2. 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.
4. 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.
6. 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.
7. 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.
8. 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.
10. The Chemist’s 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.
11. M. Zaharna Clini.
Chem. 2009
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)
12. 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)
13. 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 β chain
of HbA, HbS is formed, which
results in sickle-cell anemia.
14. M. Zaharna Clini.
Chem. 2009
Secondary structure
Initial helical folding
Beta pleated sheet
Held together by
Hydrogen bonding
15. 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
16. M. Zaharna Clini. Chem. 2009
Quaternary structure
2 or more polypeptide chains
binding together
eg. Hemoglobin
Hemoglobin has 4 subunits
Two α chains
Two β chains
Many enzymes have
quaternary structures
17. 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)
18. 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
19. M. Zaharna Clini.
Chem. 2009
Conjugated Proteins
Classification Prosthetic
group
Example
Lipoprotein Lipid HDL
Glycoprotein Carbohydrates Immunoglo-
bulins
Phosphoprotein Phosphate Casein of
milk
20. 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
21. 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
22. Monogastric Protein Digestion
Whole proteins are not absorbed
Too large to pass through cell membranes
intact
Digestive enzymes
Hydrolyze peptide bonds
Secreted as inactive pre-enzymes
Prevents self-digestion
H3N+
C
H
C
R
O
N
H
C
H
C
O
R
N
H
C
H
C
R
O
O–
23. 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
Cleaves at phenylalanine, tyrosine, tryptophan
Protein leaves stomach as mix of insoluble protein, soluble
protein, peptides and amino acids
Aromatic amino acids
Pepsinogen
HCl
Pepsin
25. Monogastric Digestion –
Small Intestine
Zymogens must be converted to active form
Trypsinogen Trypsin
Endopeptidase
Cleaves on carbonyl side of Lys & Arg
Chymotrypsinogen Chymotrypsin
Endopeptidase
Cleaves carboxy terminal Phe, Tyr and Trp
Procarboxypeptidase Carboxypeptidase
Exopeptidase
Removes carboxy terminal residues
Enteropeptidase/Trypsin
Trypsin
Trypsin
26. 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
27. 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
29. Free Amino Acid Absorption
Free amino acids
Carrier systems
Neutral AA
Basic AA
Acidic AA
Imino acids
Entrance of some AA
is via active transport
Requires energy
Na+
Na+
30. 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
31. 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)
32. 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
33. Groff & Gropper, 2000
Overview of Protein Digestion and
Absorption in Monogastrics
34. OVERVIEW OF AMINO ACID METABOLISM
ENVIRONMENT ORGANISM
Ingested
protein
Bio-
synthesis
Protein
AMINO
ACIDS
Nitrogen
Carbon
skeletons
Urea
Degradatio
n
(required)
1
2 3
a
b
Purines
Pyrimidines
Porphyrins
c c
Used for
energy pyruvate
α-ketoglutarate
succinyl-CoA
fumarate
oxaloacetate
acetoacetate
acetyl CoA
(glucogenic)(ketogenic)
35. Amino Acid Catabolism
Deamination of Amino Acids
removal of the a-amino acids
Oxidative Deamination
Non-oxidative Deamination
Transamination
40. Pyruvate is an amphibolic intermediate
in synthesis of alanine
41. 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 α-amino nitrogen of AA
43. Serine biosynthesis(oxidation of the α-hydroxyl
group of the glycolytic intermidiate 3-phosphoglycerate by 3-
phosphoglycerate dehygrogenase convert it to 3-
phosphohydroxypuruvate. Transamination and subsequent
dephosphorylation is strongly favored)
50. Amino acids that are synthesized de novo in humans.
All are related by a small number of steps to glycolysis
or TCA cycle intermediates.
51. 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
52. 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
54. FATE OF THE CARBON
SKELETONS
Carbon skeletons are used for
energy.
Glucogenic: TCA cycle
intermediates(gluconeogensis)
Ketogenic: acetyl CoA, acetoacetyl
CoA, or acetoacetate
57. Rate of protein synthesis
Ks (%/d)
Tissue Pig Steer
Liver
Gut
Muscle
23
45
5
21
39
2
Ks = fraction of tissue protein synthesized per
day
58. 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
59. Protein degradation
Also controlled by hormones and
energy status
Method to assist in metabolic control
turns off enzymes
60. 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
62. 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
63. Proline biosynthesis(the initial reaction of proline biosynthsis converts the
ᵞ-carboxyl group of glutamate to the mixed acid anhydride of glutamate ᵞ-phospate.
Subsequent reduction form glutamate ᵞ- semialdehyde,, which following
spontaneously cyclization is reduced to L-Proline )
64. 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
65. 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)
68. 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
69. 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
71. STEP 1: TRANSCRIPTION= making
RNA
Location: Eukaryotes-nucleus
Prokaryotes-cytoplasm
1. RNA polymerase binds to the gene’s
promoter
2. The two DNA strands unwind and
separate.
3. Complementary nucleotides are
added using the base pairing rules
EXCEPT:
A=U
72. Try this example.
Using the following DNA sequence,
what would be the complementary RNA
sequence?
ATCCGTAATTATGGC
UAGGCAUUAAUACCG
74. 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
75. Codon and Anticodon
Codon-found on mRNA Anticodon-found on tRNA
http://images.google.com/imgres?
imgurl=http://www.obgynacademy.com/basicsciences/feto
logy/genetics/images/codon_GCA.gif&imgrefurl=http://ww
w.obgynacademy.com/basicsciences/fetology/genetics/&u
sg=__4MvAO2N3sXbERXQwODVDSqtsOjM=&h=160&w=
168&sz=4&hl=en&start=5&tbnid=toyuIN8drVBr4M:&tbnh=
94&tbnw=99&prev=/images%3Fq%3Dcodon%26gbv
%3D2%26hl%3Den
http://www.microbelibrary.org/microbelibrary/files/ccImages/Articleim
ages/kaiser/tRNA_arg.jpg
76. 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
77. SUMMARY
Transcription= process of making RNA
from DNA
Translation= RNA directions are used to
make a protein from amino acids
• DNA→RNA →Protein
Transcription Translation
nucleus
Cytoplasm on
ribosome
78. 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
80. DNA Replication RNA Transcription
DNA polymerase is used. RNA polymerase is used.
DNA nucleotides are
linked.
RNA nucleotides are
linked.
A DNA molecule is
made.
An RNA molecule is
made.
Both DNA strands serve
as templates.
Only one part of one
strand of DNA ( a gene)
is used as a template.
81. Explain the steps in protein synthesis.
http://stemcells.nih.gov
/info/scireport/images/f
igurea6.jpg
82. 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
83. 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
84. 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 animal’s 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
85. 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
86. 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)
87. 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
88. 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!)
89. 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)
90. 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
91. 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)
92. Microbial Protein Synthesis
Synchronization of carbohydrate and N availability
NPN supplementation
Carbohydrates used for carbon skeleton of amino acids
VFA (CHO fermentation)
Rumen NH3
Blood NH3
Adapted from Van Soest, 1994
Time post-feeding
Concentration
Carbon backbone
(from CHO fermentation)
93. Microbial Protein Formation
Dietary
NPN
Dietary
Soluble RDP
Microbial
Proteins
Amino Acids
Carbon Skeletons Sulfur Other Co-factors
NH3
ATP
Dietary
Starch Sugar
Dietary Cellulose
Hemicellulose
rapid slow
rapid
slower Dietary
Insoluble RDP
very
slow
94. 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
95. 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
Urea Ammonia + CO2
Urease
96. Feed Protein,
NPN and CHO
Feed
Protein
Feed NPN
NH3/NH4
Bacterial N
NH4
+
loss
MCP
RDP
RUP
Feed
Protein
AA
MCP AA
NH3
Liver
Blood Urea
Salivary N
ATP
RUMEN
SMALL INTESTINE
97. 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
98. 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
99. Salivary Urea
NPN
NH3
POOL
Dietary
Nitrogen Non-utilized Ammonia
NH3
UREA
LIVER
LEVEL TO
PROVIDE FOR
MAXIMUM
MICROBIAL GROWTH
MICROBIAL
PROTEIN
65% OF PROTEIN
35% OF PROTEIN
SMALL
INTESTINE
AMINO
ACIDS
AMINO
ACIDSPROTEIN
AMINO
ACIDS
PEPTIDES
Reticulo-rumen
RUP
RDP
Recycled urea
100. 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
101. Functional Proteins
Functional proteins are feed-derived
proteins that, in addition to their
nutritional value, produce a biological
effect in the body
102. 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
103. 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
104. 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
105. 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
106. Functional Activity of Major Milk Proteins
Caseins (α, β and κ)
Transport of minerals and trace elements (Ca, PO4, Fe, Zn, Cu), precursor
of bioactive peptides, immunomodulation (hydrolysates/peptides)
β-Lactoglobulin
Retinol carrier, binding fatty acids, potential antioxidant, precursor for
bioactive peptides
α-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
107. Functional Activity of Minor Milk
Proteins
Growth factors (IgF, TGF, EGF)
stimulation of cell proliferation and differentation
Cytokines
regulation of immune system (interferons, interleukins,
TGFβ, TNFα)
Inflammation
Increases immune response
Milk basic protein (MBP)
Promotion of bone formation and suppression of bone
resorption
Osteopontin
Modulation of trophoblastic cell migration
109. 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