Loading…

Purification and Some Properties of Nitrite Reductase from Clostridium perfringens

Nitrite reductase from Clostridium perfringens was purified by chromatographies on DEAE-cellulose, DEAE-Sephadex, Sephadex G-150, and hydroxylapatite and by isoelectric focussing to a homogeneous state, showing essentially a single protein band in disc gel electrophoresis and a single immuno-precipi...

Full description

Saved in:

Bibliographic Details
Published in:	Journal of biochemistry (Tokyo) 1983-01, Vol.94 (4), p.1053-1059
Main Authors:	SEKIGUCHI, Satoshi, SEKI, Sachiko, ISHIMOTO, Makoto
Format:	Article
Language:	English
Subjects:	Clostridium perfringens Clostridium perfringens - enzymology Electron Transport Immunodiffusion Kinetics Molecular Weight NADH, NADPH Oxidoreductases - isolation & purification nitrite reductase Nitrite Reductases - isolation & purification Nitrite Reductases - metabolism Species Specificity
Online Access:	Get full text
Tags:	Add Tag No Tags, Be the first to tag this record!

cited_by
cites
container_end_page	1059
container_issue	4
container_start_page	1053
container_title	Journal of biochemistry (Tokyo)
container_volume	94
creator	SEKIGUCHI, Satoshi SEKI, Sachiko ISHIMOTO, Makoto
description	Nitrite reductase from Clostridium perfringens was purified by chromatographies on DEAE-cellulose, DEAE-Sephadex, Sephadex G-150, and hydroxylapatite and by isoelectric focussing to a homogeneous state, showing essentially a single protein band in disc gel electrophoresis and a single immuno-precipitation line in double diffusion against antiserum obtained from immunized rabbits. The reductase was induced in the presence of nitrate. It had a molecular weight of 54,000 and showed no absorption peak in the visible region. The pH optimum was 6.2 and Km for nitrite was 5 mM. Ferredoxin, as well as viologen dyes, was found to be an electron donor. The product of nitrite reduction was hydroxylamine. This reductase was inhibited by o-phenanthroline and azide but not by cyanide or diethyldithiocarbamate.
doi_str_mv	10.1093/oxfordjournals.jbchem.a134447
format	article
fullrecord	<record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_proquest_miscellaneous_80815242</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>13734526</sourcerecordid><originalsourceid>FETCH-LOGICAL-i373t-3eb7046314a396b91d53f864f71e494165bc5d0f7c558599a641002f002395bf3</originalsourceid><addsrcrecordid>eNqFkM9LwzAUx3NQ5pz-CUIueutsml_NUaZ1wtAxFYaXkraJZrbNTFKY_72RDa8eHo_H58Pj-x4AlyidolTga7vT1jUbO7hetn66qeoP1U0lwoQQfgTGaZqhRGRkfQJOvd_8jhnGIzBiGHHG0BisloMz2tQyGNtD2Tfw2XYKLp3dKheM8tBq-GiCM0HBlWqGOkivoHa2g7PW-ggaM3Qw2tqZ_l31_gwc65hGnR_6BLwWdy-zebJ4un-Y3SwSgzkOCVYVT0kMQiQWrBKooVjnjGiOFBEEMVrVtEk1rynNqRCSERQP0LGwoJXGE3C137t19mtQPpSd8bVqW9krO_gyT3NEM5L9K6KYh9CMRfHiIA5Vp5py60wn3Xd5-FbkyZ4bH9TuD0v3WTKOOS3n67cSZbcpKYqiXOAfiGF_VQ</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>13734526</pqid></control><display><type>article</type><title>Purification and Some Properties of Nitrite Reductase from Clostridium perfringens</title><source>J-STAGE Freely Available Titles - English</source><source>Oxford University Press:Jisc Collections:Oxford Journal Archive: Access period 2024-2025</source><creator>SEKIGUCHI, Satoshi ; SEKI, Sachiko ; ISHIMOTO, Makoto</creator><creatorcontrib>SEKIGUCHI, Satoshi ; SEKI, Sachiko ; ISHIMOTO, Makoto</creatorcontrib><description>Nitrite reductase from Clostridium perfringens was purified by chromatographies on DEAE-cellulose, DEAE-Sephadex, Sephadex G-150, and hydroxylapatite and by isoelectric focussing to a homogeneous state, showing essentially a single protein band in disc gel electrophoresis and a single immuno-precipitation line in double diffusion against antiserum obtained from immunized rabbits. The reductase was induced in the presence of nitrate. It had a molecular weight of 54,000 and showed no absorption peak in the visible region. The pH optimum was 6.2 and Km for nitrite was 5 mM. Ferredoxin, as well as viologen dyes, was found to be an electron donor. The product of nitrite reduction was hydroxylamine. This reductase was inhibited by o-phenanthroline and azide but not by cyanide or diethyldithiocarbamate.</description><identifier>ISSN: 0021-924X</identifier><identifier>DOI: 10.1093/oxfordjournals.jbchem.a134447</identifier><identifier>PMID: 6317661</identifier><language>eng</language><publisher>England: Oxford University Press</publisher><subject>Clostridium perfringens ; Clostridium perfringens - enzymology ; Electron Transport ; Immunodiffusion ; Kinetics ; Molecular Weight ; NADH, NADPH Oxidoreductases - isolation & purification ; nitrite reductase ; Nitrite Reductases - isolation & purification ; Nitrite Reductases - metabolism ; Species Specificity</subject><ispartof>Journal of biochemistry (Tokyo), 1983-01, Vol.94 (4), p.1053-1059</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/6317661$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>SEKIGUCHI, Satoshi</creatorcontrib><creatorcontrib>SEKI, Sachiko</creatorcontrib><creatorcontrib>ISHIMOTO, Makoto</creatorcontrib><title>Purification and Some Properties of Nitrite Reductase from Clostridium perfringens</title><title>Journal of biochemistry (Tokyo)</title><addtitle>J Biochem</addtitle><description>Nitrite reductase from Clostridium perfringens was purified by chromatographies on DEAE-cellulose, DEAE-Sephadex, Sephadex G-150, and hydroxylapatite and by isoelectric focussing to a homogeneous state, showing essentially a single protein band in disc gel electrophoresis and a single immuno-precipitation line in double diffusion against antiserum obtained from immunized rabbits. The reductase was induced in the presence of nitrate. It had a molecular weight of 54,000 and showed no absorption peak in the visible region. The pH optimum was 6.2 and Km for nitrite was 5 mM. Ferredoxin, as well as viologen dyes, was found to be an electron donor. The product of nitrite reduction was hydroxylamine. This reductase was inhibited by o-phenanthroline and azide but not by cyanide or diethyldithiocarbamate.</description><subject>Clostridium perfringens</subject><subject>Clostridium perfringens - enzymology</subject><subject>Electron Transport</subject><subject>Immunodiffusion</subject><subject>Kinetics</subject><subject>Molecular Weight</subject><subject>NADH, NADPH Oxidoreductases - isolation & purification</subject><subject>nitrite reductase</subject><subject>Nitrite Reductases - isolation & purification</subject><subject>Nitrite Reductases - metabolism</subject><subject>Species Specificity</subject><issn>0021-924X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1983</creationdate><recordtype>article</recordtype><recordid>eNqFkM9LwzAUx3NQ5pz-CUIueutsml_NUaZ1wtAxFYaXkraJZrbNTFKY_72RDa8eHo_H58Pj-x4AlyidolTga7vT1jUbO7hetn66qeoP1U0lwoQQfgTGaZqhRGRkfQJOvd_8jhnGIzBiGHHG0BisloMz2tQyGNtD2Tfw2XYKLp3dKheM8tBq-GiCM0HBlWqGOkivoHa2g7PW-ggaM3Qw2tqZ_l31_gwc65hGnR_6BLwWdy-zebJ4un-Y3SwSgzkOCVYVT0kMQiQWrBKooVjnjGiOFBEEMVrVtEk1rynNqRCSERQP0LGwoJXGE3C137t19mtQPpSd8bVqW9krO_gyT3NEM5L9K6KYh9CMRfHiIA5Vp5py60wn3Xd5-FbkyZ4bH9TuD0v3WTKOOS3n67cSZbcpKYqiXOAfiGF_VQ</recordid><startdate>19830101</startdate><enddate>19830101</enddate><creator>SEKIGUCHI, Satoshi</creator><creator>SEKI, Sachiko</creator><creator>ISHIMOTO, Makoto</creator><general>Oxford University Press</general><scope>BSCLL</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7QL</scope><scope>C1K</scope><scope>7X8</scope></search><sort><creationdate>19830101</creationdate><title>Purification and Some Properties of Nitrite Reductase from Clostridium perfringens</title><author>SEKIGUCHI, Satoshi ; SEKI, Sachiko ; ISHIMOTO, Makoto</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-i373t-3eb7046314a396b91d53f864f71e494165bc5d0f7c558599a641002f002395bf3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1983</creationdate><topic>Clostridium perfringens</topic><topic>Clostridium perfringens - enzymology</topic><topic>Electron Transport</topic><topic>Immunodiffusion</topic><topic>Kinetics</topic><topic>Molecular Weight</topic><topic>NADH, NADPH Oxidoreductases - isolation & purification</topic><topic>nitrite reductase</topic><topic>Nitrite Reductases - isolation & purification</topic><topic>Nitrite Reductases - metabolism</topic><topic>Species Specificity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>SEKIGUCHI, Satoshi</creatorcontrib><creatorcontrib>SEKI, Sachiko</creatorcontrib><creatorcontrib>ISHIMOTO, Makoto</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of biochemistry (Tokyo)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>SEKIGUCHI, Satoshi</au><au>SEKI, Sachiko</au><au>ISHIMOTO, Makoto</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification and Some Properties of Nitrite Reductase from Clostridium perfringens</atitle><jtitle>Journal of biochemistry (Tokyo)</jtitle><addtitle>J Biochem</addtitle><date>1983-01-01</date><risdate>1983</risdate><volume>94</volume><issue>4</issue><spage>1053</spage><epage>1059</epage><pages>1053-1059</pages><issn>0021-924X</issn><abstract>Nitrite reductase from Clostridium perfringens was purified by chromatographies on DEAE-cellulose, DEAE-Sephadex, Sephadex G-150, and hydroxylapatite and by isoelectric focussing to a homogeneous state, showing essentially a single protein band in disc gel electrophoresis and a single immuno-precipitation line in double diffusion against antiserum obtained from immunized rabbits. The reductase was induced in the presence of nitrate. It had a molecular weight of 54,000 and showed no absorption peak in the visible region. The pH optimum was 6.2 and Km for nitrite was 5 mM. Ferredoxin, as well as viologen dyes, was found to be an electron donor. The product of nitrite reduction was hydroxylamine. This reductase was inhibited by o-phenanthroline and azide but not by cyanide or diethyldithiocarbamate.</abstract><cop>England</cop><pub>Oxford University Press</pub><pmid>6317661</pmid><doi>10.1093/oxfordjournals.jbchem.a134447</doi><tpages>7</tpages></addata></record>
fulltext	fulltext
identifier	ISSN: 0021-924X
ispartof	Journal of biochemistry (Tokyo), 1983-01, Vol.94 (4), p.1053-1059
issn	0021-924X
language	eng
recordid	cdi_proquest_miscellaneous_80815242
source	J-STAGE Freely Available Titles - English; Oxford University Press:Jisc Collections:Oxford Journal Archive: Access period 2024-2025
subjects	Clostridium perfringens Clostridium perfringens - enzymology Electron Transport Immunodiffusion Kinetics Molecular Weight NADH, NADPH Oxidoreductases - isolation & purification nitrite reductase Nitrite Reductases - isolation & purification Nitrite Reductases - metabolism Species Specificity
title	Purification and Some Properties of Nitrite Reductase from Clostridium perfringens
url	http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-28T01%3A54%3A00IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Purification%20and%20Some%20Properties%20of%20Nitrite%20Reductase%20from%20Clostridium%20perfringens&rft.jtitle=Journal%20of%20biochemistry%20(Tokyo)&rft.au=SEKIGUCHI,%20Satoshi&rft.date=1983-01-01&rft.volume=94&rft.issue=4&rft.spage=1053&rft.epage=1059&rft.pages=1053-1059&rft.issn=0021-924X&rft_id=info:doi/10.1093/oxfordjournals.jbchem.a134447&rft_dat=%3Cproquest_pubme%3E13734526%3C/proquest_pubme%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-i373t-3eb7046314a396b91d53f864f71e494165bc5d0f7c558599a641002f002395bf3%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=13734526&rft_id=info:pmid/6317661&rfr_iscdi=true