The nitrate reductase activity of milk xanthine oxidase

Milk xanthine oxidase oxidizes xanthine at pH 9.6 and reduces nitrates at pH 5.2. It is shown that the nitrate reductase activity requires molybdenum and sulfur-containing sites in the enzyme, whereas oxidation of xanthine also requires iron-containing sites and FAD. As the pH changes from 5.2 to 9....

Full description

Saved in:
Bibliographic Details
Published inJournal of applied biochemistry Vol. 7; no. 2; p. 86
Main Authors Sergeev, N S, Ananiadi, L I, L'vov, N P, Kretovich, W L
Format Journal Article
LanguageEnglish
Published United States 01.04.1985
Subjects
Animals
Calcium Chloride - pharmacology
Cattle
Chloromercuribenzoates - pharmacology
Dithioerythritol - pharmacology
Flavin-Adenine Dinucleotide - metabolism
Hot Temperature
Hydrogen-Ion Concentration
Milk - enzymology
Nitrate Reductases - metabolism
p-Chloromercuribenzoic Acid
Protein Conformation
Xanthine Oxidase - metabolism
Online AccessGet more information

Cover

Abstract Milk xanthine oxidase oxidizes xanthine at pH 9.6 and reduces nitrates at pH 5.2. It is shown that the nitrate reductase activity requires molybdenum and sulfur-containing sites in the enzyme, whereas oxidation of xanthine also requires iron-containing sites and FAD. As the pH changes from 5.2 to 9.6, the conformation of the enzyme molecule is modified as demonstrated by changes in the absorption, fluorescence, and circular dichroism spectra. When the enzyme is treated with dithioerythritol, it may pass from the oxidase to the dehydrogenase form with a marked increase in the nitrate reductase activity.
AbstractList Milk xanthine oxidase oxidizes xanthine at pH 9.6 and reduces nitrates at pH 5.2. It is shown that the nitrate reductase activity requires molybdenum and sulfur-containing sites in the enzyme, whereas oxidation of xanthine also requires iron-containing sites and FAD. As the pH changes from 5.2 to 9.6, the conformation of the enzyme molecule is modified as demonstrated by changes in the absorption, fluorescence, and circular dichroism spectra. When the enzyme is treated with dithioerythritol, it may pass from the oxidase to the dehydrogenase form with a marked increase in the nitrate reductase activity.
Author L'vov, N P
Ananiadi, L I
Kretovich, W L
Sergeev, N S
Author_xml – sequence: 1
  givenname: N S
  surname: Sergeev
  fullname: Sergeev, N S
– sequence: 2
  givenname: L I
  surname: Ananiadi
  fullname: Ananiadi, L I
– sequence: 3
  givenname: N P
  surname: L'vov
  fullname: L'vov, N P
– sequence: 4
  givenname: W L
  surname: Kretovich
  fullname: Kretovich, W L
BackLink https://www.ncbi.nlm.nih.gov/pubmed/3840469$$D View this record in MEDLINE/PubMed
BookMark eNotj8tqwzAURLVISdM0n1DQDxj0vtayhL4gkE26DtfWFRGNZWMrJfn7GprVwHCYwzyxRe4zLdhKSCcr0NY8ss00pUaIuQEQZsmWujbCOL9icDgRz6mMWIiPFC5twYk4tiX9pnLjfeRdOv_wK-ZySpl4f01hJp7ZQ8TzRJt7rtn3-9th-1nt9h9f29ddNUglS0VRq0g6Sg8U7OzUIriIkYJ34D0421qUwkJA37gAxiiqa1KGjPSajFqzl__d4dJ0FI7DmDocb8f7AfUHnZxDHw
ContentType Journal Article
DBID CGR
CUY
CVF
ECM
EIF
NPM
DatabaseName Medline
MEDLINE
MEDLINE (Ovid)
MEDLINE
MEDLINE
PubMed
DatabaseTitle MEDLINE
Medline Complete
MEDLINE with Full Text
PubMed
MEDLINE (Ovid)
DatabaseTitleList MEDLINE
Database_xml – sequence: 1
  dbid: NPM
  name: PubMed
  url: https://proxy.k.utb.cz/login?url=http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed
  sourceTypes: Index Database
– sequence: 2
  dbid: EIF
  name: MEDLINE
  url: https://proxy.k.utb.cz/login?url=https://www.webofscience.com/wos/medline/basic-search
  sourceTypes: Index Database
DeliveryMethod no_fulltext_linktorsrc
ExternalDocumentID 3840469
Genre Journal Article
GroupedDBID 3O-
CGR
CUY
CVF
ECM
EIF
NPM
ID FETCH-LOGICAL-p121t-ef32fe3f197ed540430d6fafed96799765c5a1057da9b6d7442e88e24e4193e42
ISSN 0161-7354
IngestDate Thu May 23 22:56:29 EDT 2024
IsPeerReviewed false
IsScholarly false
Issue 2
Language English
LinkModel OpenURL
MergedId FETCHMERGED-LOGICAL-p121t-ef32fe3f197ed540430d6fafed96799765c5a1057da9b6d7442e88e24e4193e42
PMID 3840469
ParticipantIDs pubmed_primary_3840469
PublicationCentury 1900
PublicationDate 1985-Apr
PublicationDateYYYYMMDD 1985-04-01
PublicationDate_xml – month: 04
  year: 1985
  text: 1985-Apr
PublicationDecade 1980
PublicationPlace United States
PublicationPlace_xml – name: United States
PublicationTitle Journal of applied biochemistry
PublicationTitleAlternate J Appl Biochem
PublicationYear 1985
SSID ssib000167704
ssib008531637
Score 1.2114086
Snippet Milk xanthine oxidase oxidizes xanthine at pH 9.6 and reduces nitrates at pH 5.2. It is shown that the nitrate reductase activity requires molybdenum and...
SourceID pubmed
SourceType Index Database
StartPage 86
SubjectTerms Animals
Calcium Chloride - pharmacology
Cattle
Chloromercuribenzoates - pharmacology
Dithioerythritol - pharmacology
Flavin-Adenine Dinucleotide - metabolism
Hot Temperature
Hydrogen-Ion Concentration
Milk - enzymology
Nitrate Reductases - metabolism
p-Chloromercuribenzoic Acid
Protein Conformation
Xanthine Oxidase - metabolism
Title The nitrate reductase activity of milk xanthine oxidase
URI https://www.ncbi.nlm.nih.gov/pubmed/3840469
Volume 7
hasFullText
inHoldings 1
isFullTextHit
isPrint
link http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnZ3LS8QwEMaDDwQvoqj4Jgc9SWWbpk1yFFEWX6dd9CZpM8FFbRcpIv71Tpp0t_hCvZTSlNLm16Zfpv1mCNlPcs50EedIgEHEC9mLtDQ2EpmSzKhCSeXMyVfXWX_Iz2_T27bAeHCX1PlR8falr-Q_VHEbcnUu2T-QnRwUN-A68sUlEsblrxnjI-myPRw-uxysNb6TmvQYL-FPi6fR48PhK_bevVOT1evItF9jPgtS3QrSkaui5cvATQIwzqSJp-funWm09LjU5Ugbb7Cexl8vD5h4qcLOE__YxTPUFY5LTRznJrgdjDfgybTzm0oIQWZxJBKf-rkdQ0XnVmGd8dCnue6gGD81LBKcV3Jfo-XHxg-5sEPLLJkV0g1q193QTJwJ0Zlbog5Brent8uGMF8lCOMKHSUQjJgbLZCl0Oj32SFfIDJSrRCBOGnDSCU7a4qSVpQ4nbXHSgHONDM9OByf9KNS1iMYxi-sIbMIsJDZWAkzq0hv1TGa1BaMyoVAfpkWqXf1lo1WeGcE5AymBceAot4GzdTJXViVsEAosz1NZQGKM4kZqWaRQKJckEZJMW7FJ1v113o198pK70AFb3zVsk8Up9R0yb_FZgV0UXnW-13T4O3rCLsg
link.rule.ids 783
linkProvider National Library of Medicine
openUrl ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=The+nitrate+reductase+activity+of+milk+xanthine+oxidase&rft.jtitle=Journal+of+applied+biochemistry&rft.au=Sergeev%2C+N+S&rft.au=Ananiadi%2C+L+I&rft.au=L%27vov%2C+N+P&rft.au=Kretovich%2C+W+L&rft.date=1985-04-01&rft.issn=0161-7354&rft.volume=7&rft.issue=2&rft.spage=86&rft_id=info%3Apmid%2F3840469&rft_id=info%3Apmid%2F3840469&rft.externalDocID=3840469
thumbnail_l http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0161-7354&client=summon
thumbnail_m http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0161-7354&client=summon
thumbnail_s http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0161-7354&client=summon