Partial Purification and Properties of a Nuclease from Chicken Pancreas
A nuclease has been isolated from an acid homogenate of chicken pancreas and purified over 300-fold. The purified preparation was free of phosphomonoesterase and phosphodiesterase activity, but rapidly hydrolyzed ribonucleic acid and deoxyribonucleic acid. The enzyme which by several criteria was a...
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| Veröffentlicht in: | The Journal of biological chemistry 1966-07, Vol.241 (13), p.3063-3069 |
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| container_title | The Journal of biological chemistry |
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| creator | Eley, J Roth, J S |
| description | A nuclease has been isolated from an acid homogenate of chicken pancreas and purified over 300-fold. The purified preparation
was free of phosphomonoesterase and phosphodiesterase activity, but rapidly hydrolyzed ribonucleic acid and deoxyribonucleic
acid. The enzyme which by several criteria was a single protein required Mg ++ or Mn ++ for activity; addition of excess ethylenediaminetetraacetate completely inhibited all of the nuclease action. The pH optimum
for RNA was around 9.5 and for DNA around 8.8. The enzyme was found to be completely inactivated by heating for 10 min at
70°, but on heating at 80° from one-quarter to one-third of the activity was restored. There appeared to be no free sulfhydryl
groups essential for enzyme activity. Iodoacetate at the proper concentration completely inhibited ribonuclease activity,
but had little or no effect on deoxyribonuclease activity. |
| doi_str_mv | 10.1016/S0021-9258(18)96498-7 |
| format | Article |
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was free of phosphomonoesterase and phosphodiesterase activity, but rapidly hydrolyzed ribonucleic acid and deoxyribonucleic
acid. The enzyme which by several criteria was a single protein required Mg ++ or Mn ++ for activity; addition of excess ethylenediaminetetraacetate completely inhibited all of the nuclease action. The pH optimum
for RNA was around 9.5 and for DNA around 8.8. The enzyme was found to be completely inactivated by heating for 10 min at
70°, but on heating at 80° from one-quarter to one-third of the activity was restored. There appeared to be no free sulfhydryl
groups essential for enzyme activity. Iodoacetate at the proper concentration completely inhibited ribonuclease activity,
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was free of phosphomonoesterase and phosphodiesterase activity, but rapidly hydrolyzed ribonucleic acid and deoxyribonucleic
acid. The enzyme which by several criteria was a single protein required Mg ++ or Mn ++ for activity; addition of excess ethylenediaminetetraacetate completely inhibited all of the nuclease action. The pH optimum
for RNA was around 9.5 and for DNA around 8.8. The enzyme was found to be completely inactivated by heating for 10 min at
70°, but on heating at 80° from one-quarter to one-third of the activity was restored. There appeared to be no free sulfhydryl
groups essential for enzyme activity. Iodoacetate at the proper concentration completely inhibited ribonuclease activity,
but had little or no effect on deoxyribonuclease activity.</description><subject>Animals</subject><subject>Chromatography, Ion Exchange</subject><subject>Deoxyribonucleases - metabolism</subject><subject>Dialysis</subject><subject>In Vitro Techniques</subject><subject>Pancreas - enzymology</subject><subject>Poultry</subject><subject>Ribonucleases - metabolism</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1966</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kFtLAzEQhYMotVZ_QiEgiD6sZjbZbPIoRatQdEEF30KaTWx0LzXZRfz3bi84LwNzzpkDH0JTINdAgN-8EJJCItNMXIK4kpxJkeQHaAxE0IRm8H6Ixv-WY3QS4ycZhkkYoVEmIQXCxmhe6NB5XeGiD955ozvfNlg3JS5Cu7aDZiNuHdb4qTeV1dFiF9oaz1befNkGF7oxYTifoiOnq2jP9nuC3u7vXmcPyeJ5_ji7XSSG5rJLZFlaSXImiYAsK5lmHAwxnBOngRmdO5o70FpInvIS3JLKFHKjTZk7JoykE3Sx-7sO7XdvY6dqH42tKt3Yto9KsBSAcToYs53RhDbGYJ1aB1_r8KuAqA1AtQWoNnQUCLUFqPIhN90X9Mvalv-pPbFBP9_pK_-x-vHBqqVvzcrWKmWggCpKhvY_UtB2ug</recordid><startdate>19660710</startdate><enddate>19660710</enddate><creator>Eley, J</creator><creator>Roth, J S</creator><general>American Society for Biochemistry and Molecular Biology</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>19660710</creationdate><title>Partial Purification and Properties of a Nuclease from Chicken Pancreas</title><author>Eley, J ; Roth, J S</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c379t-9dde9074908155d4a461c0c660fa14ca7f37f1aa89626d1fb39217cacd7f48c93</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1966</creationdate><topic>Animals</topic><topic>Chromatography, Ion Exchange</topic><topic>Deoxyribonucleases - metabolism</topic><topic>Dialysis</topic><topic>In Vitro Techniques</topic><topic>Pancreas - enzymology</topic><topic>Poultry</topic><topic>Ribonucleases - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Eley, J</creatorcontrib><creatorcontrib>Roth, J S</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>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Eley, J</au><au>Roth, J S</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Partial Purification and Properties of a Nuclease from Chicken Pancreas</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1966-07-10</date><risdate>1966</risdate><volume>241</volume><issue>13</issue><spage>3063</spage><epage>3069</epage><pages>3063-3069</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>A nuclease has been isolated from an acid homogenate of chicken pancreas and purified over 300-fold. The purified preparation
was free of phosphomonoesterase and phosphodiesterase activity, but rapidly hydrolyzed ribonucleic acid and deoxyribonucleic
acid. The enzyme which by several criteria was a single protein required Mg ++ or Mn ++ for activity; addition of excess ethylenediaminetetraacetate completely inhibited all of the nuclease action. The pH optimum
for RNA was around 9.5 and for DNA around 8.8. The enzyme was found to be completely inactivated by heating for 10 min at
70°, but on heating at 80° from one-quarter to one-third of the activity was restored. There appeared to be no free sulfhydryl
groups essential for enzyme activity. Iodoacetate at the proper concentration completely inhibited ribonuclease activity,
but had little or no effect on deoxyribonuclease activity.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>5912104</pmid><doi>10.1016/S0021-9258(18)96498-7</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
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| ispartof | The Journal of biological chemistry, 1966-07, Vol.241 (13), p.3063-3069 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_84211463 |
| source | MEDLINE; Alma/SFX Local Collection; EZB Electronic Journals Library |
| subjects | Animals Chromatography, Ion Exchange Deoxyribonucleases - metabolism Dialysis In Vitro Techniques Pancreas - enzymology Poultry Ribonucleases - metabolism |
| title | Partial Purification and Properties of a Nuclease from Chicken Pancreas |
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