INTRODUCTION

Lactoferrin was first fractioned as an unknown red fraction from

cows milk by Sorensen & sorensen in 1939.
In 1960 the red protein from both human & bovine milk was
defined as a transferrin like glycoprotein.
It has also been shown to be a major iron binding protein of other
exocrine secretions.
Lactoferrrin is a glycoprotein with a MW of about 80 kDa.
Lactoferrin is comprised of a single polypeptide chain containing
703 amino acids folded into globular lobes.
Lobes are also c/d C-(carboxy) & N-(amino) terminal.
Each lobe consists of 2 domains k/n as C1,C2,N1 & N2.
The degree of glycosylation varies & determies the rate of
resistance to proteases or very low pH.

FORMS OF LACTOFERRIN
There are three forms of lactoferrin
they are as follows : Apolactoferrin (one iron free)
Monoferric form (one ferric form)
Halolactoferrin (binds 2 fe3+ ions)

LACTOFERRIN AS A TRANSFERRIN PROTEIN

Lactoferrin belongs to transferrin super family w/h includes
monomeric, non heme iron binding proteins.
Members of the transferrin family proteins are : Serotransferrin

Ovotransferrin (from egg white)

Melanotransferrin (melanoma cells)

Lactoferrin as a iron transporter.

The molecular mass of transferrin lies within the reported
range for lactoferrin.
Lactoferrin differs from transferrin in its immunologic or
antigenic properties.
Lactoferrin & transferrrin have similar C & N-terminal iron
binding domains consisting of beta sheets as well as alpha
helices.
The iron binding sites in the N & C lobes are similar:- 3
anionic ligands, 2 tyrosine & 1 aspartic amino acids.

Functions of lactoferrin
Lactoferrin helps regulate the absorption of iron in
the intestine and delivery of iron to the cells.
It also seems to protect against bacterial
infection, possibly by preventing the growth of
bacteria by depriving them of essential nutrients
or by killing bacteria by destroying their cell
walls.
In addition to bacterial infections, lactoferrin
seems to be active against infections causes by
some viruses and fungi.
Lactoferrin also seems to be involved with
regulation of bone marrow function
(myelopoiesis), and it seems to be able to boost

USES & SOURCES

USES
Lactoferrin is touted as a
natural remedy for a wide range
of health problems, including:

diarrhea
hepatitis C
osteoporosis
ulcers

In addition, lactoferrin is said to

stimulate the immune system,
treat iron deficiency, slow up
the aging process, promote the
growth of probiotic bacteria,
and aid in cancer prevention.

sources
When used in dietary
supplement form,
lactoferrin is typically
sourced from cow's milk or
genetically modified rice
or cow's milk.
There's some evidence
that colostrum (the first
milk produced by lactating
women after giving birth)
contains particularly high
levels of lactoferrin

Primary STRUCTURES
The amino acid sequence of lactoferrin
from various species are known till date.
A more characteristic feature of LFs is
their highly basic character w/h is
reflected with a sequence k/n as pI of 9.
The protien contains 6 -7 intramolecular
disulfide bridges with no sulfhydryl group.
LFs obtain from bovine, buffalo goat, &
sheep shares a sequence identity of 90%
with each other.

GLYCOSYLATION

TERTIARY STRUCTURE
Crystal structure of 5 LFs species shares the
same overall structure organisation.
The polypeptide chain folds into 2 distinct
lobes referred as N & C lobes.
Both the lobes have same folds consistent
with their sequence identity of 40%.
In each lobe, 2 alpha & beta domains referred
to as N1 & N2 & C1 & C2.
The 2 lobes are connected by a peptide linker
consisting of 10-12 residues that adopt the
confirmation of 3 turn of alpha helix.