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Iron chelation by digests of insoluble chicken muscle protein: the role of histidine residues
Author(s) -
Seth Anahita,
Mahoney Raymond R
Publication year - 2000
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/1097-0010(20010115)81:2<183::aid-jsfa799>3.0.co;2-1
Subject(s) - histidine , chelation , chemistry , ferrous , biochemistry , ferric , amino acid , organic chemistry
The role of histidine residues in the chelation of iron at neutral pH by peptides from chicken muscle was investigated to see if it could contribute to the effect of muscle tissue on iron absorption. When ferric iron was chelated by L ‐histidine at pH 6, the ratio of iron chelated to loss of reactive histidine was 1:1. Chelation of iron by soluble peptides in a digest of insoluble chicken muscle protein was accompanied by a small loss of reactive histidine (4–7%) in the peptides. When peptides were modified with diethylpyrocarbonate, increasing loss of histidine led to a progressive decrease in iron chelation. However, even 89% loss of histidine only reduced iron chelation by 30%. It was concluded that histidyl residues do contribute to iron chelation and therefore could by involved in the promotion of iron absorption by muscle tissue. However, other amino acid residues are likely to be involved. © 2000 Society of Chemical Industry