosphate and...
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| Veröffentlicht in: | Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology Biochemical, systemic, and environmental physiology, 1984, Vol.154 (1), p.55-63 |
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| container_end_page | 63 |
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| container_title | Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology |
| container_volume | 154 |
| creator | RAFFIN, J.-P |
| description | The AMp deaminase has been purified 450-500 fold from 20,000 g supernatants from trout gill. The procedure comprised cellulose phosphate and DEAE-cellulose chromatography. The gill appeared to contain different isoenzymes as indicated by different chromatographic behavior on cellulose phosphate and different heat stabilities. The two major isoenzymes were compared with respect to their pH optima and the effect of temperature. ATP and inorganic phosphate. The pH opitmum is about pH 6.7 at low substrate concentration. A second optimum is found in phosphate buffer. The substrate saturation curve is hyperbolic, even in the absence of KCl or ATP. ATP is an activator of the enzyme in the absence of KCl, but is without effect in the presence of monovalent cations. Among the monovalent cations tested, Na super(+) is the most potent activator followed by K super(+) and NH super(+)d4. |
| doi_str_mv | 10.1007/BF00683216 |
| format | Article |
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The procedure comprised cellulose phosphate and DEAE-cellulose chromatography. The gill appeared to contain different isoenzymes as indicated by different chromatographic behavior on cellulose phosphate and different heat stabilities. The two major isoenzymes were compared with respect to their pH optima and the effect of temperature. ATP and inorganic phosphate. The pH opitmum is about pH 6.7 at low substrate concentration. A second optimum is found in phosphate buffer. The substrate saturation curve is hyperbolic, even in the absence of KCl or ATP. ATP is an activator of the enzyme in the absence of KCl, but is without effect in the presence of monovalent cations. Among the monovalent cations tested, Na super(+) is the most potent activator followed by K super(+) and NH super(+)d4.</description><identifier>ISSN: 0174-1578</identifier><identifier>EISSN: 1432-136X</identifier><identifier>DOI: 10.1007/BF00683216</identifier><identifier>CODEN: JPBPDL</identifier><language>eng</language><publisher>Berlin: Springer</publisher><subject>AMP ; AMP deaminase ; Biological and medical sciences ; deamination ; enzymatic activity ; Freshwater ; Fundamental and applied biological sciences. Psychology ; gills ; isoenzymes ; Respiratory system: anatomy, metabolism, gas exchange, ventilatory mechanics, respiratory hemodynamics ; Salmo gairdneri ; Vertebrates: respiratory system ; Water and amphibous breathing</subject><ispartof>Journal of comparative physiology. 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B, Biochemical, systemic, and environmental physiology</title><description>The AMp deaminase has been purified 450-500 fold from 20,000 g supernatants from trout gill. The procedure comprised cellulose phosphate and DEAE-cellulose chromatography. The gill appeared to contain different isoenzymes as indicated by different chromatographic behavior on cellulose phosphate and different heat stabilities. The two major isoenzymes were compared with respect to their pH optima and the effect of temperature. ATP and inorganic phosphate. The pH opitmum is about pH 6.7 at low substrate concentration. A second optimum is found in phosphate buffer. The substrate saturation curve is hyperbolic, even in the absence of KCl or ATP. ATP is an activator of the enzyme in the absence of KCl, but is without effect in the presence of monovalent cations. Among the monovalent cations tested, Na super(+) is the most potent activator followed by K super(+) and NH super(+)d4.</description><subject>AMP</subject><subject>AMP deaminase</subject><subject>Biological and medical sciences</subject><subject>deamination</subject><subject>enzymatic activity</subject><subject>Freshwater</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>gills</subject><subject>isoenzymes</subject><subject>Respiratory system: anatomy, metabolism, gas exchange, ventilatory mechanics, respiratory hemodynamics</subject><subject>Salmo gairdneri</subject><subject>Vertebrates: respiratory system</subject><subject>Water and amphibous breathing</subject><issn>0174-1578</issn><issn>1432-136X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1984</creationdate><recordtype>article</recordtype><recordid>eNpFkD1PwzAYhC0EEqWw8As8IAakwPvajj_GgiggFdGhA1vkODYySpNiJwP_nqBWMN1wz51OR8glwi0CqLv7JYDUnKE8IjMUnBXI5fsxmQEqUWCp9Ck5y_kTAARqMSNqPaYYorND7Dtqu4buUr_zaYg-0z7QIfXjQD9i29LF65o23m5jZ7M_JyfBttlfHHRONsvHzcNzsXp7enlYrArHtBkKLxQHtIAoHLdKlCUDr0xta103omk4C9IYkME5znwZ6hqNk9rVODnG8Tm53tdOq75Gn4dqG7PzbWs734-5Qq4lLzVM4M0edKnPOflQ7VLc2vRdIVS_11T_10zw1aHVZmfbkGznYv5LGCkUA-A_FAZhwg</recordid><startdate>1984</startdate><enddate>1984</enddate><creator>RAFFIN, J.-P</creator><general>Springer</general><scope>IQODW</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>C1K</scope><scope>F1W</scope><scope>H95</scope><scope>L.G</scope></search><sort><creationdate>1984</creationdate><title>Purification and properties of trout gill AMP deaminase</title><author>RAFFIN, J.-P</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c289t-e47301a0114c3a745520e79bab8bd4dd32f69906fcc32e5fbb19c68cb132f9c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1984</creationdate><topic>AMP</topic><topic>AMP deaminase</topic><topic>Biological and medical sciences</topic><topic>deamination</topic><topic>enzymatic activity</topic><topic>Freshwater</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>gills</topic><topic>isoenzymes</topic><topic>Respiratory system: anatomy, metabolism, gas exchange, ventilatory mechanics, respiratory hemodynamics</topic><topic>Salmo gairdneri</topic><topic>Vertebrates: respiratory system</topic><topic>Water and amphibous breathing</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>RAFFIN, J.-P</creatorcontrib><collection>Pascal-Francis</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 1: Biological Sciences & Living Resources</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Professional</collection><jtitle>Journal of comparative physiology. 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The two major isoenzymes were compared with respect to their pH optima and the effect of temperature. ATP and inorganic phosphate. The pH opitmum is about pH 6.7 at low substrate concentration. A second optimum is found in phosphate buffer. The substrate saturation curve is hyperbolic, even in the absence of KCl or ATP. ATP is an activator of the enzyme in the absence of KCl, but is without effect in the presence of monovalent cations. Among the monovalent cations tested, Na super(+) is the most potent activator followed by K super(+) and NH super(+)d4.</abstract><cop>Berlin</cop><pub>Springer</pub><doi>10.1007/BF00683216</doi><tpages>9</tpages></addata></record> |
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| ispartof | Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology, 1984, Vol.154 (1), p.55-63 |
| issn | 0174-1578 1432-136X |
| language | eng |
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| subjects | AMP AMP deaminase Biological and medical sciences deamination enzymatic activity Freshwater Fundamental and applied biological sciences. Psychology gills isoenzymes Respiratory system: anatomy, metabolism, gas exchange, ventilatory mechanics, respiratory hemodynamics Salmo gairdneri Vertebrates: respiratory system Water and amphibous breathing |
| title | Purification and properties of trout gill AMP deaminase |
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