I believe that the reasoning behind the need to add genetically engineered
human lactoferrin to infant formula is because of the "iron" problem.  This
patent explains the uses of lactoferrin because of its iron-binding properties
that helps prevent the growth of various microorganisms.  In my opinion low iron
formulas are just as much an experiment on infants as any other infant
formula.  We take risks when using any kind of infant formula.  The level of risk is
what seems to be debatable.  I think the true risk in developed nations is
very much hidden.  The infant formula industry's continuous need to improve
infant formula is based on the deficiencies of their products.  Should we accept
that one infant formula is better than another?  This is the scientific quest
that the US government is funding--the quest for an infant formula better than
human milk (NICHD statement in 1990 in announcing grant funding for
lactoferrin investigation and its role in infant feeding).
Valerie W. McClain, IBCLC

http://www.uspto.gov/patft/index.html
patent # 6635447
"Production of recombinant lactoferrin and lactoferrin polypeptides using
cDNA sequences in various organisms"
inventor:  Conneely et al.
assignee:  Baylor College of Medicine

"1. Field of the Invention

The present invention relates generally to the field of iron-binding
glycoproteins. More specifically, the present invention relates to the recombinant
production of various lactoferrins.

2. Description of the Prior Art

Lactoferrin (LF) is an iron-binding glycoprotein found in milk and other
secretions and body fluids. It is one of a number of iron binding proteins,
sometimes referred to as transferring, and is involved in iron binding and delivery
in mammals.

Human lactoferrin (hLF) is a member of the transferrin family of iron-binding
monomeric glycoproteins. It was originally discovered in milk where it can
reach levels of 7 grams/liter in colostrum. LF has since been detected in other
external fluids of humans and other mammals. The fluids include tears, saliva
and mucosal secretions and also in the secondary granules of polymorphonuclear
leukocytes.

Lactoferrin has been implicated as a factor in resistance against enteritis
infections in suckled newborn humans. The bacteriocidal/bacteriostatic actions
are considered to be due at least in part to the iron binding properties of
lactoferrin. Lactoferrin decreases the iron availability to iron-requiring
microorganisms and thereby interferes with their growth and reproduction. At least
one non-iron-binding bactericidal domain has also been reported for human
lactoferrin. Lactoferrin is also considered to have antiviral properties and to
have other potential therapeutic applications.

LF is a 78 kilo Dalton (k Da) glycoprotein having a bilobal structure with a
high degree of homology between the C and N terminal halves which is evident
at both the amino acid and three dimensional structural level. Each of these
lobes can reversibly bind one ferric iron with high affinity and with the
concomitant binding of bicarbonate. The biological functions proposed for
lactoferrin include protection against microbial infection, enhanced intestinal iron
absorption in infants, promotion of cell growth, regulation of myelopoiesis and
modulation of inflammatory responses."





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