Serum Lactoferrin and Immunoglobulin G Concentrations in Healthy or Ill Neonatal Foals and Healthy Adult Horses

Barton, Michelle Henry; Hurley, David J.; Norton, Natalie; Heusner, Gary L.; Costa, Lais R. R.; Jones, Samuel L.; Byars, Doug; Watanabe, Kiyotaka

doi:10.1111/j.1939-1676.2006.tb00766.x

Cited by 14 publications

(13 citation statements)

References 22 publications

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“…colostrums and milk have been also measured. The obtained results were 21.7 μg/mL, and 0.82 g/kg, respectively (Malacarne et al, 2002;Barton et al, 2006). The mean milk Lfe concentration was reported to be 0.229±0.135 mg/mL in the camel (Konuspayeva et al, 2007).…”

Section: Discussionmentioning

confidence: 60%

Lactoferrin Concentration in Buffalo Milk

Giacinti

Basiricò

Ronchi

et al. 2013

Italian Journal of Animal Science

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The objective of this study was to quantify lactoferrin (Lfe) in buffalo milk and to examine the factors affecting milk Lfe, such as the lactation stage, daily milk yield, parity, and milk somatic cells count (SCC). Milk Lfe concentration was detected by the SDS-polyacrilamide gel electrophoresis (SDS-PAGE). The overall mean of Lfe concentration was 0.332±0.165 g/kg and ranged from 0.030 to 0.813 g/kg. Milk Lfe concentrations increased (P<0.01) with the increase of days in milk, but it was not affected by parity. Milk Lfe concentration was significantly affected by SCC. The differences became significant when the levels of SCC increased up to 200,000/mL. This is the first investigation on the levels of Lfe in buffalo milk in reference to daily milk production, lactation stage, parity and SCC. Further studies are needed to clarify the relationship between Lfe and SCC in buffalo milk.

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Section: Discussionmentioning

confidence: 60%

Lactoferrin Concentration in Buffalo Milk

Giacinti

Basiricò

Ronchi

et al. 2013

Italian Journal of Animal Science

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“…The obtained results were 21.7 μg/ml, 0.249 μg/ml, and 0.445 μg/ml, respectively (Barton et al, 2006). The mean milk lactoferrin concentration was reported to be 0.229 ± 0.135 mg/ml in the camel (Konuspayeva et al, 2007).…”

Section: Lactoferrin In Different Speciesmentioning

confidence: 62%

Lactoferrin: a review

Adlerova¹,

Bartošková²,

Faldyna³

2008

Vet. Med.

265

217

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This review discusses the biological properties of the glycoprotein lactoferrin. Lactoferrin has been identified in secretions from exocrine glands and in specific granules of neutrophils. After degranulation, neutrophils become the main source of lactoferrin in blood plasma. Lactoferrin possesses various biological functions, including roles in iron metabolism, cell proliferation and differentiation, and antibacterial, antiviral, and antiparasitic activity. Many of these functions do not appear to be connected with its iron binding ability. Of late, lactoferrin concentrations have been measured mostly in humans but also in some other species. However, the relationship between its concentration and physiological or pathological effects on body functions is not yet well characterised.

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“…It is also found in the specific granules of neutrophilic leucocytes . It plays an important role as an antimicrobial molecule by sequestering iron with a very high affinity , and has also been shown to be involved in immune and inflammatory responses . The bilobal structure of lactoferrin is designed to double its iron‐sequestering capacity.…”

Section: Introductionmentioning

confidence: 99%

Structure of the iron‐free true C‐terminal half of bovine lactoferrin produced by tryptic digestion and its functional significance in the gut

et al. 2014

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Bovine lactoferrin, a 76-kDa glycoprotein (Ala1-Arg689) consists of two similar N-and C-terminal molecular halves with the ability to bind two Fe 3+ ions. The N-terminal half, designated as the N-lobe (Ala1-Arg341) and the C-terminal half designated as the C-lobe (Tyr342-Arg689) have similar iron-binding properties, but the resistant C-lobe prolongs the physiological role of bovine lactoferrin in the digestive tract. Here, we report the crystal structure of true C-lobe, which was produced by limited proteolysis of bovine lactoferrin using trypsin. In the first proteolysis step, two fragments of 21 kDa (Glu86-Lys282) and 45 kDa (Ser283-Arg689) were generated because two lysine residues, Lys85 and Lys282, in the structure of iron-saturated bovine lactoferrin were fully exposed. The 45-kDa fragment was further digested at the newly exposed side chain of Arg341, generating a 38-kDa perfect C-lobe (Tyr342-Arg689). By contrast, the apo-lactoferrin was cut by trypsin only at Arg341, which was exposed in the structure of apo-lactoferrin, whereas the other two sites with Lys85 and Lys282 are inaccessible. The purified iron-saturated C-lobe was crystallized at pH 4.0. The structure was determined by the molecular replacement method using coordinates of the C-terminal half (Arg342-Arg689) of intact camel apolactoferrin. The structure determination revealed that the iron atom was absent and the iron-binding cleft was found in a wide-open conformation, whereas in the previously determined structure of iron-saturated C-lobe of bovine lactoferrin, the iron atom was present and the iron-binding site was in the closed confirmation. Structured digital abstract• trypsin cleaves lactoferrin by enzymatic study (View interaction)

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Serum Lactoferrin and Immunoglobulin G Concentrations in Healthy or Ill Neonatal Foals and Healthy Adult Horses

Cited by 14 publications

References 22 publications

Lactoferrin Concentration in Buffalo Milk

Lactoferrin Concentration in Buffalo Milk

Lactoferrin: a review

Structure of the iron‐free true C‐terminal half of bovine lactoferrin produced by tryptic digestion and its functional significance in the gut

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