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Preparation and characterization of trypsin‐nicked ovotransferrin
Author(s) -
Ikeda Hiroshi,
Nabuchi Yoshiaki,
Nakazato Katsuyoshi,
Tanaka Yuichi,
Satake Kazuo
Publication year - 1985
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(85)80321-5
Subject(s) - ovotransferrin , trypsin , chemistry , cooperativity , hydrolysis , covalent bond , denaturation (fissile materials) , chromatography , crystallography , biochemistry , nuclear chemistry , enzyme , organic chemistry , egg white
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 2 Tf) of 77 kDa was hydrolyzed by trypsin preferentially at the portion connecting both domains. The main product was a nicked Fe 2 Tf, in which the two fragmented domains of 35 kDa each were still bound together non‐covalently and showed a notable cooperativity on their denaturation.