Preparation and characterization of trypsin-nicked ovotransferrin
The N- and C-domains isolated from ovotransferrin (Tf) with trypsin could be separated from each other and from intact Tf by HPLC with a TSK-GEL G-3000SWG-0.1% SDS system. The analytical method revealed that Fe (III)-saturated Tf (Fe 2Tf) of 77 kDa was hydrolyzed by trypsin preferentially at the por...
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| Veröffentlicht in: | FEBS letters 1985-03, Vol.182 (2), p.305-309 |
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| container_start_page | 305 |
| container_title | FEBS letters |
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| creator | Ikeda, Hiroshi Nabuchi, Yoshiaki Nakazato, Katsuyoshi Tanaka, Yuichi Satake, Kazuo |
| description | The N- and C-domains isolated from ovotransferrin (Tf) with trypsin could be separated from each other and from intact Tf by HPLC with a TSK-GEL G-3000SWG-0.1% SDS system. The analytical method revealed that Fe (III)-saturated Tf (Fe
2Tf) of 77 kDa was hydrolyzed by trypsin preferentially at the portion connecting both domains. The main product was a nicked Fe
2Tf, in which the two fragmented domains of 35 kDa each were still bound together non-covalently and showed a notable cooperativity on their denaturation. |
| doi_str_mv | 10.1016/0014-5793(85)80321-5 |
| format | Article |
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2Tf) of 77 kDa was hydrolyzed by trypsin preferentially at the portion connecting both domains. The main product was a nicked Fe
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2Tf) of 77 kDa was hydrolyzed by trypsin preferentially at the portion connecting both domains. The main product was a nicked Fe
2Tf, in which the two fragmented domains of 35 kDa each were still bound together non-covalently and showed a notable cooperativity on their denaturation.</description><subject>albumen</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Biological and medical sciences</subject><subject>chickens</subject><subject>Cooperativity</subject><subject>Denaturation</subject><subject>Fe2Tf, Fe(III)-saturated Tf</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>GuHCl, guanidine hydrochloride</subject><subject>HPLC, high-performance liquid chromatography</subject><subject>Limited proteolysis</subject><subject>Metalloproteins</subject><subject>nicked Fe2Tf, Fe(III)-saturated nicked Tf</subject><subject>Other metalloproteins</subject><subject>ovotransferrin</subject><subject>Proteins</subject><subject>Tf, ovotransferrin</subject><subject>Transferrin</subject><subject>tryptic peptides</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1985</creationdate><recordtype>article</recordtype><recordid>eNqNkDFPwzAQhS0EEqXwDxgyIARDwI7txFmQStUCUiUYYLYc5ywMaRzstKj8epKm6oiYTvf87p3vQ-ic4BuCSXqLMWExz3J6Jfi1wDQhMT9AIyIyGlOWikM02luO0UkIH7jrBclHaPLioVFetdbVkarLSL93nW7B259BdCZq_aYJto5rqz-hjNzatV7VwYD3tj5FR0ZVAc52dYze5rPX6WO8eH54mk4WseY053GioWSEKc4hhbzIdalzTZlOFWGZhkIYQw0vqEowE4YljGRZUaQ5ZlkOBed0jC6H3Ma7rxWEVi5t0FBVqga3CpL0E2mSdkY2GLV3IXgwsvF2qfxGEix7XrKHIXsYUnC55SX7_ItdvgpaVaa7UNuwnxWMp5SwzjYfbN-2gs2_ouV8dp_0D70u-Fbt990NQdBBW1vwMmgLdYfJetCtLJ39-8O_dmuSag</recordid><startdate>19850325</startdate><enddate>19850325</enddate><creator>Ikeda, Hiroshi</creator><creator>Nabuchi, Yoshiaki</creator><creator>Nakazato, Katsuyoshi</creator><creator>Tanaka, Yuichi</creator><creator>Satake, Kazuo</creator><general>Elsevier B.V</general><general>Elsevier</general><scope>6I.</scope><scope>AAFTH</scope><scope>IQODW</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>C1K</scope></search><sort><creationdate>19850325</creationdate><title>Preparation and characterization of trypsin-nicked ovotransferrin</title><author>Ikeda, Hiroshi ; Nabuchi, Yoshiaki ; Nakazato, Katsuyoshi ; Tanaka, Yuichi ; Satake, Kazuo</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5395-2ced414a55e6e9b9cdc9c34c6a147ceb8ff3f5b3a2048f424177bb690479eb553</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1985</creationdate><topic>albumen</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Biological and medical sciences</topic><topic>chickens</topic><topic>Cooperativity</topic><topic>Denaturation</topic><topic>Fe2Tf, Fe(III)-saturated Tf</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>GuHCl, guanidine hydrochloride</topic><topic>HPLC, high-performance liquid chromatography</topic><topic>Limited proteolysis</topic><topic>Metalloproteins</topic><topic>nicked Fe2Tf, Fe(III)-saturated nicked Tf</topic><topic>Other metalloproteins</topic><topic>ovotransferrin</topic><topic>Proteins</topic><topic>Tf, ovotransferrin</topic><topic>Transferrin</topic><topic>tryptic peptides</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ikeda, Hiroshi</creatorcontrib><creatorcontrib>Nabuchi, Yoshiaki</creatorcontrib><creatorcontrib>Nakazato, Katsuyoshi</creatorcontrib><creatorcontrib>Tanaka, Yuichi</creatorcontrib><creatorcontrib>Satake, Kazuo</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Pascal-Francis</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ikeda, Hiroshi</au><au>Nabuchi, Yoshiaki</au><au>Nakazato, Katsuyoshi</au><au>Tanaka, Yuichi</au><au>Satake, Kazuo</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Preparation and characterization of trypsin-nicked ovotransferrin</atitle><jtitle>FEBS letters</jtitle><date>1985-03-25</date><risdate>1985</risdate><volume>182</volume><issue>2</issue><spage>305</spage><epage>309</epage><pages>305-309</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><coden>FEBLAL</coden><abstract>The N- and C-domains isolated from ovotransferrin (Tf) with trypsin could be separated from each other and from intact Tf by HPLC with a TSK-GEL G-3000SWG-0.1% SDS system. The analytical method revealed that Fe (III)-saturated Tf (Fe
2Tf) of 77 kDa was hydrolyzed by trypsin preferentially at the portion connecting both domains. The main product was a nicked Fe
2Tf, in which the two fragmented domains of 35 kDa each were still bound together non-covalently and showed a notable cooperativity on their denaturation.</abstract><cop>Amsterdam</cop><pub>Elsevier B.V</pub><doi>10.1016/0014-5793(85)80321-5</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0014-5793 |
| ispartof | FEBS letters, 1985-03, Vol.182 (2), p.305-309 |
| issn | 0014-5793 1873-3468 |
| language | eng |
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| source | Elsevier ScienceDirect Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | albumen Analytical, structural and metabolic biochemistry Biological and medical sciences chickens Cooperativity Denaturation Fe2Tf, Fe(III)-saturated Tf Fundamental and applied biological sciences. Psychology GuHCl, guanidine hydrochloride HPLC, high-performance liquid chromatography Limited proteolysis Metalloproteins nicked Fe2Tf, Fe(III)-saturated nicked Tf Other metalloproteins ovotransferrin Proteins Tf, ovotransferrin Transferrin tryptic peptides |
| title | Preparation and characterization of trypsin-nicked ovotransferrin |
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