Zone of diameters of LF, 21LF, 38LF and 45LF against <i>Candida albicans</i>.

<p>Zone of diameters of LF, 21LF, 38LF and 45LF against <i>Candida albicans</i>.</p

Zone of diameters of LF, 21LF, 38LF and 45LF against bacterial species.

<p>Zone of diameters of LF, 21LF, 38LF and 45LF against bacterial species.</p

LC₅₀ values of LF, 21LF, 38LF and 45LF against bacterial species.

<p>All the data were expressed as mean values ± standard deviations; <i>P</i><0.05, student's <i>t-</i> test.</p><p>*Highest concentration tested.</p

Antifungal activity of LF and its three tryptic fragments.

<p>The antifungal activity of (A) LF (•), (B) 21LF (♦), (C) 38LF (▾) and (D) 45LF (▪) is plotted against <i>C. albicans</i> ATCC 90028. All the data were expressed as mean values ± standard deviations; <i>P</i><0.05, student's <i>t-</i> test</p

Sequence comparison of the cleavage sites of LF from various species.

<p>The different species are human (HLF), bovine (CLF), buffalo (BLF), equine (ELF) and caprine LF (GLF). The identity in the sequences is shown in blue. The places where trypsin cleaves the molecules are indicated by an arrow.</p

The entire sequence of bovine native LF.

<p>Arrows [blue (21LF), green (38LF), red (45LF)] indicate the origin sites of the three fragments respectively. The amino acid sequence of the first fifteen residues of 21LF, 38LF and 45LF is indicated against their names towards the left,</p

Comparative study of iron-desaturation of LF and its three tryptic fragments.

<p>The iron desaturation was plotted against decrease in pH for iron saturated bovine lactoferrin (black), 21LF (orange), 38LF (green) and 45LF (red) and their corresponding apo form of bovine lactoferrin (blue), 21LF (brown), 38LF (pink), 45LF (cyan) under identical conditions.</p

LC₉₀ values of LF, 21LF, 38LF and 45LF against <i>Candida albicans</i>.

<p>All the data were expressed as mean values ± standard deviations; <i>P</i><0.05, student's <i>t-</i> test.</p

Superimposition of the backbone chains of iron-saturated LFs from various species.

<p>The figure shows that the overall chain folds in a similar fashion in all the species.</p

Elution profile during the purification of the hydrolyzate of bovine LF after trypsin digestion.

<p>Elution was performed using ion exchange chromatography by CM-Sephadex C-50 in 0.05 M Tris-HCl, pH 8.0. Peak 1 indicates the unbound fraction while Peak 2 is eluted in the bound fraction.</p