Analysis of the Acid-Base Titration Curve of Hen Lysozyme
The acid-base titration curves of hen egg-white lysozyme [EC 3.2.1.17] obtained by three groups (Sakakibara & Hamaguchi (1968) J. Biochem. 64, 613–618; Tanford & Roxby (1972) Biochemistry 11, 2192–2198; Pfeil & Privalov (1976) Biophys. Chem. 4, 23–32) were analyzed using the empirical fo...
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| Veröffentlicht in: | Journal of biochemistry (Tokyo) 1980-04, Vol.87 (4), p.1215-1219 |
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| creator | KURAMITSU, Seiki HAMAGUCHI, Kozo |
| description | The acid-base titration curves of hen egg-white lysozyme [EC 3.2.1.17] obtained by three groups (Sakakibara & Hamaguchi (1968) J. Biochem. 64, 613–618; Tanford & Roxby (1972) Biochemistry 11, 2192–2198; Pfeil & Privalov (1976) Biophys. Chem. 4, 23–32) were analyzed using the empirical formula of Linderstrøm-Lang. Hen lysozyme has 32 ionizable groups including the α-amino and α-carboxyl groups. Of the 21 groups other than the 11 arginyl residues, the pK values of 17 ionizable groups have been determined by various methods. Using these pK values, the pK values of the other four ionizable groups were estimated. The apparent pK values obtained were 2.0 (pKint=3.4), 2.1 (pKint=3.5), 2.5 (pKint=3.8), and 7.9 (pKint=8.5) at 0.1 ionic strength and 25°C. The titration curves obtained by the above three groups were consistently explained in terms of the same set of pKint values. The results obtained also showed that no buried and untitratable groups are present in the native lysozyme molecule. |
| doi_str_mv | 10.1093/oxfordjournals.jbchem.a132855 |
| format | Article |
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Biochem. 64, 613–618; Tanford & Roxby (1972) Biochemistry 11, 2192–2198; Pfeil & Privalov (1976) Biophys. Chem. 4, 23–32) were analyzed using the empirical formula of Linderstrøm-Lang. Hen lysozyme has 32 ionizable groups including the α-amino and α-carboxyl groups. Of the 21 groups other than the 11 arginyl residues, the pK values of 17 ionizable groups have been determined by various methods. Using these pK values, the pK values of the other four ionizable groups were estimated. The apparent pK values obtained were 2.0 (pKint=3.4), 2.1 (pKint=3.5), 2.5 (pKint=3.8), and 7.9 (pKint=8.5) at 0.1 ionic strength and 25°C. The titration curves obtained by the above three groups were consistently explained in terms of the same set of pKint values. The results obtained also showed that no buried and untitratable groups are present in the native lysozyme molecule.</description><identifier>ISSN: 0021-924X</identifier><identifier>DOI: 10.1093/oxfordjournals.jbchem.a132855</identifier><identifier>PMID: 6771251</identifier><language>eng</language><publisher>England: Oxford University Press</publisher><subject>Animals ; Aspartic Acid ; Chickens ; Glutamates ; Histidine ; Hydrogen-Ion Concentration ; Kinetics ; Lysine ; Muramidase ; Tyrosine</subject><ispartof>Journal of biochemistry (Tokyo), 1980-04, Vol.87 (4), p.1215-1219</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,778,782,27911,27912</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/6771251$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>KURAMITSU, Seiki</creatorcontrib><creatorcontrib>HAMAGUCHI, Kozo</creatorcontrib><title>Analysis of the Acid-Base Titration Curve of Hen Lysozyme</title><title>Journal of biochemistry (Tokyo)</title><addtitle>J Biochem</addtitle><description>The acid-base titration curves of hen egg-white lysozyme [EC 3.2.1.17] obtained by three groups (Sakakibara & Hamaguchi (1968) J. Biochem. 64, 613–618; Tanford & Roxby (1972) Biochemistry 11, 2192–2198; Pfeil & Privalov (1976) Biophys. Chem. 4, 23–32) were analyzed using the empirical formula of Linderstrøm-Lang. Hen lysozyme has 32 ionizable groups including the α-amino and α-carboxyl groups. Of the 21 groups other than the 11 arginyl residues, the pK values of 17 ionizable groups have been determined by various methods. Using these pK values, the pK values of the other four ionizable groups were estimated. The apparent pK values obtained were 2.0 (pKint=3.4), 2.1 (pKint=3.5), 2.5 (pKint=3.8), and 7.9 (pKint=8.5) at 0.1 ionic strength and 25°C. The titration curves obtained by the above three groups were consistently explained in terms of the same set of pKint values. The results obtained also showed that no buried and untitratable groups are present in the native lysozyme molecule.</description><subject>Animals</subject><subject>Aspartic Acid</subject><subject>Chickens</subject><subject>Glutamates</subject><subject>Histidine</subject><subject>Hydrogen-Ion Concentration</subject><subject>Kinetics</subject><subject>Lysine</subject><subject>Muramidase</subject><subject>Tyrosine</subject><issn>0021-924X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1980</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9j11LwzAUhnOhzDn9CUJv9K4zn816uc2PCQUZTBjehKRJWObazKSV1V9vx4ZXh5fnOe_hAHCP4BjBnDz6g_VBb30barmL460qN6YaS0TwhLELMIQQozTHdH0FrmPcHiMmZAAGGecIMzQE-bTf7KKLibdJszHJtHQ6nclokpVrgmycr5N5G37MUViYOim66H-7ytyAS9sfNbfnOQIfL8-r-SIt3l_f5tMidYTiJi2R5pMS28wqaDNNtcZEMkkUlBOtLMeQqkxLgizLOTFUMc0owzTPcmYxR2QEHk69--C_WxMbUblYmt1O1sa3UXCGOCTwKN6dxVZVRot9cJUMnTj_2vP0xF1szOEfy_DVK4QzsVh_ihw-FXyJl2JG_gDsQWjN</recordid><startdate>198004</startdate><enddate>198004</enddate><creator>KURAMITSU, Seiki</creator><creator>HAMAGUCHI, Kozo</creator><general>Oxford University Press</general><scope>BSCLL</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>198004</creationdate><title>Analysis of the Acid-Base Titration Curve of Hen Lysozyme</title><author>KURAMITSU, Seiki ; HAMAGUCHI, Kozo</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-i342t-c1d78c2f6fb0f6d4dd23a5a3b0a8dbf7204b6da31f5973e4b5d545249695f2713</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1980</creationdate><topic>Animals</topic><topic>Aspartic Acid</topic><topic>Chickens</topic><topic>Glutamates</topic><topic>Histidine</topic><topic>Hydrogen-Ion Concentration</topic><topic>Kinetics</topic><topic>Lysine</topic><topic>Muramidase</topic><topic>Tyrosine</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>KURAMITSU, Seiki</creatorcontrib><creatorcontrib>HAMAGUCHI, Kozo</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of biochemistry (Tokyo)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>KURAMITSU, Seiki</au><au>HAMAGUCHI, Kozo</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Analysis of the Acid-Base Titration Curve of Hen Lysozyme</atitle><jtitle>Journal of biochemistry (Tokyo)</jtitle><addtitle>J Biochem</addtitle><date>1980-04</date><risdate>1980</risdate><volume>87</volume><issue>4</issue><spage>1215</spage><epage>1219</epage><pages>1215-1219</pages><issn>0021-924X</issn><abstract>The acid-base titration curves of hen egg-white lysozyme [EC 3.2.1.17] obtained by three groups (Sakakibara & Hamaguchi (1968) J. Biochem. 64, 613–618; Tanford & Roxby (1972) Biochemistry 11, 2192–2198; Pfeil & Privalov (1976) Biophys. Chem. 4, 23–32) were analyzed using the empirical formula of Linderstrøm-Lang. Hen lysozyme has 32 ionizable groups including the α-amino and α-carboxyl groups. Of the 21 groups other than the 11 arginyl residues, the pK values of 17 ionizable groups have been determined by various methods. Using these pK values, the pK values of the other four ionizable groups were estimated. The apparent pK values obtained were 2.0 (pKint=3.4), 2.1 (pKint=3.5), 2.5 (pKint=3.8), and 7.9 (pKint=8.5) at 0.1 ionic strength and 25°C. The titration curves obtained by the above three groups were consistently explained in terms of the same set of pKint values. The results obtained also showed that no buried and untitratable groups are present in the native lysozyme molecule.</abstract><cop>England</cop><pub>Oxford University Press</pub><pmid>6771251</pmid><doi>10.1093/oxfordjournals.jbchem.a132855</doi><tpages>5</tpages></addata></record> |
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| source | J-STAGE Free; MEDLINE; Oxford University Press Journals Digital Archive Legacy; Free Full-Text Journals in Chemistry |
| subjects | Animals Aspartic Acid Chickens Glutamates Histidine Hydrogen-Ion Concentration Kinetics Lysine Muramidase Tyrosine |
| title | Analysis of the Acid-Base Titration Curve of Hen Lysozyme |
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