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J. Biochem, 1988, Vol. 103, No. 6 1066-1072
© 1988 Japanese Biochemical Society

research-article

Amino-Terminal and Carboxyl-Terminal Half-Molecules of Ovotransferrin: Preparation by a Novel Procedure and Their Interactions

Hideo Oe, Etsushiro Doi and Masaaki Hirose1

The Research Institute for Food Science, Kyoto University Uji, Kyoto 611

1To whom correspondence should be addressed.

The amino- (N-) and carboxyl- (C-)terminal half-molecules of ovotransferrin were prepared by a novel procedure. The trypsin-nicked ovotransferrin (Ikeda et al. (1985) FEBS Lett. 182, 305–309), in which the two half-molecules interact non-covalently forming a stable dimer, was purified by gel filtration and anion-exchange column chromatography. By subsequent cation-exchange chromatography, the nicked form was distinctly separated into an equivalent amount of the N-terminal and C-terminal half-molecules. Analyses of the N-terminal and C-terminal sequences indicated that the N-terminal and C-terminal half-molecules comprised the alignments of residues 1–332 and 342–686 of ovotransferrin, respectively. Anion-exchange chromatography, gel filtration chromatography, and non-denaturing polyacrylamide gel electrophoresis revealed that the isolated half-molecules had the ability to re-associate in solution. The contents of {alpha}-helix and ß-sheet of the two half-molecules, as determined by circular dichroism (CD) spectra, were very similar to those of intact ovotransferrin. No prominent alteration in the secondary structure of the two half-molecules was induced by the re-association.


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