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Bullen Jj

Bio: Bullen Jj is an academic researcher from National Institute for Medical Research. The author has contributed to research in topics: Iron-binding proteins & Escherichia coli infection. The author has an hindex of 2, co-authored 2 publications receiving 596 citations.

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Journal Article
TL;DR: It seems that iron-binding proteins in milk may play an important part in resistance to infantile enteritis caused by E. coli.
Abstract: Human milk contains large quantities of iron-binding protein, of which the greater proportion is lactoferrin, though small amounts of transferrin are also present. Three samples of human milk with unsaturated iron-binding capacities of between 56 and 89% had a powerful bacteriostatic effect on Escherichia coli O111/B4. The bacteriostatic properties of milk were abolished if the iron-binding proteins were saturated with iron. Purified human lactoferrin, in combination with specific E. coli antibody, strongly inhibited the growth of E. coli, and this effect was also abolished by saturating the lactoferrin with iron. Guinea-pig milk also contains lactoferrin and transferrin. Newly born guinea-pigs fed on an artificial diet and dosed with E. coli O111 had higher counts of E. coli O111 in the intestine than suckled animals. The apparent suppressive effect of guinea-pig milk on E. coli in the intestine could be reversed by feeding the iron compound haematin. It seems that iron-binding proteins in milk may play an important part in resistance to infantile enteritis caused by E. coli.

562 citations

Journal ArticleDOI
TL;DR: It seems that iron-binding proteins in milk may play an important part in resistance to infantile enteritis caused by E. coli.
Abstract: Human milk contains large quantities of iron-binding protein, of which the greater proportion is lactoferrin, though small amounts of transferrin are also present. Three samples of human milk with unsaturated iron-binding capacities of between 56 and 89% had a powerful bacteriostatic effect on Escherichia coli O111/B4. The bacteriostatic properties of milk were abolished if the iron-binding proteins were saturated with iron. Purified human lactoferrin, in combination with specific E. coli antibody, strongly inhibited the growth of E. coli, and this effect was also abolished by saturating the lactoferrin with iron.Guinea-pig milk also contains lactoferrin and transferrin. Newly born guinea-pigs fed on an artificial diet and dosed with E. coli O111 had higher counts of E. coli O111 in the intestine than suckled animals. The apparent suppressive effect of guinea-pig milk on E. coli in the intestine could be reversed by feeding the iron compound haematin. It seems that iron-binding proteins in milk may play an important part in resistance to infantile enteritis caused by E. coli.

35 citations


Cited by
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Journal ArticleDOI
TL;DR: Tannin toxicity for fungi, bacteria and yeasts is reviewed and compared to toxicity of related lower molecular weight phenols and the dependence of toxicity on tannin structure is examined.

2,129 citations

Journal ArticleDOI
TL;DR: This review summarises current knowledge of granule biology and highlights the effects of neutrophil degranulation in the acute inflammatory response.

1,117 citations

Journal ArticleDOI
TL;DR: An overview of how probiotics, prebiotics, and synbiotics may contribute toward nutritional modulation of the gut microecology, with emphasis on the neonatal intestine where appropriate is provided.

916 citations

Journal ArticleDOI
TL;DR: Lactoferrin has been proposed to play a role in iron uptake by the intestinal mucosa and to act as a bacteriostatic agent by withholding iron from iron-requiring bacteria.
Abstract: Lactoferrin is an 80-kDa, iron-binding glycoprotein present in milk and, to a lesser extent, in exocrine fluids such as bile and tears. It consists of a single-chain polypeptide with two gobular lobes and is relatively resistant to proteolysis. The complete cDNAs for lactoferrin from human milk, neutrophils, and bovine milk have been reported, and recombinant proteins have been produced. Owing to its iron-binding properties, lactoferrin has been proposed to play a role in iron uptake by the intestinal mucosa and to act as a bacteriostatic agent by withholding iron from iron-requiring bacteria. Its presence in neutrophils and its release during inflammation suggest that lactoferrin is also involved in phagocytic killing and immune responses. Additionally, lactoferrin may function in ways not related to iron-binding, e.g. as a growth factor and as a bactericidal agent. This review attempts to evaluate these proposed functions and their biological significance in more detail.

766 citations

Journal ArticleDOI
TL;DR: This work reviews the scientific literature and attempts to stimulate consideration of the continued use of bioactive peptides and their expanded development as a commercial product.

695 citations