In-vitro digestion behaviour of iron saturated (holo)-, native- and iron depleted (apo)- bovine lactoferrin (LF) was studied in simulated oral, gastric and intestinal digestion conditions. All LFs were hydrolysed to <10 kDa peptides; 93% of iron was released from holo-LF within 2 h of gastric digestion. Iron binding ability of all the three LFs was decreased by 80-90% during gastric digestion, while antioxidant activities at the end of gastric digestion were 3-8 times higher than those at the end of oral and intestinal digestion. Antioxidant activity of apo-LF was higher than that of holo-LF after gastric and intestinal digestion. Gastric and intestinal digestion of all the three forms of LF produced negatively charged peptides or am...
Apo and holo forms of lactoferrin (LF) from caprine and bovine species have been characterized and c...
The current state, prospects for using and priorities in studying multifunctional protein lactoferri...
Lactoferrin is an iron-binding protein present in large quantities in colostrum and in breast milk, ...
Lactoferrin (LF) is a multifunctional protein occurring in many biological secretions including milk...
Lactoferrin (LF) is a multifunctional protein occurring in many biological secretions including milk...
Human and bovine lactoferrin (hLf and bLf) are multifunctional iron-binding glycoprotein constitut...
Lactoferrin (Lf) samples from several manufacturers were evaluated in vitro. The purity and protein ...
Lactoferrin is an 80 kDa bilobal, iron binding glycoprotein which is primarily antimicrobial in natu...
Complex coacervates of bovine lactoferrin (LF) and sodium alginate (NaAlg) were prepared aiming to p...
J Nutr 2001 Aug;131(8):2101-4 Related Articles, Books, LinkOut Gastric digestion of bovine lactofer...
Recently there is an increasing realization that dietary proteins may affect health beyond their mer...
Oral delivery is the most common method for bovine lactoferrin (bLf) administration. However, the pr...
Lactoferrin (LF) is a non-heme iron-binding protein that is a pari of the transferrin protein family...
The heat denaturation of Fe-saturated lactoferrin (If) and Fe-free lactoferrin (apo-lf) was studied ...
In this thesis, the structure, stability and digestion of caprine and bovine lactoferrin were compar...
Apo and holo forms of lactoferrin (LF) from caprine and bovine species have been characterized and c...
The current state, prospects for using and priorities in studying multifunctional protein lactoferri...
Lactoferrin is an iron-binding protein present in large quantities in colostrum and in breast milk, ...
Lactoferrin (LF) is a multifunctional protein occurring in many biological secretions including milk...
Lactoferrin (LF) is a multifunctional protein occurring in many biological secretions including milk...
Human and bovine lactoferrin (hLf and bLf) are multifunctional iron-binding glycoprotein constitut...
Lactoferrin (Lf) samples from several manufacturers were evaluated in vitro. The purity and protein ...
Lactoferrin is an 80 kDa bilobal, iron binding glycoprotein which is primarily antimicrobial in natu...
Complex coacervates of bovine lactoferrin (LF) and sodium alginate (NaAlg) were prepared aiming to p...
J Nutr 2001 Aug;131(8):2101-4 Related Articles, Books, LinkOut Gastric digestion of bovine lactofer...
Recently there is an increasing realization that dietary proteins may affect health beyond their mer...
Oral delivery is the most common method for bovine lactoferrin (bLf) administration. However, the pr...
Lactoferrin (LF) is a non-heme iron-binding protein that is a pari of the transferrin protein family...
The heat denaturation of Fe-saturated lactoferrin (If) and Fe-free lactoferrin (apo-lf) was studied ...
In this thesis, the structure, stability and digestion of caprine and bovine lactoferrin were compar...
Apo and holo forms of lactoferrin (LF) from caprine and bovine species have been characterized and c...
The current state, prospects for using and priorities in studying multifunctional protein lactoferri...
Lactoferrin is an iron-binding protein present in large quantities in colostrum and in breast milk, ...