The formation of iron-binding fragments of hen ovotransferrin by limited proteolysis.
نویسنده
چکیده
1. Iron was added to hen ovotransferrin to 30% saturation and the protein was digested with trypsin or chymotrypsin. 2. Iron-binding fragments were isolated. They carried one atom of iron/mol (mol.wt. 35000) and consisted of a single polypeptide chain derived from the N-terminal half of the protein. Carbohydrate was not present. 3. The fragments were able to bind a variety of metals and to donate iron to reticulocytes.
منابع مشابه
Electron-paramagnetic-resonance spectroscopy of iron-binding fragments of hen ovotransferrins.
1. It is confirmed that there are two e.p.r. (electron-paramagnetic-resonance) signals associated with fully loaded ovotransferrin, which has two iron-binding sites. 2. Through experiments in which either of the two sites of whole ovotransferrin is occupied, the other being empty, the first occupied site is shown to belong to the N-terminal region of the protein; the second occupied site is in ...
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عنوان ژورنال:
- The Biochemical journal
دوره 141 3 شماره
صفحات -
تاریخ انتشار 1974