normal range for hemoglobin is different b/w men and women. for men it is _ and for women it is_
men 13-18g/dl (grams per deciliter)
women is 12-16
to remember just remember that girls go thru puberty first so the number is lower, they start around 12 and end sooner too. men start later and go longer.
Hb is a quaternary protein with 4 __ polypeptide chains
tertiary (2 alpha and 2 beta)
each of the four chains in Hb has an iron containing _ group
heme
oxygen can bind to the _ in hemoglobin
heme group’s iron will bind oxygen
carbon dioxide can bind to _ in hemoglobin
the amino acids in the chains
how many iron atoms in each Hb
4
each iron can bind how many oxygen molecules? how many oxygen atoms?
Hb has 4 iron’s (one per heme per chain), and each iron can bind one MOLECULE of oxygen = O2, which means it can bind 2 oxygens per iron = 8 total atoms of oxygen or 4 molecules of oxygen
what is the normal value of Hb in women? men? newborn?
in g/dl
12-16 grams per deciliter = women
13-18 g/dl = men
14-20 g/dl in newborn
how do you convert dl to mL?
1 dl = 100 mL
1 dl = (10)-1
1mL = (10)-3
difference is (10)2 = 100
blood hemoglobin depends on the
number of rbc and amount of hb in each rbc
a low Hb value is found in
anemia, hyperPT and cirrhosis of liver
a high Hb value is found in
polycythemia, COPD, and congestive heart failure
the Bohr effect is very strong in the
fetus
blood leaving the lungs is __% saturated with oxygen
98%
hemoglobin of normal venous blood returning to the lungs is _ saturated
75%
carbaminohemoglobin is Hb that is carrying
CO2 from tissues to the lungs
most CO2 is transported to lungs by Hb or bicarb?
bicarbonate > 30% by carbaminohemoglobin > CO2
colloid osmotic pressure is
oncotic pressure (exerted by proteins in the BV)
___ (or tissue fluid) is a solution that bathes and surrounds the cells. It is the main component of the extracellular fluid, which also includes plasma and transcellular fluid.
Interstitial fluid
plasma -fibrinogen =
serum
plasma makes up _% of blood
55%
to remember think 55inch plasma tv
hematocrit makes up _% of blood
45% = formed elements/hematocrit (RBC, WBC, platelets/thrombocytes)
to remember: H looks like 4 in 45%
blood makes us _% of our body weight
8%
to remember: B in blood looks like an 8
Blood = plasma + formed elements
Plasma is the fluid portion and contains no
cells
serum is clear, thin, sticky part of blood that remains after you take out the fibrin from plasma. it also contains no
cells
proteins make up _% of plasma
7%
water make up _% of plasma
91%
other solutes make up _% of plasma
2% (hormones, metabolic products, gases, hormones, ions
iron is absorbed mainly in the
duodenum
iron is absorbed as Fe2+/Fe3+
Fe2+ duodenum
our bodies contain 4-5g of iron which is almost exclusively in _ form
protein bound
75% of iron is found in
heme = in myoglobin and hemoglobin
15-25% of iron is stored in the
liver, spleen bone marrow in iron protein complexes intracellularly
iron is stored in the form of
ferritin and hemosiderin
_ is a complex of ferritin, denatured ferritin, and other proteins
hemosiderin
after iron is absorbed into the duodenum, it combines with a beta globulin, ____ to form _
apotransferrin ==> forms transferrin
hemochromatosis
iron storage disease that results in the deposition of iron pigments in peripheral tissues with bronzing of skin, diabetes, and weakness
Hemoglobin has 2 conformational states
T (tense) and R relaxed
which state of hemoglobin has a weak affinity for oxygen
T = in capillaries R= relaxed = higher affinity for oxygen in the pulmonary capillaries
the P50 = partial pressure of oxygen that results in 50% of Hb being saturated in normal adults
27mmHg
P50 indicates the partial pressure of a gas required to achieve 50% enzyme saturation = 2 of the 4 heme groups have O2 bound
the adult hemoglobin = globin (protein portion) is made of 4 polypeptide chains = ?
2 alpha and 2 beta
the fetal hemoglobin = globin (protein portion) is made of 4 polypeptide chains = ?
2 alpha and 2 gamma chains!
to remember = baby says gaga = 2 alpha 2 gamma
how many heme molecules in Hb? are these proteins?
4 heme (just like there are 4 protein/globin chains) but heme is the NON PROTEIN part
each heme is a nitrogen containing organic pigment that has a single iron in what state?
reduced state (Fe2+) = FERROUS iron
what is ferric iron?
3+
ferrous iron?
2+ (think two people can ride the ferrous wheel) = Hb
the PROTEIN PORTION of Hb will bind
carbon dioxide
the protein/non protein portion of Hb binds oxygen
non protein portion (Heme)
does carbon dioxide compete with oxygen for binding sites in Hb
No! they bind different areas. BUT CARBON MONOXIDE competes with Oxygen for spots
carbon monoxide has a much__affinity for Hb than oxygen
higher 240x
Methemoglobin contains iron in the _ state and cannot function as an oxygen carrier
ferric (3+)
which is less acidic deoxygenated/oxygenated hemoglobin
deoxygenated = ideal for buffering the H+ coming from tissue
Hb is a major _
H+ buffer
the most common form of Hb in adult is
HgA
Hemoglobin H is abnormal hemoglobin that is composed of __ chains
4 beta chains
Hemoglobin H is usually associated w a defect in three of the 4 alpha chain genes resulting in
alpha thalassemia
__ is a blood disorder passed down through families (inherited) in which the body makes an abnormal form of hemoglobin, the protein in red blood cells that carries oxygen. The disorder results in excessive destruction of red blood cells, which leads to anemia
Thalassemia
Hemoglobin is made of two proteins: Alpha globin and beta globin. Thalassemia occurs when there is a defect in a gene that helps control production of one of these proteins.
There are two main types of thalassemia:
- Alpha thalassemia occurs when a gene or genes related to the ___ globin protein are missing or changed (mutated).
- Beta thalassemia occurs when similar gene defects affect production of the __globin protein
- alpha
2. beta
Hemoglobin _ is an abnormal hemoglobin in which valine has replaced glutamic acid in the _ chain
S, beta chain
to remember think sickle sex, chromosome Six, occurs in Blacks, Beta chain
Hemoglobin S is the predominant form of Hgb in pp with
sickle cell anemia
a major effect of sickle cell anemia is the decreased __ of the deoxy from of Hgb
solubility
Hemoglobin __ is a group of abnormal hemoglobins in which a single amino acid substitution favors the formation of methemoglobin and is thus associated with methemoglobinemia.
M
Hemoglobin _ is abnormal hemoglobin in which LYSINE has replaced GLUTAMIC ACID, causing reduced plasticity of RBCs
C
substitution of a glutamic acid residue with a lysine residue at the 6th position of the β-globin chain has occurred
- when lysine replaces glutamic acid = Hb _
- when valine replaces glutamic acid = Hb _
- when there are 4 beta chains instead of the normal 2 alpha and 2 beta?
- when methemoglobin formation is favored =
- HgC
- HgS
- HgH
- HgM
90% of all erythropoietin is formed in the _ and the rest formed in the _
90% kidneys
10% liver
anoxia
low oxygen: The term anoxia means a total depletion in the level of oxygen, an extreme form of hypoxia or “low oxygen
RBC’s are _ shaped
biconcave
do RBC have nuclei or mitochondria
no mature RBCs do not
carbonic anhydrase is found in RBC it converts
CO2 and water ==> bicarb and H+
principal function of Rbc
carry Hg
portion of RBC in blood is called
hematocrit
do men or women have more hematocrit
men 46%
women 41%
life span of erythrocytes
105-120 days
In the early embryo, where are RBCs produced
yolk sac
in mid gestation where are RBC produced
mostly liver, but also spleen and lymph nodes
in the final month of gestation until 20years old where are RBC produced
ONLY in the bone marrow
after 20 years old where are RBC produced
marrow of membranous bones ie. vertebrae, sternum, ribs, ilia
- _ effect states hemoglobin’s oxygen binding affinity is inversely related both to acidity and to the concentration of carbon dioxide
- _ effect states that Deoxygenation of the blood increases its ability to carry carbon dioxide; this property is the Haldane effect. Conversely, oxygenated blood has a reduced capacity for carbon dioxide
- Bohr
2. Haldane effect
does myoglobin also show the Bohr effect?
The Bohr effect is dependent on allosteric interactions between the hemes of the hemoglobin tetramer. This is evidenced by the fact that myoglobin, a monomer with no allostery, does not exhibit the Bohr effect. Hemoglobin mutants with weaker allostery may exhibit a reduced Bohr effect
- The iron in hemoglobin is in the reduced or oxidized state?
- is it in ferrous or ferric state?
- hemoglobin molecules have 4 polypeptide chains that contain _ groups.
- the sulfhydryl groups (-SH) must be kept in reduced/oxidized form
- reduced
- ferrous (Fe2+)
- sulfhydryl (SH)
- reduced
transport of oxygen n the blood can occur in what 2 ways
either dissolved in plasma (outside of the RBCs) = 1.5%
or bound to hemoglobin (Hb) inside the RBC = 98.5%
RBCs transport both
oxygen and carbon dioxide
Hemoglobin in RBCs transport _% of the total amount of CO2 produced by the body as carbaminohemoglobin aka carboxyhemoglobin
30%
according to the hemoglobin-oxygen dissociation curve, at PO2 of 100mmHg (ex. arterial blood oxygen partial pressure) hemoglobin is _ saturated =
98% = means O2 is bound to all 4 groups on all hemoglobin molecules.
according to the hemoglobin-oxygen dissociation curve, at PO2 of 40mmHg (ex. mixed venous blood oxygen partial pressure) hemoglobin is _ saturated =
75% saturated = means that on average, 3 of the 4 heme groups on hemoglobin are bound
- at PO2 100mmHg (arterial)= _% saturation of Hb
- at PO2 40mmHg (venous) = _% saturation of Hb
- at PO2 25mmHg = _% saturation of Hb
- 98%—>all 4 heme occupied w/O2
- 75% 3 of 4 occupied
- 50% 2 of 4 occupied = aka the P50 point
__ is an iron-storage complex. It is always found within cells (as opposed to circulating in blood) and appears to be a complex of ferritin, denatured ferritin and other material
Hemosiderin
hemosiderin pathological relationship?
Hemosiderin is most commonly found in macrophages and is especially abundant in situations following hemorrhage, suggesting that its formation may be related to phagocytosis of red blood cells and hemoglobin.Hemosiderin often forms after bleeding (hemorrhage). When blood leaves a ruptured blood vessel, the red blood cell dies, and the hemoglobin of the cell is released into the extracellular space. Phagocytic cells (of the reticulo-endothelial system)called macrophages engulf (phagocytose) the hemoglobin to degrade it, producing hemosiderin and biliverdin. Excessive systemic accumulations of hemosiderin may occur in macrophages in the liver, lungs, spleen, kidneys, lymph nodes, and bone marrow. These accumulations may be caused by excessive red blood cell destruction (haemolysis),
why is hemoglobin a great buffer? what component in its structure
Histidine residues in hemoglobin can accept protons and act as buffers. Deoxygenated hemoglobin is a better proton acceptor than the oxygenated form
alpha thalassemia is associated with Hemoglobin H and what disease?
The worldwide distribution of inherited alpha-thalassemia corresponds to areas of malaria exposure, suggesting a protective role for alpha-thalassemia against the more severe manifestations of malaria. to remember: look at alpha (alpha chains not made) and tHalassemia = think H hemoglobin
Alpha-thalassemia is due to impaired production of 1,2,3, or 4 alpha globin chains, leading to a relative excess of __globin chains
beta
Hemoglobinopathy
a kind of genetic defect that results in abnormal structure of one of the globin chains of the hemoglobin molecule
ex. sickle cell