Abstract
When iron · lactoferrin and apolactoferrin were submitted to nitration with tetranitromethane, the number of unmodified tyrosine residues recovered upon acid hydrolysis was 4–5 in the former case against 0–1 in the latter. The iron‐binding capacity of lactoferrin appeared to remain intact following nitration of the iron‐containing form of the protein, whereas metal‐combining properties were destroyed when apolactoferrin was treated similarly.Tetranitromethane was found to cause changes in lactoferrin that went far beyond the mere nitration of a few tyrosine residues. Much of the tyrosine was destroyed and the same applied to tryptophan, part of which was converted to unidentified reaction products.
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