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Purification and Characterization of a Neutral Protease from Rat-Liver Cytosolic Fraction
Rat liver cytosol contains a neutral protease which degrades acetylated hemoglobin and some urea-denatured proteins maximally at pH 7.5. The enzyme was purified to homogeneity by conventional chromatographic techniques. It appears to be a metalloprotease since it is inhibited by EDTA and o-phenanthr...
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| Published in: | Journal of biochemistry (Tokyo) 1987-11, Vol.102 (5), p.985-992 |
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| Main Authors: | , |
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| Language: | English |
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| cited_by | cdi_FETCH-LOGICAL-c491t-ec7a75101fe414c8ee71237a637e9c6f2eca53db1617c6dceb0b4d9db70a3a5d3 |
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| container_end_page | 992 |
| container_issue | 5 |
| container_start_page | 985 |
| container_title | Journal of biochemistry (Tokyo) |
| container_volume | 102 |
| creator | HIROI, Yuzo NATORI, Yasuo |
| description | Rat liver cytosol contains a neutral protease which degrades acetylated hemoglobin and some urea-denatured proteins maximally at pH 7.5. The enzyme was purified to homogeneity by conventional chromatographic techniques. It appears to be a metalloprotease since it is inhibited by EDTA and o-phenanthroline, the metaldepleted enzyme can be reactivated by Co2+, Zn2+, Mn2+, or Mg2+, and it is not inhibited by reagents specific for carboxyl, seryl, or thiol proteases. The enzyme has an apparent molecular weight of 200,000 as determined on Sephacryl S-200 column chromatography, and electrophoresis in sodium dodecyl sulfate showed 3 protein bands corresponding to the molecular weights of 110,000, 74,000, and 40,000. |
| doi_str_mv | 10.1093/oxfordjournals.jbchem.a122175 |
| format | article |
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The enzyme was purified to homogeneity by conventional chromatographic techniques. It appears to be a metalloprotease since it is inhibited by EDTA and o-phenanthroline, the metaldepleted enzyme can be reactivated by Co2+, Zn2+, Mn2+, or Mg2+, and it is not inhibited by reagents specific for carboxyl, seryl, or thiol proteases. The enzyme has an apparent molecular weight of 200,000 as determined on Sephacryl S-200 column chromatography, and electrophoresis in sodium dodecyl sulfate showed 3 protein bands corresponding to the molecular weights of 110,000, 74,000, and 40,000.</description><identifier>ISSN: 0021-924X</identifier><identifier>EISSN: 1756-2651</identifier><identifier>DOI: 10.1093/oxfordjournals.jbchem.a122175</identifier><identifier>PMID: 3125167</identifier><identifier>CODEN: JOBIAO</identifier><language>eng</language><publisher>Oxford: Oxford University Press</publisher><subject>Analytical, structural and metabolic biochemistry ; Animals ; Biological and medical sciences ; Cations, Divalent ; Chromatography ; Chromatography, Gel ; Cytosol - enzymology ; Edetic Acid - pharmacology ; Endopeptidases - isolation & purification ; Enzyme Activation - drug effects ; Enzyme Reactivators ; Enzymes and enzyme inhibitors ; Fundamental and applied biological sciences. Psychology ; Hydrogen-Ion Concentration ; Hydrolases ; Liver - enzymology ; livers ; Male ; Metals - pharmacology ; Molecular Weight ; Neprilysin ; neutral proteinase ; Phenanthrolines - pharmacology ; Protease Inhibitors ; proteinase ; Rats ; Rats, Inbred Strains ; Substrate Specificity</subject><ispartof>Journal of biochemistry (Tokyo), 1987-11, Vol.102 (5), p.985-992</ispartof><rights>1988 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c491t-ec7a75101fe414c8ee71237a637e9c6f2eca53db1617c6dceb0b4d9db70a3a5d3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=7444114$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/3125167$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>HIROI, Yuzo</creatorcontrib><creatorcontrib>NATORI, Yasuo</creatorcontrib><title>Purification and Characterization of a Neutral Protease from Rat-Liver Cytosolic Fraction</title><title>Journal of biochemistry (Tokyo)</title><addtitle>J Biochem</addtitle><description>Rat liver cytosol contains a neutral protease which degrades acetylated hemoglobin and some urea-denatured proteins maximally at pH 7.5. The enzyme was purified to homogeneity by conventional chromatographic techniques. It appears to be a metalloprotease since it is inhibited by EDTA and o-phenanthroline, the metaldepleted enzyme can be reactivated by Co2+, Zn2+, Mn2+, or Mg2+, and it is not inhibited by reagents specific for carboxyl, seryl, or thiol proteases. The enzyme has an apparent molecular weight of 200,000 as determined on Sephacryl S-200 column chromatography, and electrophoresis in sodium dodecyl sulfate showed 3 protein bands corresponding to the molecular weights of 110,000, 74,000, and 40,000.</description><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Cations, Divalent</subject><subject>Chromatography</subject><subject>Chromatography, Gel</subject><subject>Cytosol - enzymology</subject><subject>Edetic Acid - pharmacology</subject><subject>Endopeptidases - isolation & purification</subject><subject>Enzyme Activation - drug effects</subject><subject>Enzyme Reactivators</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Hydrogen-Ion Concentration</subject><subject>Hydrolases</subject><subject>Liver - enzymology</subject><subject>livers</subject><subject>Male</subject><subject>Metals - pharmacology</subject><subject>Molecular Weight</subject><subject>Neprilysin</subject><subject>neutral proteinase</subject><subject>Phenanthrolines - pharmacology</subject><subject>Protease Inhibitors</subject><subject>proteinase</subject><subject>Rats</subject><subject>Rats, Inbred Strains</subject><subject>Substrate Specificity</subject><issn>0021-924X</issn><issn>1756-2651</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1987</creationdate><recordtype>article</recordtype><recordid>eNqFkUFv1DAQhS0EKtvCT0DyAbhlsWPHbg4cUERbpIUuqJVKL9bEGatekrjYCWr59WSVaCVOvXhkv--NR_MIecfZmrNSfAgPLsRmF8bYQ5vWu9reYbcGnudcF8_IajpVlquCPycrxnKelbm8eUmOU9rtr7kQR-RI8LzgSq_Iz-0YvfMWBh96Cn1DqzuIYAeM_u_8GBwF-g3HIUJLtzEMCAmpi6GjP2DINv4PRlo9DiGF1lt6tndPvlfkhZsGxNdLPSHXZ5-vqotsc3n-pfq0yaws-ZCh1aALzrhDyaU9RdTTjBqU0Fha5XK0UIim5oprqxqLNatlUza1ZiCgaMQJeT_3vY_h94hpMJ1PFtsWegxjMlqXBdOlehLkBWOnuWQT-HEGbQwpRXTmPvoO4qPhzOwzMP9nYOYMzJLB5H-zfDTWHTYH97L0SX-76JAstC5Cb306YFpKybmcsGzGfBrw4SBD_GWmJrowFze35nulmLj9ujVM_AN6cKfb</recordid><startdate>19871101</startdate><enddate>19871101</enddate><creator>HIROI, Yuzo</creator><creator>NATORI, Yasuo</creator><general>Oxford University Press</general><scope>BSCLL</scope><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>FR3</scope><scope>M81</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>19871101</creationdate><title>Purification and Characterization of a Neutral Protease from Rat-Liver Cytosolic Fraction</title><author>HIROI, Yuzo ; NATORI, Yasuo</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c491t-ec7a75101fe414c8ee71237a637e9c6f2eca53db1617c6dceb0b4d9db70a3a5d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1987</creationdate><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Cations, Divalent</topic><topic>Chromatography</topic><topic>Chromatography, Gel</topic><topic>Cytosol - enzymology</topic><topic>Edetic Acid - pharmacology</topic><topic>Endopeptidases - isolation & purification</topic><topic>Enzyme Activation - drug effects</topic><topic>Enzyme Reactivators</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Hydrogen-Ion Concentration</topic><topic>Hydrolases</topic><topic>Liver - enzymology</topic><topic>livers</topic><topic>Male</topic><topic>Metals - pharmacology</topic><topic>Molecular Weight</topic><topic>Neprilysin</topic><topic>neutral proteinase</topic><topic>Phenanthrolines - pharmacology</topic><topic>Protease Inhibitors</topic><topic>proteinase</topic><topic>Rats</topic><topic>Rats, Inbred Strains</topic><topic>Substrate Specificity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>HIROI, Yuzo</creatorcontrib><creatorcontrib>NATORI, Yasuo</creatorcontrib><collection>Istex</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 3</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of biochemistry (Tokyo)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>HIROI, Yuzo</au><au>NATORI, Yasuo</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification and Characterization of a Neutral Protease from Rat-Liver Cytosolic Fraction</atitle><jtitle>Journal of biochemistry (Tokyo)</jtitle><addtitle>J Biochem</addtitle><date>1987-11-01</date><risdate>1987</risdate><volume>102</volume><issue>5</issue><spage>985</spage><epage>992</epage><pages>985-992</pages><issn>0021-924X</issn><eissn>1756-2651</eissn><coden>JOBIAO</coden><abstract>Rat liver cytosol contains a neutral protease which degrades acetylated hemoglobin and some urea-denatured proteins maximally at pH 7.5. The enzyme was purified to homogeneity by conventional chromatographic techniques. It appears to be a metalloprotease since it is inhibited by EDTA and o-phenanthroline, the metaldepleted enzyme can be reactivated by Co2+, Zn2+, Mn2+, or Mg2+, and it is not inhibited by reagents specific for carboxyl, seryl, or thiol proteases. The enzyme has an apparent molecular weight of 200,000 as determined on Sephacryl S-200 column chromatography, and electrophoresis in sodium dodecyl sulfate showed 3 protein bands corresponding to the molecular weights of 110,000, 74,000, and 40,000.</abstract><cop>Oxford</cop><pub>Oxford University Press</pub><pmid>3125167</pmid><doi>10.1093/oxfordjournals.jbchem.a122175</doi><tpages>8</tpages></addata></record> |
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| identifier | ISSN: 0021-924X |
| ispartof | Journal of biochemistry (Tokyo), 1987-11, Vol.102 (5), p.985-992 |
| issn | 0021-924X 1756-2651 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_77950796 |
| source | J-STAGE Free Content; Oxford University Press Archive |
| subjects | Analytical, structural and metabolic biochemistry Animals Biological and medical sciences Cations, Divalent Chromatography Chromatography, Gel Cytosol - enzymology Edetic Acid - pharmacology Endopeptidases - isolation & purification Enzyme Activation - drug effects Enzyme Reactivators Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Hydrogen-Ion Concentration Hydrolases Liver - enzymology livers Male Metals - pharmacology Molecular Weight Neprilysin neutral proteinase Phenanthrolines - pharmacology Protease Inhibitors proteinase Rats Rats, Inbred Strains Substrate Specificity |
| title | Purification and Characterization of a Neutral Protease from Rat-Liver Cytosolic Fraction |
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