Immunochemical Reactions of Conalbumin and its Metal Complexes

Tengerdy, C.; Azari, Parviz; Tengerdy, Robert P.

doi:10.1038/211203a0

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1971

1985

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Cited by 12 publications

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“…Charlwood-(1971) found that iron binding causes a 1.8 % increase in the sedimentation coefficient of human transferrin, the increase being divided into two approximately equal steps which accompany the binding of the two metal atoms. Immunological reactivity has also been found to change on iron binding (Tengerdy et al, 1966). Ofthe greatest interest in the present context was the finding by Fraenkel-Conrat (1950) and by Azari & Feeney (1958) that iron-saturated ovotransferrin is very resistant to proteolysis by trypsin and chymotrypsin, whereas native apo-ovotransferrin undergoes rapid digestion.…”

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confidence: 74%

The formation of iron-binding fragments of hen ovotransferrin by limited proteolysis

Williams

1974

Biochemical Journal

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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.

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confidence: 74%