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Noncovalent binding of 4-nitroquinoline-N-oxide to proteins

Journal Article:

Abstract

Binding of 4NQO to various kinds of enzymes or proteins was studied. Each one of proteins was mixed with 4NQO in 0.4 mM NaHCO/sub 3/ solution and eluted through Ultrogel AcA 22 column. Radioactivity of /sup 14/C-labeled 4NQO found in protein fraction was measured. 4NQO bound hardly to polyglutamic acid and polyaspertic acid, somewhat to serum albumin, insulin, trypsin, RNA polymerase and DNA polymerase, and markedly to ureas which is an SH enzyme. Lactate dehydrogenase, one of SH enzymes, aggregated with 4NQO. The binding of SH enzyme with the N-oxide would be attributable to a noncovalent binding such as >N-O---H-S-, because 4NQO-urease binding yield markedly decreased in the presence of sodium dodecyl sulfate or cysteine, and also 4NQO-bound urease released 4NQO by the addition of sodium dodecyl sulfate.
Authors:
Yamamoto, O [1] 
  1. Hiroshima Univ. (Japan). Research Inst. for Nuclear Medicine and Biology
Publication Date:
Dec 01, 1979
Product Type:
Journal Article
Reference Number:
AIX-12-584873; EDB-81-047666
Resource Relation:
Journal Name: J. Radiat. Res.; (Japan); Journal Volume: 20:4
Subject:
59 BASIC BIOLOGICAL SCIENCES; ALBUMINS; CHEMICAL BONDS; NITROSO-R SALT; CARBON 14 COMPOUNDS; CHEMICAL RADIATION EFFECTS; COVALENCE; CROSS-LINKING; DNA-ASE; INSULIN; PH VALUE; QUINOLINES; RNA-ASE; SULFHYDRYL RADICALS; TRACER TECHNIQUES; TRYPSIN; UREASE; AMIDINASES; AROMATICS; AZINES; CHEMICAL REACTIONS; CHEMISTRY; ENZYMES; ESTERASES; HETEROCYCLIC COMPOUNDS; HORMONES; HYDROLASES; HYDROXY COMPOUNDS; ISOTOPE APPLICATIONS; LABELLED COMPOUNDS; NAPHTHOLS; NITROSO COMPOUNDS; NON-PEPTIDE C-N HYDROLASES; ORGANIC ACIDS; ORGANIC COMPOUNDS; ORGANIC NITROGEN COMPOUNDS; ORGANIC SULFUR COMPOUNDS; PEPTIDE HORMONES; PEPTIDE HYDROLASES; PHENOLS; PHOSPHODIESTERASES; POLYMERIZATION; PROTEINS; PYRIDINES; RADIATION CHEMISTRY; RADIATION EFFECTS; RADICALS; SERINE PROTEINASES; SULFONIC ACIDS; 550201* - Biochemistry- Tracer Techniques
OSTI ID:
6601003
Country of Origin:
Japan
Language:
English
Other Identifying Numbers:
Journal ID: CODEN: JRARA
Submitting Site:
INIS
Size:
Pages: 276-283
Announcement Date:

Journal Article:

Citation Formats

Yamamoto, O. Noncovalent binding of 4-nitroquinoline-N-oxide to proteins. Japan: N. p., 1979. Web.
Yamamoto, O. Noncovalent binding of 4-nitroquinoline-N-oxide to proteins. Japan.
Yamamoto, O. 1979. "Noncovalent binding of 4-nitroquinoline-N-oxide to proteins." Japan.
@misc{etde_6601003,
title = {Noncovalent binding of 4-nitroquinoline-N-oxide to proteins}
author = {Yamamoto, O}
abstractNote = {Binding of 4NQO to various kinds of enzymes or proteins was studied. Each one of proteins was mixed with 4NQO in 0.4 mM NaHCO/sub 3/ solution and eluted through Ultrogel AcA 22 column. Radioactivity of /sup 14/C-labeled 4NQO found in protein fraction was measured. 4NQO bound hardly to polyglutamic acid and polyaspertic acid, somewhat to serum albumin, insulin, trypsin, RNA polymerase and DNA polymerase, and markedly to ureas which is an SH enzyme. Lactate dehydrogenase, one of SH enzymes, aggregated with 4NQO. The binding of SH enzyme with the N-oxide would be attributable to a noncovalent binding such as >N-O---H-S-, because 4NQO-urease binding yield markedly decreased in the presence of sodium dodecyl sulfate or cysteine, and also 4NQO-bound urease released 4NQO by the addition of sodium dodecyl sulfate.}
journal = {J. Radiat. Res.; (Japan)}
volume = {20:4}
journal type = {AC}
place = {Japan}
year = {1979}
month = {Dec}
}