Binding of N-Methyl Nicotinamide Chloride by Tryptophan Residues of α-Lactalbumin
Studies of the binding of N -methyl nicotinamide chloride by α-lactalbumin show that complex formation occurs with 1 of 4 tryptophan residues at pH 6 whereas two form complexes at pH 2 as a result of acid denaturation. Alkaline denaturation likewise leads to an increase in exposure of tryptophans,...
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Veröffentlicht in: | The Journal of biological chemistry 1972-05, Vol.247 (10), p.3062 |
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container_title | The Journal of biological chemistry |
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creator | Frederick M. Robbins Leo G. Holmes |
description | Studies of the binding of N -methyl nicotinamide chloride by α-lactalbumin show that complex formation occurs with 1 of 4 tryptophan residues at pH 6
whereas two form complexes at pH 2 as a result of acid denaturation. Alkaline denaturation likewise leads to an increase in
exposure of tryptophans, and three of the four groups form complexes at pH 11. From a consideration of previous studies and
a recently proposed molecular model for α-lactalbumin, the residues involved in binding N -methyl nicotinamide chloride have been tentatively identified as tryptophan-118, tryptophan-104, and tryptophan-60. |
format | Article |
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whereas two form complexes at pH 2 as a result of acid denaturation. Alkaline denaturation likewise leads to an increase in
exposure of tryptophans, and three of the four groups form complexes at pH 11. From a consideration of previous studies and
a recently proposed molecular model for α-lactalbumin, the residues involved in binding N -methyl nicotinamide chloride have been tentatively identified as tryptophan-118, tryptophan-104, and tryptophan-60.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>PMID: 4260381</identifier><language>eng</language><publisher>American Society for Biochemistry and Molecular Biology</publisher><ispartof>The Journal of biological chemistry, 1972-05, Vol.247 (10), p.3062</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</link.rule.ids></links><search><creatorcontrib>Frederick M. Robbins</creatorcontrib><creatorcontrib>Leo G. Holmes</creatorcontrib><title>Binding of N-Methyl Nicotinamide Chloride by Tryptophan Residues of α-Lactalbumin</title><title>The Journal of biological chemistry</title><description>Studies of the binding of N -methyl nicotinamide chloride by α-lactalbumin show that complex formation occurs with 1 of 4 tryptophan residues at pH 6
whereas two form complexes at pH 2 as a result of acid denaturation. Alkaline denaturation likewise leads to an increase in
exposure of tryptophans, and three of the four groups form complexes at pH 11. From a consideration of previous studies and
a recently proposed molecular model for α-lactalbumin, the residues involved in binding N -methyl nicotinamide chloride have been tentatively identified as tryptophan-118, tryptophan-104, and tryptophan-60.</description><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1972</creationdate><recordtype>article</recordtype><sourceid/><recordid>eNpjYuA0NLAw1jU2NYxgYeA0MDAy1LU0MrXgYOAqLs4yAAITS0N2BnYTIzMDYwtDToYQp8y8lMy8dIX8NAU_Xd_UkozKHAW_zOT8ksy8xNzMlFQF54yc_CIQI6lSIaSosqAkvyAjMU8hKLU4M6U0tRik8XDfoY26PonJJYk5SaW5mXk8DKxpiTnFqbxQmptB2c01xNlDNyMzPaM8syg1PikzPzkjNTfeyMQ83tAg3tjAzMiYOFUADRtDkw</recordid><startdate>19720525</startdate><enddate>19720525</enddate><creator>Frederick M. Robbins</creator><creator>Leo G. Holmes</creator><general>American Society for Biochemistry and Molecular Biology</general><scope/></search><sort><creationdate>19720525</creationdate><title>Binding of N-Methyl Nicotinamide Chloride by Tryptophan Residues of α-Lactalbumin</title><author>Frederick M. Robbins ; Leo G. Holmes</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-highwire_biochem_247_10_30623</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1972</creationdate><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Frederick M. Robbins</creatorcontrib><creatorcontrib>Leo G. Holmes</creatorcontrib><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Frederick M. Robbins</au><au>Leo G. Holmes</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Binding of N-Methyl Nicotinamide Chloride by Tryptophan Residues of α-Lactalbumin</atitle><jtitle>The Journal of biological chemistry</jtitle><date>1972-05-25</date><risdate>1972</risdate><volume>247</volume><issue>10</issue><spage>3062</spage><pages>3062-</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>Studies of the binding of N -methyl nicotinamide chloride by α-lactalbumin show that complex formation occurs with 1 of 4 tryptophan residues at pH 6
whereas two form complexes at pH 2 as a result of acid denaturation. Alkaline denaturation likewise leads to an increase in
exposure of tryptophans, and three of the four groups form complexes at pH 11. From a consideration of previous studies and
a recently proposed molecular model for α-lactalbumin, the residues involved in binding N -methyl nicotinamide chloride have been tentatively identified as tryptophan-118, tryptophan-104, and tryptophan-60.</abstract><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>4260381</pmid></addata></record> |
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title | Binding of N-Methyl Nicotinamide Chloride by Tryptophan Residues of α-Lactalbumin |
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