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
Hauptverfasser:	Ikeda, Hiroshi, Nabuchi, Yoshiaki, Nakazato, Katsuyoshi, Tanaka, Yuichi, Satake, Kazuo
Format:	Artikel
Sprache:	eng
Schlagworte:	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
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Zusammenfassung:	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.
ISSN:	0014-5793 1873-3468
DOI:	10.1016/0014-5793(85)80321-5