The Effect of Gamma Radiation on Collagen

Collagen was irradiated with 5- and 50-Mrad doses of gamma rays under various conditions. Such doses lead to loss of crystallinity, as indicated by the x-ray-diffraction pattern, increase in solubility, and other changes in physical properties indicative of extensive loss of molecular structure and...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Radiation research 1962-03, Vol.16 (3), p.211-223
Hauptverfasser: Bowes, J. H., Moss, J. A.
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 223
container_issue 3
container_start_page 211
container_title Radiation research
container_volume 16
creator Bowes, J. H.
Moss, J. A.
description Collagen was irradiated with 5- and 50-Mrad doses of gamma rays under various conditions. Such doses lead to loss of crystallinity, as indicated by the x-ray-diffraction pattern, increase in solubility, and other changes in physical properties indicative of extensive loss of molecular structure and breakdown to smaller units. Determination of N-terminal residues using fluorodinitrobenzene indicates that there was relatively little hydrolytic scission of peptide bonds. Increase in amide nitrogen and in carbonyl groups indicates that --N-- C-- bonds were broken by a previously suggested mechanism. On irradiation with doses of 50 Mrad there was some loss of nitrogen and an over- all loss of some l0 to 20% of amino acids. The formation of carbonyl compounds accounts for only a small proportion of this loss, and large amounts of breskdown products remain unidentified. Relative losses of amino acids varied with the conditibns of irradiation, but in general the acidic and basic amino acids and those having a ring structure were the most radiosensitive. The chemical changes occurring as a result of gamma radiation are compared with those caused by other forms of degradation. (auth)
doi_str_mv 10.2307/3571153
format Article
fullrecord <record><control><sourceid>jstor_osti_</sourceid><recordid>TN_cdi_osti_scitechconnect_4789054</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><jstor_id>3571153</jstor_id><sourcerecordid>3571153</sourcerecordid><originalsourceid>FETCH-LOGICAL-c335t-d947702613989cfef8ffeb471dd0a63afa65b537735cefedeeab4629b693b0863</originalsourceid><addsrcrecordid>eNp10F1LwzAUBuAgiptT_AdSRBQvqklP83UpY05hIMi8DmmauI61mU124b830oJXwoHDgYeXw4vQJcEPBWD-CJQTQuEITYkEkdMSl8doijFAzqngE3QWwhanmzB5iiYEBC8whym6X29stnDOmph5ly112-rsXdeNjo3vsjRzv9vpT9udoxOnd8FejHuGPp4X6_lLvnpbvs6fVrkBoDGvZck5LhgBKaRx1okUXpWc1DXWDLTTjFYUOAdqrLO1tboqWSErJqHCgsEMXQ-5PsRGBdNEazbGd116UZVcSEzLhG4HtO_918GGqNomGJs-7aw_BCUKSTAwmuDdAE3vQ-itU_u-aXX_rQhWv9Wpsbokr8bIQ9Xa-s-NXSVwM4BtiL7_N-cH7-lwzw</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>82910365</pqid></control><display><type>article</type><title>The Effect of Gamma Radiation on Collagen</title><source>Jstor Complete Legacy</source><source>MEDLINE</source><creator>Bowes, J. H. ; Moss, J. A.</creator><creatorcontrib>Bowes, J. H. ; Moss, J. A. ; British Leather Manufacturers' Research Assn., Egham, Surrey, Eng</creatorcontrib><description>Collagen was irradiated with 5- and 50-Mrad doses of gamma rays under various conditions. Such doses lead to loss of crystallinity, as indicated by the x-ray-diffraction pattern, increase in solubility, and other changes in physical properties indicative of extensive loss of molecular structure and breakdown to smaller units. Determination of N-terminal residues using fluorodinitrobenzene indicates that there was relatively little hydrolytic scission of peptide bonds. Increase in amide nitrogen and in carbonyl groups indicates that --N-- C-- bonds were broken by a previously suggested mechanism. On irradiation with doses of 50 Mrad there was some loss of nitrogen and an over- all loss of some l0 to 20% of amino acids. The formation of carbonyl compounds accounts for only a small proportion of this loss, and large amounts of breskdown products remain unidentified. Relative losses of amino acids varied with the conditibns of irradiation, but in general the acidic and basic amino acids and those having a ring structure were the most radiosensitive. The chemical changes occurring as a result of gamma radiation are compared with those caused by other forms of degradation. (auth)</description><identifier>ISSN: 0033-7587</identifier><identifier>EISSN: 1938-5404</identifier><identifier>DOI: 10.2307/3571153</identifier><identifier>PMID: 13872073</identifier><language>eng</language><publisher>United States: Academic Press, Inc</publisher><subject>AMIDES ; AMINO ACIDS ; BIOLOGY AND MEDICINE ; COLLAGEN ; Collagen - radiation effects ; Collagens ; GAMMA RADIATION ; Gamma Rays ; Gelatins ; Irradiation ; NITROGEN ; Old Medline ; Oxygen ; PROTEINS ; QUANTITY RATIO ; Radiation dosage ; RADIATION DOSES ; RADIATION EFFECTS ; RADIOCHEMISTRY ; RADIOSENSITIVITY ; SOLUBILITY ; TISSUES</subject><ispartof>Radiation research, 1962-03, Vol.16 (3), p.211-223</ispartof><rights>Copyright 1962 Academic Press Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c335t-d947702613989cfef8ffeb471dd0a63afa65b537735cefedeeab4629b693b0863</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/3571153$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/3571153$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,776,780,799,881,27901,27902,57992,58225</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/13872073$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://www.osti.gov/biblio/4789054$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>Bowes, J. H.</creatorcontrib><creatorcontrib>Moss, J. A.</creatorcontrib><creatorcontrib>British Leather Manufacturers' Research Assn., Egham, Surrey, Eng</creatorcontrib><title>The Effect of Gamma Radiation on Collagen</title><title>Radiation research</title><addtitle>Radiat Res</addtitle><description>Collagen was irradiated with 5- and 50-Mrad doses of gamma rays under various conditions. Such doses lead to loss of crystallinity, as indicated by the x-ray-diffraction pattern, increase in solubility, and other changes in physical properties indicative of extensive loss of molecular structure and breakdown to smaller units. Determination of N-terminal residues using fluorodinitrobenzene indicates that there was relatively little hydrolytic scission of peptide bonds. Increase in amide nitrogen and in carbonyl groups indicates that --N-- C-- bonds were broken by a previously suggested mechanism. On irradiation with doses of 50 Mrad there was some loss of nitrogen and an over- all loss of some l0 to 20% of amino acids. The formation of carbonyl compounds accounts for only a small proportion of this loss, and large amounts of breskdown products remain unidentified. Relative losses of amino acids varied with the conditibns of irradiation, but in general the acidic and basic amino acids and those having a ring structure were the most radiosensitive. The chemical changes occurring as a result of gamma radiation are compared with those caused by other forms of degradation. (auth)</description><subject>AMIDES</subject><subject>AMINO ACIDS</subject><subject>BIOLOGY AND MEDICINE</subject><subject>COLLAGEN</subject><subject>Collagen - radiation effects</subject><subject>Collagens</subject><subject>GAMMA RADIATION</subject><subject>Gamma Rays</subject><subject>Gelatins</subject><subject>Irradiation</subject><subject>NITROGEN</subject><subject>Old Medline</subject><subject>Oxygen</subject><subject>PROTEINS</subject><subject>QUANTITY RATIO</subject><subject>Radiation dosage</subject><subject>RADIATION DOSES</subject><subject>RADIATION EFFECTS</subject><subject>RADIOCHEMISTRY</subject><subject>RADIOSENSITIVITY</subject><subject>SOLUBILITY</subject><subject>TISSUES</subject><issn>0033-7587</issn><issn>1938-5404</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1962</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp10F1LwzAUBuAgiptT_AdSRBQvqklP83UpY05hIMi8DmmauI61mU124b830oJXwoHDgYeXw4vQJcEPBWD-CJQTQuEITYkEkdMSl8doijFAzqngE3QWwhanmzB5iiYEBC8whym6X29stnDOmph5ly112-rsXdeNjo3vsjRzv9vpT9udoxOnd8FejHuGPp4X6_lLvnpbvs6fVrkBoDGvZck5LhgBKaRx1okUXpWc1DXWDLTTjFYUOAdqrLO1tboqWSErJqHCgsEMXQ-5PsRGBdNEazbGd116UZVcSEzLhG4HtO_918GGqNomGJs-7aw_BCUKSTAwmuDdAE3vQ-itU_u-aXX_rQhWv9Wpsbokr8bIQ9Xa-s-NXSVwM4BtiL7_N-cH7-lwzw</recordid><startdate>19620301</startdate><enddate>19620301</enddate><creator>Bowes, J. H.</creator><creator>Moss, J. A.</creator><general>Academic Press, Inc</general><general>Radiation Research Society</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><scope>OTOTI</scope></search><sort><creationdate>19620301</creationdate><title>The Effect of Gamma Radiation on Collagen</title><author>Bowes, J. H. ; Moss, J. A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c335t-d947702613989cfef8ffeb471dd0a63afa65b537735cefedeeab4629b693b0863</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1962</creationdate><topic>AMIDES</topic><topic>AMINO ACIDS</topic><topic>BIOLOGY AND MEDICINE</topic><topic>COLLAGEN</topic><topic>Collagen - radiation effects</topic><topic>Collagens</topic><topic>GAMMA RADIATION</topic><topic>Gamma Rays</topic><topic>Gelatins</topic><topic>Irradiation</topic><topic>NITROGEN</topic><topic>Old Medline</topic><topic>Oxygen</topic><topic>PROTEINS</topic><topic>QUANTITY RATIO</topic><topic>Radiation dosage</topic><topic>RADIATION DOSES</topic><topic>RADIATION EFFECTS</topic><topic>RADIOCHEMISTRY</topic><topic>RADIOSENSITIVITY</topic><topic>SOLUBILITY</topic><topic>TISSUES</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bowes, J. H.</creatorcontrib><creatorcontrib>Moss, J. A.</creatorcontrib><creatorcontrib>British Leather Manufacturers' Research Assn., Egham, Surrey, Eng</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><collection>OSTI.GOV</collection><jtitle>Radiation research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bowes, J. H.</au><au>Moss, J. A.</au><aucorp>British Leather Manufacturers' Research Assn., Egham, Surrey, Eng</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The Effect of Gamma Radiation on Collagen</atitle><jtitle>Radiation research</jtitle><addtitle>Radiat Res</addtitle><date>1962-03-01</date><risdate>1962</risdate><volume>16</volume><issue>3</issue><spage>211</spage><epage>223</epage><pages>211-223</pages><issn>0033-7587</issn><eissn>1938-5404</eissn><abstract>Collagen was irradiated with 5- and 50-Mrad doses of gamma rays under various conditions. Such doses lead to loss of crystallinity, as indicated by the x-ray-diffraction pattern, increase in solubility, and other changes in physical properties indicative of extensive loss of molecular structure and breakdown to smaller units. Determination of N-terminal residues using fluorodinitrobenzene indicates that there was relatively little hydrolytic scission of peptide bonds. Increase in amide nitrogen and in carbonyl groups indicates that --N-- C-- bonds were broken by a previously suggested mechanism. On irradiation with doses of 50 Mrad there was some loss of nitrogen and an over- all loss of some l0 to 20% of amino acids. The formation of carbonyl compounds accounts for only a small proportion of this loss, and large amounts of breskdown products remain unidentified. Relative losses of amino acids varied with the conditibns of irradiation, but in general the acidic and basic amino acids and those having a ring structure were the most radiosensitive. The chemical changes occurring as a result of gamma radiation are compared with those caused by other forms of degradation. (auth)</abstract><cop>United States</cop><pub>Academic Press, Inc</pub><pmid>13872073</pmid><doi>10.2307/3571153</doi><tpages>13</tpages></addata></record>
fulltext fulltext
identifier ISSN: 0033-7587
ispartof Radiation research, 1962-03, Vol.16 (3), p.211-223
issn 0033-7587
1938-5404
language eng
recordid cdi_osti_scitechconnect_4789054
source Jstor Complete Legacy; MEDLINE
subjects AMIDES
AMINO ACIDS
BIOLOGY AND MEDICINE
COLLAGEN
Collagen - radiation effects
Collagens
GAMMA RADIATION
Gamma Rays
Gelatins
Irradiation
NITROGEN
Old Medline
Oxygen
PROTEINS
QUANTITY RATIO
Radiation dosage
RADIATION DOSES
RADIATION EFFECTS
RADIOCHEMISTRY
RADIOSENSITIVITY
SOLUBILITY
TISSUES
title The Effect of Gamma Radiation on Collagen
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-05T11%3A38%3A12IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-jstor_osti_&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=The%20Effect%20of%20Gamma%20Radiation%20on%20Collagen&rft.jtitle=Radiation%20research&rft.au=Bowes,%20J.%20H.&rft.aucorp=British%20Leather%20Manufacturers'%20Research%20Assn.,%20Egham,%20Surrey,%20Eng&rft.date=1962-03-01&rft.volume=16&rft.issue=3&rft.spage=211&rft.epage=223&rft.pages=211-223&rft.issn=0033-7587&rft.eissn=1938-5404&rft_id=info:doi/10.2307/3571153&rft_dat=%3Cjstor_osti_%3E3571153%3C/jstor_osti_%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=82910365&rft_id=info:pmid/13872073&rft_jstor_id=3571153&rfr_iscdi=true