Proteins

Dr.Mahr-un -nisa
Proteins-----AA
Proteins are made from 20 different amino acids,
9 of which are essential.
Each amino acid has an amino group, an acid
group, a hydrogen atom, and a side group.
It is the side group that makes each amino acid
unique.
The sequence of amino acids in each protein
determines its unique shape and function.
 Amino Acids
Have unique side groups that result in
differences in the size, shape and electrical
charge of an amino acid
Nonessential amino acids, also called
dispensable amino acids, are ones the
body can create.
Nonessential amino acids include alanine,
arginine, asparagines, aspartic acid, cysteine,
glutamic acid, glutamine, glycine, proline,
serine, and tyrosine.
 Amino Acids
Essential amino acids, also called indispensable
amino acids, must be supplied by the foods people
consume.
Essential amino acids include histidine, isoleucine,
leucine, lysine, methionine, phenyalanine, threonine,
tryptophan, and valine.
Conditionally essential amino acids refer to amino
acids that are normally nonessential but essential
under certain conditions.
 Amino Acid Requirements of Humans
--------------------------------------------------------------------
Nutritionally Essential Nutritionally Nonessential
--------------------------------------------------------------------
Argininea Alanine
Histidine Asparagine
Isoleucine Aspartate
Leucine Cysteine
Lysine Glutamate
Methionine Glutamine
Phenylalanine Glycine
Threonine Proline
Tryptophan Serine
Valine Tyrosine
---------------------------------------------------------------------
a
Nutritionally semiessential. Synthesized at rates
inadequate to support growth of children.
What is protein
Proteins
Amino acid chains are linked by peptide bonds in
condensation reactions.
Dipeptides have two amino acids bonded together.
Tripeptides have three amino acids bonded together.
Polypeptides have more than two amino acids bonded
together.
Amino acid sequences are all different, which
allows for a wide variety of possible sequences.
Peptide bond

M. Zaharna Clini.
Chem. 2009
The Chemists View of Proteins
Proteins
Protein Shapes
Hydrophilic side groups are attracted to water.
Hydrophobic side groups repel water.
Coiled and twisted chains help to provide
stability.
Classification of protein
Proteins are polymers of amino acids produced
by living cells in all forms of life.
A large number of proteins exist with diverse
functions, sizes, shapes and structures but each
is composed of essential and non-essential
amino acids in varying numbers and sequences.
The number of distinct proteins within one cell is
estimated at 3,000 - 5,000
The most abundant organic molecule in cells (50-70%
of cell dry weight)
M. Zaharna Clini.
Chem. 2009
Size
A typical protein contains 200-300
amino acids, but some are much
smaller and some are much larger
Proteins range in molecular weight from
6,000 Daltons (insulin) to millions of
Daltons (structural proteins)

M. Zaharna Clini.
Chem. 2009
 Protein Structure
Primary structure
sequence of AA
In order to function properly,
proteins must have the correct
sequence of amino acids.
e.g when valine is substituted
for glutamic acid in the chain
of HbA, HbS is formed, which
results in sickle-cell anemia.

M. Zaharna Clini.
Chem. 2009
 Secondary structure
Initial helical folding
Beta pleated sheet
Held together by
Hydrogen bonding

M. Zaharna Clini.
Chem. 2009
Tertiary Structure
Chain folds back on itself
to form 3D structure
Interaction of R groups
Responsible for biologic
activity of molecule

M. Zaharna Clini. Chem. 2009

Quaternary structure
2 or more polypeptide chains
binding together
eg. Hemoglobin
Hemoglobin has 4 subunits
Two chains
Two chains
Many enzymes have
quaternary structures

M. Zaharna Clini. Chem. 2009

Classification by Protein
Structure
Simple Proteins (contain only amino
acids) are classified by shape as
Globular proteins: compact, tightly
folded and coiled chains
Majority of serum proteins are globular
Fibrous proteins: elongated, high
viscosity (hair, collagen)

M. Zaharna Clini.
Chem. 2009
Classification by Protein
Structure
Conjugated proteins contain non-amino
acid groups
Amino acid portion is called apoprotein and
non-amino acid portion is called the
prosthetic group
It is the prothetic groups that define the
characteristics of these proteins.
Name of the conjugated protein is derived
from the prosthetic group
M. Zaharna Clini.
Chem. 2009
 Conjugated Proteins

Classification Prosthetic Example

group
Lipoprotein Lipid HDL
Glycoprotein Carbohydrates Immunoglo-
bulins
Phosphoprotein Phosphate Casein of
milk
M. Zaharna Clini.
Chem. 2009
Functions of proteins
Generally speaking, proteins do everything in the living cells
Functional classification of plasma proteins is useful in
understanding the changes that occur in disease:
Tissue nutrition

Proteins of immune defense

Antibodies
Acute phase proteins
Proteins associated with inflammation
Transport proteins( albumin, transferrin)
Proteins used to bind and transport
Hemostasis
Proteins involved in forming clots and acting very closely with
complement
M. Zaharna Clini.
Chem. 2009
Functions of proteins
Regulatory
( receptors, hormones )
Catalysis,
enzymes
Osmotic force
Maintenance of water distribution between cells
and tissue and the vascular system of the body
Acid-base balance
Participation as buffers to maintain pH
Structural, contractile, fibrous and keratinous
M. Zaharna Clini.
Chem. 2009
Monogastric Protein Digestion
Whole proteins are not absorbed
Too large to pass through cell membranes
intact H O
H3N+ C C
H O
R
Digestive enzymes N
H
C
R
C
H O

Hydrolyze peptide bonds N

H
C C
O
R
Secreted as inactive pre-enzymes
Prevents self-digestion
Monogastric Protein Digestion
Initiated in stomach
HCl from parietal cells
Stomach pH 1.6 to 3.2
Denatures 40, 30, and 20 structures
Pepsinogen from chief cells
HCl
Pepsinogen Pepsin
Cleaves at phenylalanine, tyrosine, tryptophan

Aromatic amino acids

Protein leaves stomach as mix of insoluble protein, soluble

protein, peptides and amino acids
Protein Digestion Small Intestine
Pancreatic enzymes secreted
Trypsinogen
Chymotrypsinogen
Procarboxypeptidase Zymogens
Proelastase
Collagenase
 Monogastric Digestion
Small Intestine
Zymogens must be converted to active form
Trypsinogen Enteropeptidase/Trypsin Trypsin
Endopeptidase
Cleaves on carbonyl side of Lys & Arg
Trypsin
Chymotrypsinogen Chymotrypsin
Endopeptidase
Cleaves carboxy terminal Phe, Tyr and Trp
Trypsin
Procarboxypeptidase Carboxypeptidase
Exopeptidase
Removes carboxy terminal residues
Protein Digestion
Small intestine (brush border)
Aminopeptidases
Cleave at N-terminal AA

Dipeptidases
Cleave dipeptides

Enterokinase (or enteropeptidase)

Trypsinogen trypsin
Trypsin then activates all the other enzymes
Trypsin Inhibitors
Small proteins or peptides
Present in plants, organs, and fluids
Soybeans, peas, beans, wheat
Pancreas, colostrum
Block digestion of specific proteins
Inactivated by heat
Protein Digestion
Proteins are broken down to
Tripeptides
Dipeptides
Free amino acids
 Free Amino Acid Absorption
Free amino acids
Carrier systems
Neutral AA
Basic AA Na+ Na+
Acidic AA
Imino acids
Entrance of some AA
is via active transport
Requires energy
 Peptide Absorption
Form in which the majority
of protein is absorbed
More rapid than absorption
of free amino acids
Active transport
Energy required
Metabolized into free amino
acids in enterocyte
Only free amino acids
absorbed into blood
Absorption of Intact Proteins
Newborns
First 24 hours after birth
Immunoglobulins
Passive immunity
Adults
Para cellular routes
Tight junctions between cells
Intracellular routes
Endocytosis
Pinocytosis
Of little nutritional significance...
Affects health (allergies and passive immunity)
 Protein Transport in the Blood
Amino acids diffuse across the
basolateral membrane
Enterocytes portal blood liver
tissues
Transported mostly as free amino acids
Liver
Breakdown of amino acids
Synthesis of non-essential amino acids
Overview of Protein Digestion and
Absorption in Monogastrics

Groff & Gropper, 2000

 OVERVIEW OF AMINO ACID METABOLISM

ENVIRONMENT
ORGANISM

Bio-
Ingested synthesis Protein
protein
2 3
1
a
AMINO
ACIDS
b
c c Purines
Degradatio Pyrimidines
n Porphyrins
(required)
Carbon
Nitrogen
skeletons
(ketogenic) (glucogenic)
Urea Used for
energy pyruvate
acetoacetate -ketoglutarate
acetyl CoA succinyl-CoA
fumarate
oxaloacetate
 Amino Acid Catabolism
Deamination of Amino Acids
removal of the a-amino acids
Oxidative Deamination
Non-oxidative Deamination
Transamination
TRANSAMINATION
The term amphibolic is used to describe a biochemical
pathway that involves both catabolism and anabolism
Reductive amination catalyzed by
glutamate dehydrogenase (this is physiological important
becouse high conc. Of NH4 ion are cytotoxic)
Glutamine synthesis is coupled to
hydrolysis of ATP
Pyruvate is an amphibolic intermediate
in synthesis of alanine
Glutamte dehydrogenase, glutamine synthetase and
aminotranferases play central roles in amino acid
biostynthsis

The combined action of the above said

enzymes converts inorganic ammonium
ion in to the -amino nitrogen of AA
Asparagine synthesis is energetically
favorable due to coupling to ATP
hydrolysis
Serine biosynthesis(oxidation of the -hydroxyl group
of the glycolytic intermidiate 3-phosphoglycerate by 3-phosphoglycerate
dehygrogenase convert it to 3-phosphohydroxypuruvate. Transamination and

subsequent dephosphorylation is strongly favored )

Multistep pathway for glycine biosynthesis
Glycine is also synthesized from serine
 O-

O C
H2 H2
Cysteine is CH C C S CH3

not +NH3
nutritionally
essential,
however it
is derived
from
methionine
Tyrosine is
formed
from
phenylalanine
Hydroxyproline is formed after protein
synthesis
Selenocysteine is synthesized from serine
and selenophosphate
Amino acids that are synthesized de novo in humans.
All are related by a small number of steps to glycolysis
or TCA cycle intermediates.
Salvage pathways for formation of certain
nonessential amino acids from other amino acids

Amino Acid formed Precursor Amino Acid

Arginine Proline

Cysteine Methionine

Tyrosine Phenylalanine
 NITROGEN BALANCE

Nitrogen balance = nitrogen ingested - nitrogen excreted

(primarily as protein) (primarily as urea)

Nitrogen balance = 0 (nitrogen equilibrium)

protein synthesis = protein degradation

Positive nitrogen balance

protein synthesis > protein degradation

Negative nitrogen balance

protein synthesis < protein degradation
 UREA CYCLE

mitochondria
cytosol

Function: detoxification of ammonia

(prevents hyperammonemia)
 FATE OF THE CARBON SKELETONS

Carbon skeletons are used for

energy.

Glucogenic: TCA cycle

intermediates(gluconeogensis)

Ketogenic: acetyl CoA, acetoacetyl

CoA, or acetoacetate
Protein synthesis
On-going, semicontinuous activity in all
cells but rate varies greatly between
tissues
Rate of protein synthesis
Ks (%/d)
Tissue Pig Steer

Liver 23 21
Gut 45 39
Muscle 5 2
Ks = fraction of tissue protein synthesized per
day
Protein synthesis
On-going, semicontinuous activity in all cells
but rate varies greatly between tissues
Rate is regulated by hormones and supply of
amino acids and energy
Energetically expensive
requires about 5 ATP per one peptide bond
Accounts for about 20% of whole-body
energy expenditure
Protein degradation
Also controlled by hormones and energy
status
Method to assist in metabolic control
turns off enzymes
Protein synthesis and
degradation
Synthesis must exceed degradation for
net protein deposition or secretion
Changes in deposition can be achieved
by different combinations of changes in
synthesis and degradation
Changes in deposition
Synthesis Degradation Deposition

No change

No change

No change
Protein synthesis and
degradation
Synthesis must exceed degradation for
net protein deposition or secretion
Changes in deposition can be achieved
by different combinations of changes in
synthesis and degradation
Allows for fine control of protein
deposition
Proline biosynthesis(the initial reaction of proline biosynthsis converts the
-carboxyl group of glutamate to the mixed acid anhydride of glutamate -phospate.
Subsequent reduction form glutamate - semialdehyde,, which following
spontaneously cyclization is reduced to L-Proline )
Protein synthesis and
degradation
Other possible reasons for evolution of
protein turnover include
Allows post-translational conversion of
inactive peptides to active forms (e.g.,
pepsinogen to pepsin)
Minimizes possible negative consequences
of translation errors
Protein catabolism
Some net catabolism of body proteins
occurs at all times
Expressed as urinary nitrogen excretion
yields urea
Minimal nitrogen excretion is termed
endogenous urinary nitrogen (EUN)
Urinary nitrogen excretion
LIVER
Amino acids keto acids
NH3
CO2

Urea

Blood

KIDNEY Urea

Urine
Protein Synthesis
Protein Synthesis
Synthesis= the process of building or
making
DNA= (deoxyribonucleic acid) the
genetic code or instructions for the cell
RNA= ribonucleic acid
Amino Acids= building blocks of
proteins
DNA RNA

Deoxyribonucleic Acid Ribonucleic Acid

Sugar=deoxyribose Sugar= ribose

Contains 1 more H atom
than deoxyribose
Double stranded Single stranded- a single
strand of nucleotides
Nitrogen bases: ATCG Nitrogen bases: AUCG
U=Uracil
http://image
s2.clinicaltoo
ls.com/imag
es/gene/dna
_versus_rna
_reversed.jp
g
http://www.princeton.e
du/%7Ehos/images/rna
 STEP 1: TRANSCRIPTION= making RNA
Location: Eukaryotes-nucleus
Prokaryotes-cytoplasm

1. RNA polymerase binds to the genes

promoter
2. The two DNA strands unwind and
separate.
3. Complementary nucleotides are
added using the base pairing rules
EXCEPT:
A=U
Try this example.
Using the following DNA sequence,
what would be the complementary RNA
sequence?
ATCCGTAATTATGGC
UAGGCAUUAAUACCG
http://www.odec.ca/projects/2004/mcgo4s0/public_html/t3/mRNA%20to%20protein.gif
 1. Messenger RNA= mRNA is a form of
RNA that carries the instructions for making
the protein from a gene and delivers it to the
site of translation.
Codon= three nucleotide sequence
Transfer RNA= tRNA single strands of RNA
that temporarily carry a specific amino acid
on one end and has an anticodon
Anticodon-a 3 nucleotide sequence that is
complementary to an mRNA codon
Ribosomal RNA= rRNA- a part of the
structure of ribosomes
 Codon and Anticodon
Codon-found on mRNA Anticodon-found on tRNA

http://images.google.com/imgres?imgurl=http://www.obg
ynacademy.com/basicsciences/fetology/genetics/images/c
odon_GCA.gif&imgrefurl=http://www.obgynacademy.com
/basicsciences/fetology/genetics/&usg=__4MvAO2N3sXbE
RXQwODVDSqtsOjM=&h=160&w=168&sz=4&hl=en&start
=5&tbnid=toyuIN8drVBr4M:&tbnh=94&tbnw=99&prev=/i
mages%3Fq%3Dcodon%26gbv%3D2%26hl%3Den

http://www.microbelibrary.org/microbelibrary/files/ccImages/Articlei
mages/kaiser/tRNA_arg.jpg
STEP 2-TRANSLATION-
Assembling proteins- in the
cytoplasm
mRNA leaves nucleus and enters cytoplasm
tRNA molecules with the complementary
anticodon and a specific amino acid arrives at
the ribosome where the mRNA is waiting.
Peptide bond forms between amino acids
tRNA molecule leaves and a new one comes
with another amino acid.
Amino acids continue to attach together until
the stop codon and a protein is formed
 SUMMARY
Transcription= process of making RNA
from DNA
Translation= RNA directions are used to
make a protein from amino acids

DNARNA Protein
Transcription Translation
Cytoplasm on
nucleus
ribosome
DNA RNA

Deoxyribonucleic Acid Ribonucleic Acid

Sugar=deoxyribose Sugar= ribose

Contains 1 more H atom
than deoxyribose
Double stranded Single stranded- a single
strand of nucleotides
Nitrogen bases: ATCG Nitrogen bases: AUCG
U=Uracil
Video Clips
http://www.youtube.com/watch?v=KvY
EqGb7XN8&feature=related
http://www.youtube.com/watch?v=B6O
6uRb1D38&feature=related
DNA Replication RNA Transcription

DNA polymerase is used. RNA polymerase is used.

DNA nucleotides are RNA nucleotides are

linked. linked.
A DNA molecule is An RNA molecule is
made. made.
Both DNA strands serve Only one part of one
as templates. strand of DNA ( a gene)
is used as a template.
Explain the steps in protein synthesis.

http://stemcells.nih.go
v/info/scireport/image
s/figurea6.jpg
 Ruminant Protein Digestion
Ruminants can exist with limited dietary
protein sources due to microbial protein
synthesis
Essential amino acids synthesized
Microbial protein is not sufficient during:
Rapid growth
High production
Protein in the Ruminant Diet
Types of protein:
Dietary protein contains amino acids
Rumen Degradable Protein (RDP) available for use by
rumen microbes
Rumen Undegradable Protein (RUP) escapes rumen
fermentation; enters small intestine unaltered
Varies with diet, feed processing
Dietary non-protein nitrogen (NPN) not true
protein; provides a source of nitrogen for
microbial protein synthesis
Relatively CHEAP - decreases cost of protein
supplementation
Ruminant Protein Feeding
Feed the rumen microbes first (RDP)
Two counteractive processes in rumen
Degradation of (dietary) protein
Synthesis of microbial protein
Feed proteins that will escape fermentation to
meet remainder of animals protein requirements
Escape protein, bypass protein, or
rumen undegradable protein (RUP)
Aldehydes increase inter-protein cross-linking
Heat treatment
Utilization depends on
Digestibility of RUP source in the small intestine
Protein quality
Protein Degradation in Rumen
Feedstuff % Degraded
in 2 hours
Urea 100
Alfalfa (fresh) 90
Wheat Grain 78
Soybean Meal 65
Corn Grain 48
Blood Meal 18
Rumen Protein Utilization
Factors affecting ruminal degradation
Rate of passage
Rate of passage degradation
Solubility in water
Must be solubilized prior to degradation
Heat treatment
Degradation
N (and S) availability
Energy availability (carbohydrates)
Protein Fractions
Dietary proteins classified based on
solubility in the rumen
A
NPN, instantly solubilized/degraded
B1 B2 B3
Potentially degradable
C
Insoluble, recovered in ADF, undegradable
Ruminant Protein Digestion
Rumen microbes use dietary protein
Creates difference between protein quality in feed
and protein actually absorbed by host
Microbes break down dietary protein to
Amino acids
NH3, VFAs, and CO2
Microbes re-synthesize amino acids
Including all the essential amino acids from NH3 and
carbon skeletons

No absorption of protein or amino acids from

rumen (or from cecum or large intestine!)
Protein Hydrolysis by
Rumen Microbes
Process with multiple steps
Insoluble protein is solubilized when possible
Peptide bonds of solubilized protein are cleaved
Microbial endo- and exo-peptidases
Amino acids and peptides released
Peptides and amino acids absorbed rapidly by
bacteria
Bacteria degrade into ammonia N (NH3)
NH3 used to produce microbial crude protein (MCP)
Microbial Crude Protein (MCP)
Protein produced by microbial synthesis in
the rumen
Primary source of protein to the ruminant
animal
Microbes combine ammonia nitrogen and
carbohydrate carbon skeleton to make
microbial crude protein
Diet affects the amount of nitrogen
entering the small intestine as microbial
crude protein
Factors Limiting Microbial
Protein Synthesis
Amount of energy
ATP
Available nitrogen
NPN
Degraded feed intake protein nitrogen (RDP)
Available carbohydrates
Carbon residues for backbone of new amino acid

Microbial crude protein synthesis relies on synchronization

of carbohydrate (for carbon backbones) and nitrogen
availability (for amino group)
 Microbial Protein Synthesis
Synchronization of carbohydrate and N availability
NPN supplementation
Carbohydrates used for carbon skeleton of amino acids
Concentration

VFA (CHO fermentation)

Blood NH3
Rumen NH3
Carbon backbone
(from CHO fermentation)
Time post-feeding
Adapted from Van Soest, 1994
 Microbial Protein Formation
Dietary Dietary Cellulose
Starch Sugar Hemicellulose
rapid slow

Dietary Carbon Skeletons Sulfur Other Co-factors

NPN
rapid
NH3 Microbial
Proteins
ATP
Amino Acids
slower very Dietary
Dietary slow Insoluble RDP
Soluble RDP
Nitrogen Recycling
Excess NH3 is absorbed
through the rumen wall to the blood
Quickly converted to urea in the liver
Excess NH3 may elevate blood pH
Ammonia toxicity
Costs energy
Urea (two ammonia molecules linked together)
Relatively non-toxic
Excreted in urine
Returned to rumen via saliva (rumination important)
Efficiency of nitrogen recycling decreases with
increasing nitrogen intake
Nitrogen Recycling
Nitrogen is continually recycled to rumen for
reutilization
Ability to survive on low nitrogen diets
Up to 90% of plasma urea CAN be recycled to
rumen on low protein diet
Over 75% of plasma urea will be excreted on high
protein diet
Plasma urea enters rumen
Saliva
Diffuses through rumen wall from blood
Urease
Urea Ammonia + CO2
 Feed Protein,
NPN and CHO

RUP
Feed AA
Protein
Feed RDP
NH3/NH4 NH3
Protein
Feed NPN SMALL INTESTINE
Bacterial N MCP MCP AA
NH4+
Salivary N loss RUMEN

Liver

ATP
Blood Urea
Ruminant Digestion and
Absorption
Post-ruminal digestion and absorption
closely resembles the processes of
monogastric animals
However, amino acid profile entering small
intestine different from dietary profile
 Overview of Protein Feeding
Issues in Ruminants
Rumen degradable protein (RDP)
Low protein quality in feed very good quality
microbial proteins
Great protein quality in feed very good quality
microbial proteins
Feed the cheapest RDP source that is practical
regardless of quality
Rumen undegradable protein (RUP)
Not modified in rumen, so should be higher
quality protein as fed to animal
May cost more initially, but may be worth cost if
performance boosted enough
Salivary Urea Recycled urea
NH3 UREA

LIVER
NPN

Dietary
Nitrogen
PEPTIDES NH3 AMINO
LEVEL TO
PROVIDE FOR
ACIDS
AMINO POOL MAXIMUM
ACIDS MICROBIAL GROWTH
AMINO
PROTEIN ACIDS
MICROBIAL
PROTEIN
SMALL
INTESTINE

35% OF PROTEIN
RUP

Reticulo-rumen
Functional Feeds
Functional feeds may be defined as any
feed or feed ingredient that produces a
biological effect or health benefit that is
above and beyond the nutritive value
of that feedstuff
Many feeds and their components fit
this definition
Functional Proteins
Functional proteins are feed-derived
proteins that, in addition to their
nutritional value, produce a biological
effect in the body
Feedstuffs with Biologically Active
Proteins
Milk
Colostrum
Whey Protein Concentrates/Isolates
Plasma or serum
Other animal-derived feedstuffs
Fish meal
Meat and bone meal
Fermented animal-based products
Yeast
Lactobacillus organisms
Soy products
Protein Size Affects Function
Many protein hormones are functional even
when fed to animals
thyrotropin-releasing hormone (TRH, a 3-amino acid
peptide)
luteinizing hormone-releasing hormone (LHRH, a 10-amino
acid peptide)
insulin (a 51-amino acid polypeptide)
The smaller the peptide, the more functional it is
when fed
100% activity for TRH, 50% for LHRH, and 30% for insulin
Feedstuffs containing protein hormones (colostrum)
have biological activity when fed to animals
Production of Bioactive Peptides
From Biologically-Inactive Proteins
Peptides produced from intact inactive
proteins by incomplete digestion via
proteases in stomach and duodenum or via
microbial proteases in rumen
Many of these biologically active peptides
(typically 2-4 amino acid residues) are stable
from further digestion
Some peptides bind to specific epithelial receptors
in intestinal lumen and induce physiological
reactions
Some peptides are absorbed intact by a specific
peptide transporter system into the circulatory
system and transported to target organs
 Responses to Feeding Functional
Proteins or Peptides
Antimicrobial including control of gut microflora
Antiviral
Binding of enterotoxins
Anti-carcinogenic
Immunomodulation
Anti-oxidant effects
Opioid effects
Enhance tissue development or function
Anti-inflammatory
Appetite regulation
Anti-hypertensive
Anti-thrombic
Functional Activity of Major Milk Proteins
Caseins (, and )
Transport of minerals and trace elements (Ca, PO4, Fe, Zn, Cu), precursor of
bioactive peptides, immunomodulation (hydrolysates/peptides)
-Lactoglobulin
Retinol carrier, binding fatty acids, potential antioxidant, precursor for
bioactive peptides
-Lactalbumin
Lactose synthesis in mammary gland, Ca carrier, immunomodulation,
anticarcinogenic, precursor for bioactive peptides
Immunoglobulins
Specific immune protection (antibodies and complement system), G, M, A
potential precursor for bioactive peptides
Glycomacropeptide
Antiviral, antithrombotic, bifidogenic, gastric regulation
Lactoferrin
Antimicrobial, antioxidative, anticarcinogenic, anti-inflammatory,
immunomodulation, iron transport, cell growth regulation, precursor for
bioactive peptides
Lactoperoxidase
Antimicrobial, synergistic effect with Igs and LF
Lysozyme
Antimicrobial, synergistic effect with Igs and LF
Serum albumin
Precursor for bioactive peptides
Proteose peptones
Potential mineral carrier
 Functional Activity of Minor Milk
Proteins
Growth factors (IgF, TGF, EGF)
stimulation of cell proliferation and differentation
Cytokines
regulation of immune system (interferons,
interleukins, TGF, TNF)
Inflammation
Increases immune response
Milk basic protein (MBP)
Promotion of bone formation and suppression of bone
resorption
Osteopontin
Modulation of trophoblastic cell migration
Protein Fragments That Have
Biological Activity
 Functional Protein Effects During
Toxin or Disease Challenge
During intestinal inflammation, some functional proteins:
Reduce
local inflammatory response
excessive activation of inflammatory cells
permeability
Increase
Nutrient absorption
Barrier function
Intestinal health
During intestinal inflammation, some functional proteins:
Are absorbed and create adverse allergenic and immune
responses in the body

Modified from Campbell, 2007