specific proteins 2 Flashcards
Binds thyroxine; transports vitamin A
Prealbumin
molecular weight of prealbumin
62,000 Da,
prealbumin is also called
thyroxine-binding prealbumin (TBPA) or transthyretin (TTR)
for Oncotic pressure; amino acid reservoir;
carries small molecules
albumin
protease inhibitors
a-antitrypsin
α2-Macroglobulin
Binds hemoglobin
Haptoglobulin
for Lipid transport
β-Lipoprotein
Transports iron
Transferrin
Component of complement system
C3
Clot formation
Fibrinogen
for Surface immunity
Immunoglobulin A
Immunoglobulin D
Binds to mast cells; hypersensitivity reactions
Immunoglobulin E
Humoral immunity primary response
Immunoglobulin M
is a small protein of only 182 amino acids, and so it would be rapidly
removed from the circulation by filtration through the kidney if it were
not held in the plasma by the larger protein prealbumin
retinol-binding protein (RBP
Prealbumin is rich in
tryptophan
β-pleated sheet conformation
source of the β-fibrillar amyloid component in type
I familial amyloidotic polyneuropathy
Prealbumin
halflife of prealbumin
roughly 2 days
detected from patients who have had heparin therapy
prealbumin
has major clinical utility as a marker for
nutritional status;
considered to be a better early
indicator of change in nutritional status than other commonly used
markers,
prealbumin
is used only as a landmark to
confirm that the specimen was likely CSF.
presence of a distinct band of prealbumin
True prealbumin is generally
below the level of detection by serum electrophoresis; instead it is best
quantified by
immunologic measurements such as nephelometry
crosses more easily into the
CSF than do the other serum proteins.
prealbumin
is usually
requested for detection of oligoclonal bands of immunoglobulin
Electrophoresis of CSF
what is present in prealbumin– apolipoprotein or beta-lipoprotein?
apolipoprotein
-B-lipoprotein is not present
The single most abundant protein in normal plasma is
albumin
2/3 of total plasma
loss of albumin results to
peripheral edema
the congenital absence of albumin (analbuminemia) generally does not lead
to such problems like edema because|___
lifelong compensatory mechanisms
that control hydrostatic pressures
The primary sequence of albumin contains
three major
regions with three peptide loops each
has regions of homology with serum albumin
α-fetoprotein
most common allotype of albumin
albumin A
how many amino acids are in albumin? and how is albumin arranged
585 amino acids arranged in
nine loops held together by the disulfide bonds between cysteine residues
percentage of albumin circulating in normal persons becomes glycosylated
nonenzymatically
8%
The half-life of circulating albumin is
about 17 days
other term for glycosylated albumin
fructosamine
Diabetic patients on hemodialysis can be
monitored with
glycosylated hemoglobin or glycosylated albumin
serves as a mobile repository of amino acids for incorporation into other
proteins
albumin
The primary structure of albumin
consists of
35 cysteine residues, of which 34 form intramolecular disulfide
bonds and one remains free
can be very useful for assessing diabetic control
in patients with hemolytic anemias
Measurement of glycosylated albumin
general transport or carrier protein
albumin
Analysis of newly synthesized albumin from intracellular sites has
revealed the existence of
precursor proalbumin
measures albumin and total protein
comprehensive metabolic panel
hepatic function
panel
measures albumin only
renal function panel
sensitive but
nonspecific reduction of albumin in so many different conditions has led
to its being termed a
“negative acute phase reactant”
these ions are
bound to albumin, and so decreases in albumin are directly responsible for
depression of their concentrations, too.
calcium and magnesium
compensatory mechanism showed by patients with cirrhosis
major polyclonal increase of immunoglobulins
in the γ-fraction
compensatory mechanism showed by patients with nephrotic syndrome
shows high levels
of α2-macroglobulin