· ACUTE-PHASE PROTEINS: Proteins released by the liver when the body is under stress.
ü
alpha1-Antitrypsin:
Protease inhibitor. When there is tissue damage, the dead tissue releases
proteases, so the anti-proteases help to prevent further damage.
ü
alpha2-Macroglobulin:
Indirect anti-protease that fixes proteases and allows macrophages to engulf
them.
ü
C-Reactive Protein
(CRP): Opsonin, help to fix antibodies to antigen to facilitate phagocytosis.
ü
Ceruloplasmin:
Copper-carrying protein, and anti-oxidant.
ü
Complement Proteins:
Inflammatory mediators.
ü
Ferritin: Iron
protein-carrier.
ü
Fibrinogen: Clotting
factor.
ü
Haptoglobin: Binds to
hemoglobin in blood.
ü
Serum Amyloid A Protein:
Apolipoprotein.
·
PROTEIN
ELECTROPHORESIS: alpha1, alpha2, beta, and gamma zones all have distinct
proteins.
alpha1
Zone: Closest to the anode (right): Albumin, Pre-Albumin: Fetal
albumin is called pre-albumin. It consists of two proteins. (AFP & Transthyretin)
alpha2
Zone: alpha2-Macroglobulin, Haptoglobin, Ceruloplasmin, GC Globulin
beta
Zone: LDL Lipoprotein, Transferrin, C3 Complement Factor, beta2-Microglobulin,
Hemopexin
gamma
Zone: Closest to cathode (left) : Fibrinogen, Lysozyme, Ig, CRP
·
LDH-Flip:
LDH-5 is normally highest, but in cases of MI LDH-1 may be higher. This is
called an LDH-flip and is suggestive of MI.
·
·
Proteins are the most important intracellular buffer.
Bicarbonate is the most important extracellular buffer.
·
In order to absorb molecules they need to remain
neutral = bioavailable. Follow these rules to keep molecules neutral.
- To absorb more acid need to place in a stronger acid
- Acid + Strong Acid = Behaves as a BASE
- To absorb more base place in a stronger base
- Base + Strong Base = Behaves as a ACID
- Understand that the body makes 20x more HCO3- than acid
- Because we ingest primarily acidic substances
·
If ingest acid à need to keep it charged so it will not be absorbed à give base (NaHCO3)
o Recall Activated Charcoal in the ER
If ingest base à keep charged by giving acid (coke,
juice) à will absorb less base.
·
Water molecules have a dipole nature and dissolve salts because of attractions between the water dipoles and
the ions that exceed the force of attraction between the oppositely charged
ions of the salt. In addition, the latter force is weakened by the high
dielectric constant of water. Nonionic but polar compounds are dissolved in
water because of hydrogen bonding between water molecules and groups such as
alcohols, aldehydes, and ketones.
·
Cathode – is where cations GO
Anode – is where anions GO
·
Ninhydrin
Reaction: Separate out proline
Proline will stain yellow
All others will stain purple.
·
Edmund’s
Degradation: Degradation that needs Propylisothiocyanate (PITC)
Will react with one amino acid at a
time
From the L amino terminal
Used in spectrophotometry
Good for only 100 amino acids accuracy.
·
All Restriction Peptidases CUT TO THE RIGHT.
EXCEPTION: Carboxy peptidase - cuts to the LEFT of any
amino acid on carboxy terminal.
·
ALA Synthase & Ferrochelatese Both are inhibited by
LEAD POISONING
·
In Methemaglobanemia
Low O2 saturation BUT pO2 will be normal
Treatment:
ü
Methylene
Blue – “Give them something blue to turn them pink”
ü
Anyl Nitrite- will convert Hg to Fe3+
not allowing CN to act.
ü
Sodium Thiosulfate will bind CN and recant
thiocyanate
ü
Blood transfusion
·
Collagen in the ONLY protein to get modified
in ER. All other proteins get modified in the Golgi.
·
DESMOSINE in Elastin gives it ELASTIC Property. Desmosine is a major cross link in elastin
and is unique to it. It is formed by three lysine derived aldehydes and one
lysine residue.
·
Disulfide
Bond can be disrupted by Water, Alcohol.
·
Coomb’s Test
o This
test tells if an anti-body is killing the RBC → indication of Autoimmune
attack against RBC
§ Direct
Test → Antibodies are ON the RBC surface causing the hemolysis
§ Indirect
Test → There are antibodies in the serum causing the hemolysis
·
Non-collagen collagen : substances that are not collagen but work similarly.
e.g. C1 q complement component , SP A , SP D the pulmonary surfactanty
proteins.
·
Mucin in GIT and genitourinary tract is a
glycoprotein.
·
Saturated fatty
acids have straighter tails , but the unsaturated fatty acids have kinked
tails. This needs more space and thus creates in the membrane an ability to be
a fluid structure.
·
Centrifugation of a cellular homogenate at a force
of 100,000 × g will pellet all cellular organelles and membranes.
Only soluble cellular molecules found in the
cytosol will remain in the supernatant. Thus, the enzymes of
glycolysis and most of those of gluconeogenesis, fatty acid synthesis, and the
pentose phosphate pathway will be in the supernatant. Glucose-6-phosphate
dehydrogenase, which results in the formation of 6-phosphogluconolactone from
glucose-6-phosphate, is the committed step in the pentose phosphate pathway.
In the pellet will be the enzymes within
mitochondria, including those of the citric acid cycle (aconitase),
fatty acid beta oxidation (acyl CoA hydratase), and ketogenesis (hydroxybutyrate
dehydrogenase). Enzymes of glycogen degradation and synthesis (glycogen
synthetase) will also be in the pellet associated with glycogen particles.
·
The primary control hormones of metabolism are
insulin and glucagon. Epinephrine has effects similar to those of glucagon,
except that glucagon has a greater effect on the liver while epinephrine has a
greater effect on muscle.
·
A coenzyme
usually binds loosely and can be separated from the enzyme. When a coenzyme
binds tightly to an enzyme, it is spoken of as a prosthetic
group of the enzyme. Coenzymes can be viewed as a second substrate
for the enzyme, often undergoing chemical changes that counterbalance those of
the substrate.
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