Optical rotation and viscosity of native and denatured proteins. XIII. Further studies on enzyme proteins
The optical rotatory dispersion of aldolase, bacterial amylase, deoxyribonuclease, elastase, lactic acid dehydrogenase, lysozyme, and ribonuclease was studied by the method of spectropolarimetry. The dispersion constants (λ c ) of deoxyribonuclease and elastase were found in the same low range as th...
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| Veröffentlicht in: | Archives of biochemistry and biophysics 1961-02, Vol.92 (2), p.216-220 |
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| creator | Jirgensons, B. |
| description | The optical rotatory dispersion of aldolase, bacterial amylase, deoxyribonuclease, elastase, lactic acid dehydrogenase, lysozyme, and ribonuclease was studied by the method of spectropolarimetry. The dispersion constants (λ
c
) of deoxyribonuclease and elastase were found in the same low range as the constant of ribonuclease. The high dispersion constants of aldolase, lactic acid dehydrogenase, and bacterial amylase decreased strongly upon denaturation with acid, alkali, or guanidine thiocyanate. The rotatory properties of lysozyme were but little affected by alkali, although the protein could be readily denatured by guanidine thiocyanate. Complex dispersion was observed by means of ultraviolet light with lysozyme but not with ribonuclease. |
| doi_str_mv | 10.1016/0003-9861(61)90339-3 |
| format | Article |
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) of deoxyribonuclease and elastase were found in the same low range as the constant of ribonuclease. The high dispersion constants of aldolase, lactic acid dehydrogenase, and bacterial amylase decreased strongly upon denaturation with acid, alkali, or guanidine thiocyanate. The rotatory properties of lysozyme were but little affected by alkali, although the protein could be readily denatured by guanidine thiocyanate. Complex dispersion was observed by means of ultraviolet light with lysozyme but not with ribonuclease.</description><identifier>ISSN: 0003-9861</identifier><identifier>EISSN: 1096-0384</identifier><identifier>DOI: 10.1016/0003-9861(61)90339-3</identifier><identifier>PMID: 13790115</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Enzymes - chemistry ; Old Medline ; Optical Rotation ; Protein Denaturation ; Proteins ; Viscosity</subject><ispartof>Archives of biochemistry and biophysics, 1961-02, Vol.92 (2), p.216-220</ispartof><rights>1961</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c275t-5f45d735a9c1f1326f8885c6cdfe27be13182c006e00c0a5f0497db750a6b9ad3</citedby><cites>FETCH-LOGICAL-c275t-5f45d735a9c1f1326f8885c6cdfe27be13182c006e00c0a5f0497db750a6b9ad3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0003-9861(61)90339-3$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3549,27923,27924,45994</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/13790115$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Jirgensons, B.</creatorcontrib><title>Optical rotation and viscosity of native and denatured proteins. XIII. Further studies on enzyme proteins</title><title>Archives of biochemistry and biophysics</title><addtitle>Arch Biochem Biophys</addtitle><description>The optical rotatory dispersion of aldolase, bacterial amylase, deoxyribonuclease, elastase, lactic acid dehydrogenase, lysozyme, and ribonuclease was studied by the method of spectropolarimetry. The dispersion constants (λ
c
) of deoxyribonuclease and elastase were found in the same low range as the constant of ribonuclease. The high dispersion constants of aldolase, lactic acid dehydrogenase, and bacterial amylase decreased strongly upon denaturation with acid, alkali, or guanidine thiocyanate. The rotatory properties of lysozyme were but little affected by alkali, although the protein could be readily denatured by guanidine thiocyanate. Complex dispersion was observed by means of ultraviolet light with lysozyme but not with ribonuclease.</description><subject>Enzymes - chemistry</subject><subject>Old Medline</subject><subject>Optical Rotation</subject><subject>Protein Denaturation</subject><subject>Proteins</subject><subject>Viscosity</subject><issn>0003-9861</issn><issn>1096-0384</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1961</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kMFKAzEQhoMotlbfQCQn0cPWyWY3u7kIUqwWBC8K3kKazGKk3a1JtlCf3tQWvQmBMMM3_zAfIecMxgyYuAEAnslasCvBriVwLjN-QIYMpMiA18UhGf4iA3ISwgcAY4XIj8mA8UqmohwS97yKzugF9V3U0XUt1a2laxdMF1zc0K6hbeqv8advMRW9R0tXiUfXhjF9m81mYzrtfXxHT0PsrcNAUxC2X5sl_pKn5KjRi4Bn-39EXqf3L5PH7On5YTa5e8pMXpUxK5uitBUvtTSsYTwXTV3XpRHGNphXc2Sc1bkBEAhgQJcNFLKy86oELeZSWz4il7vctPizxxDVMl2Di4VuseuDqvO6kCCKBBY70PguBI-NWnm31H6jGKitYrX1p7b-VHo_ihVPYxf7_H6-RPs3tHeagNsdgOnKtUOvgnHYGrTOo4nKdu7_Dd93RIuq</recordid><startdate>196102</startdate><enddate>196102</enddate><creator>Jirgensons, B.</creator><general>Elsevier Inc</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></search><sort><creationdate>196102</creationdate><title>Optical rotation and viscosity of native and denatured proteins. XIII. Further studies on enzyme proteins</title><author>Jirgensons, B.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c275t-5f45d735a9c1f1326f8885c6cdfe27be13182c006e00c0a5f0497db750a6b9ad3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1961</creationdate><topic>Enzymes - chemistry</topic><topic>Old Medline</topic><topic>Optical Rotation</topic><topic>Protein Denaturation</topic><topic>Proteins</topic><topic>Viscosity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Jirgensons, B.</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><jtitle>Archives of biochemistry and biophysics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Jirgensons, B.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Optical rotation and viscosity of native and denatured proteins. XIII. Further studies on enzyme proteins</atitle><jtitle>Archives of biochemistry and biophysics</jtitle><addtitle>Arch Biochem Biophys</addtitle><date>1961-02</date><risdate>1961</risdate><volume>92</volume><issue>2</issue><spage>216</spage><epage>220</epage><pages>216-220</pages><issn>0003-9861</issn><eissn>1096-0384</eissn><abstract>The optical rotatory dispersion of aldolase, bacterial amylase, deoxyribonuclease, elastase, lactic acid dehydrogenase, lysozyme, and ribonuclease was studied by the method of spectropolarimetry. The dispersion constants (λ
c
) of deoxyribonuclease and elastase were found in the same low range as the constant of ribonuclease. The high dispersion constants of aldolase, lactic acid dehydrogenase, and bacterial amylase decreased strongly upon denaturation with acid, alkali, or guanidine thiocyanate. The rotatory properties of lysozyme were but little affected by alkali, although the protein could be readily denatured by guanidine thiocyanate. Complex dispersion was observed by means of ultraviolet light with lysozyme but not with ribonuclease.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>13790115</pmid><doi>10.1016/0003-9861(61)90339-3</doi><tpages>5</tpages></addata></record> |
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| language | eng |
| recordid | cdi_proquest_miscellaneous_82849064 |
| source | MEDLINE; ScienceDirect Journals (5 years ago - present) |
| subjects | Enzymes - chemistry Old Medline Optical Rotation Protein Denaturation Proteins Viscosity |
| title | Optical rotation and viscosity of native and denatured proteins. XIII. Further studies on enzyme proteins |
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