Isolation and purification of calmodulin from the shrimp, Crangon crangon
Calmodulin was isolated and purified from shrimp abdominal muscle by heat precipitation, ion exchange and hydrophobic interaction chromatography. The purified calmodulin was homogeneous when evaluated by polyacrylamide gel electrophoresis. A still remaining contaminant was eliminated by high perform...
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| Veröffentlicht in: | Life sciences (1973) 1992, Vol.51 (24), p.1881-1889 |
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| container_end_page | 1889 |
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| container_issue | 24 |
| container_start_page | 1881 |
| container_title | Life sciences (1973) |
| container_volume | 51 |
| creator | Michael, Rainer H. Pipkorn, Rüdiger Willig, Axel Jaros, Peter P. |
| description | Calmodulin was isolated and purified from shrimp abdominal muscle by heat precipitation, ion exchange and hydrophobic interaction chromatography. The purified calmodulin was homogeneous when evaluated by polyacrylamide gel electrophoresis. A still remaining contaminant was eliminated by high performance liquid chromatography on a phenyl column. The biological and physicochemical properties of shrimp calmodulin such as amino acid composition, molecular weight and the ability to activate calmodulin-deficient bovine heart phosphodiesterase were compared to those of other invertebrate calmodulins. |
| doi_str_mv | 10.1016/0024-3205(92)90040-V |
| format | Article |
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The purified calmodulin was homogeneous when evaluated by polyacrylamide gel electrophoresis. A still remaining contaminant was eliminated by high performance liquid chromatography on a phenyl column. The biological and physicochemical properties of shrimp calmodulin such as amino acid composition, molecular weight and the ability to activate calmodulin-deficient bovine heart phosphodiesterase were compared to those of other invertebrate calmodulins.</description><identifier>ISSN: 0024-3205</identifier><identifier>EISSN: 1879-0631</identifier><identifier>DOI: 10.1016/0024-3205(92)90040-V</identifier><identifier>PMID: 1333028</identifier><identifier>CODEN: LIFSAK</identifier><language>eng</language><publisher>Amsterdam: Elsevier Inc</publisher><subject>3',5'-Cyclic-AMP Phosphodiesterases - analysis ; Amino Acids - analysis ; Animals ; biochemical analysis ; Biochemistry. Physiology. Immunology ; Biological and medical sciences ; Brackish ; calcium ; Calmodulin - chemistry ; Calmodulin - isolation & purification ; Chromatography, High Pressure Liquid ; Chromatography, Ion Exchange ; Crangon crangon ; Crustacea ; Decapoda (Crustacea) - chemistry ; Electrophoresis, Polyacrylamide Gel ; Enzyme Activation ; Fundamental and applied biological sciences. Psychology ; Invertebrates ; ion transport ; isolation ; Marine ; molecular structure ; Molecular Weight ; Physiology. 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The purified calmodulin was homogeneous when evaluated by polyacrylamide gel electrophoresis. A still remaining contaminant was eliminated by high performance liquid chromatography on a phenyl column. The biological and physicochemical properties of shrimp calmodulin such as amino acid composition, molecular weight and the ability to activate calmodulin-deficient bovine heart phosphodiesterase were compared to those of other invertebrate calmodulins.</description><subject>3',5'-Cyclic-AMP Phosphodiesterases - analysis</subject><subject>Amino Acids - analysis</subject><subject>Animals</subject><subject>biochemical analysis</subject><subject>Biochemistry. Physiology. Immunology</subject><subject>Biological and medical sciences</subject><subject>Brackish</subject><subject>calcium</subject><subject>Calmodulin - chemistry</subject><subject>Calmodulin - isolation & purification</subject><subject>Chromatography, High Pressure Liquid</subject><subject>Chromatography, Ion Exchange</subject><subject>Crangon crangon</subject><subject>Crustacea</subject><subject>Decapoda (Crustacea) - chemistry</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Enzyme Activation</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Invertebrates</subject><subject>ion transport</subject><subject>isolation</subject><subject>Marine</subject><subject>molecular structure</subject><subject>Molecular Weight</subject><subject>Physiology. Development</subject><subject>proteins</subject><subject>purification</subject><issn>0024-3205</issn><issn>1879-0631</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1r3DAQQEVp2GzT_oMGfCihgTrVSLZlXwJhycdCIJd0r0IrjboKtrWR7EL-fbT1srkllxmYeTPMPEK-A70ACtVvSlmRc0bLnw07bygtaL76ROZQiyanFYfPZH5AjsmXGJ8opWUp-IzMgHNOWT0ny2X0rRqc7zPVm2w7BmedngreZlq1nTdj6_rMBt9lwwazuAmu2_7KFkH1fxOmp_yVHFnVRvy2zyfkz8314-Iuv3-4XS6u7nNdgBjyGhmi4UxUa6hECQprAxoEA20bwYQRuEZTCmYs0EoJQFs1ACkYpvW64ifkbNq7Df55xDjIzkWNbat69GOUIr0mBC8-BKFKV5S8TmAxgTr4GANauU0fqvAigcqdarnzKHceZcPkf9VylcZO9_vHdYfmbWhym_o_9n0Vk0ebNGkXD1hR1MCbMmGXE4ZJ2j-HQUbtsNdoXEA9SOPd-3e8AkJQmdE</recordid><startdate>1992</startdate><enddate>1992</enddate><creator>Michael, Rainer H.</creator><creator>Pipkorn, Rüdiger</creator><creator>Willig, Axel</creator><creator>Jaros, Peter P.</creator><general>Elsevier Inc</general><general>Elsevier</general><scope>IQODW</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><scope>7QL</scope><scope>8FD</scope><scope>C1K</scope><scope>F1W</scope><scope>FR3</scope><scope>H95</scope><scope>L.G</scope><scope>M81</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>1992</creationdate><title>Isolation and purification of calmodulin from the shrimp, Crangon crangon</title><author>Michael, Rainer H. ; Pipkorn, Rüdiger ; Willig, Axel ; Jaros, Peter P.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c417t-8e2eed3276b16751ae8d1c1721cf9727d7ebed572df106a71ef6911f69d2ccb63</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>3',5'-Cyclic-AMP Phosphodiesterases - analysis</topic><topic>Amino Acids - analysis</topic><topic>Animals</topic><topic>biochemical analysis</topic><topic>Biochemistry. Physiology. Immunology</topic><topic>Biological and medical sciences</topic><topic>Brackish</topic><topic>calcium</topic><topic>Calmodulin - chemistry</topic><topic>Calmodulin - isolation & purification</topic><topic>Chromatography, High Pressure Liquid</topic><topic>Chromatography, Ion Exchange</topic><topic>Crangon crangon</topic><topic>Crustacea</topic><topic>Decapoda (Crustacea) - chemistry</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Enzyme Activation</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Invertebrates</topic><topic>ion transport</topic><topic>isolation</topic><topic>Marine</topic><topic>molecular structure</topic><topic>Molecular Weight</topic><topic>Physiology. 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The purified calmodulin was homogeneous when evaluated by polyacrylamide gel electrophoresis. A still remaining contaminant was eliminated by high performance liquid chromatography on a phenyl column. The biological and physicochemical properties of shrimp calmodulin such as amino acid composition, molecular weight and the ability to activate calmodulin-deficient bovine heart phosphodiesterase were compared to those of other invertebrate calmodulins.</abstract><cop>Amsterdam</cop><pub>Elsevier Inc</pub><pmid>1333028</pmid><doi>10.1016/0024-3205(92)90040-V</doi><tpages>9</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0024-3205 |
| ispartof | Life sciences (1973), 1992, Vol.51 (24), p.1881-1889 |
| issn | 0024-3205 1879-0631 |
| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals Complete |
| subjects | 3',5'-Cyclic-AMP Phosphodiesterases - analysis Amino Acids - analysis Animals biochemical analysis Biochemistry. Physiology. Immunology Biological and medical sciences Brackish calcium Calmodulin - chemistry Calmodulin - isolation & purification Chromatography, High Pressure Liquid Chromatography, Ion Exchange Crangon crangon Crustacea Decapoda (Crustacea) - chemistry Electrophoresis, Polyacrylamide Gel Enzyme Activation Fundamental and applied biological sciences. Psychology Invertebrates ion transport isolation Marine molecular structure Molecular Weight Physiology. Development proteins purification |
| title | Isolation and purification of calmodulin from the shrimp, Crangon crangon |
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