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CARBOHYDRATES BLOOD
INRODUCTION COMPONENTS
OXYHEMOGLOBIN
GLYCOLYSIS
ANAEROBIC
RESPIRATION CARBOXYHEMOGLOBIN
KERBS CYCLE
GLUCONEOGENESIS
AEROBIC RESPIRATION
In the presence of oxygen, pyruvate can enter the Krebs cycle where
additional energy is extracted as electrons are transferred from the
pyruvate to the receptors NAD+, GDP, and FAD, with carbon dioxide
being a “waste product” (Figure 3). The NADH and FADH2 pass
electrons on to the electron transport chain, which uses the transferred
energy to produce ATP. As the terminal step in the electron transport
chain, oxygen is the terminal electron acceptor and creates water
inside the mitochondria.
Krebs Cycle /Citric Acid Cycle
The pyruvate molecules generated during glycolysis are transported
across the mitochondrial membrane into the inner mitochondrial
matrix, where they are metabolized by enzymes in a pathway called
the Krebs cycle (Figure 4). The Krebs cycle is also commonly called the
citric acid cycle or the tricarboxylic acid (TCA) cycle. During the Krebs
cycle, high-energy molecules, including ATP, NADH, and FADH2, are
created. NADH and FADH2 then pass electrons through the electron
transport chain in the mitochondria to generate more ATP molecules.
To start the Krebs cycle, citrate synthase combines acetyl CoA and
oxaloacetate to form a six-carbon citrate molecule; CoA is
subsequently released and can combine with another pyruvate
molecule to begin the cycle again. The aconitase enzyme converts
citrate into isocitrate. In two successive steps of oxidative
decarboxylation, two molecules of CO2 and two NADH molecules are
produced when isocitrate dehydrogenase converts isocitrate into the
five-carbon α-ketoglutarate, which is then catalyzed and converted
into the four-carbon succinyl CoA by α-ketoglutarate dehydrogenase.
The enzyme succinyl CoA dehydrogenase then converts succinyl CoA
into succinate and forms the high-energy molecule GTP, which
transfers its energy to ADP to produce ATP. Succinate dehydrogenase
then converts succinate into fumarate, forming a molecule of FADH2.
Fumarase then converts fumarate into malate, which malate
dehydrogenase then converts back into oxaloacetate while reducing
NAD+ to NADH. Oxaloacetate is then ready to combine with the next
acetyl CoA to start the Krebs cycle again (see Figure 4). For each turn of
the cycle, three NADH, one ATP (through GTP), and one FADH2 are
created. Each carbon of pyruvate is converted into CO2, which is
released as a byproduct of oxidative (aerobic) respiration.
GLUCONEOGENESIS
Gluconeogenesis is the synthesis of new glucose molecules
from pyruvate, lactate, glycerol, or the amino acids alanine or
glutamine. This process takes place primarily in the liver
during periods of low glucose, that is, under conditions of
fasting, starvation, and low carbohydrate diets. So, the
question can be raised as to why the body would create
something it has just spent a fair amount of effort to break
down? Certain key organs, including the brain, can use only
glucose as an energy source; therefore, it is essential that the
body maintain a minimum blood glucose concentration. When
the blood glucose concentration falls below that certain point,
new glucose is synthesized by the liver to raise the blood
concentration to normal.
Gluconeogenesis is not simply the reverse of glycolysis. There
are some important differences (Figure 7). Pyruvate is a
common starting material for gluconeogenesis. First, the
pyruvate is converted into oxaloacetate. Oxaloacetate then
serves as a substrate for the enzyme phosphoenolpyruvate
carboxykinase (PEPCK), which transforms oxaloacetate into
phosphoenolpyruvate (PEP). From this step, gluconeogenesis
is nearly the reverse of glycolysis. PEP is converted back into
2-phosphoglycerate, which is converted into 3-
phosphoglycerate. Then, 3-phosphoglycerate is converted into
1,3 bisphosphoglycerate and then into glyceraldehyde-3-
phosphate. Two molecules of glyceraldehyde-3-phosphate
then combine to form fructose-1-6-bisphosphate, which is
converted into fructose 6-phosphate and then into glucose-6-
phosphate. Finally, a series of reactions generates glucose
itself. In gluconeogenesis (as compared to glycolysis), the
enzyme hexokinase is replaced by glucose-6-phosphatase,
and the enzyme phosphofructokinase-1 is replaced by
fructose-1,6-bisphosphatase. This helps the cell to regulate
glycolysis and gluconeogenesis independently of each other.
AGING AND METABOLIC RATE
The human body’s metabolic rate decreases nearly 2 percent
per decade after age 30. Changes in body composition,
including reduced lean muscle mass, are mostly responsible
for this decrease. The most dramatic loss of muscle mass, and
consequential decline in metabolic rate, occurs between 50
and 70 years of age. Loss of muscle mass is the equivalent of
reduced strength, which tends to inhibit seniors from
engaging in sufficient physical activity. This results in a
positive-feedback system where the reduced physical activity
leads to even more muscle loss, further reducing metabolism.
There are several things that can be done to help prevent
general declines in metabolism and to fight back against the
cyclic nature of these declines. These include eating breakfast,
eating small meals frequently, consuming plenty of lean
protein, drinking water to remain hydrated, exercising
(including strength training), and getting enough sleep. These
measures can help keep energy levels from dropping and
curb the urge for increased calorie consumption from
excessive snacking. While these strategies are not
guaranteed to maintain metabolism, they do help prevent
muscle loss and may increase energy levels. Some experts
also suggest avoiding sugar, which can lead to excess fat
storage. Spicy foods and green tea might also be beneficial.
Because stress activates cortisol release, and cortisol slows
metabolism, avoiding stress, or at least practicing relaxation
techniques, can also help.
What is Blood?
Blood is essential to life. Blood circulates through our body and
delivers essential substances like oxygen and nutrients to the body’s
cells. It also transports metabolic waste products away from those
same cells. There is no substitute for blood. It cannot be made or
manufactured. Generous blood donors are the only source of blood
for patients in need of a blood transfusion.
BLOOD COMPONENTS
PLASMA
PLATELETS
PLATELETS
Platelets are an amazing part of your blood. Platelets are the
smallest of our blood cells and literally look like small plates in their
non-active form. Platelets control bleeding. Wherever a wound
occurs, the blood vessel will send out a signal. Platelets receive that
signal and travel to the area and transform into their “active”
formation, growing long tentacles to make contact with the vessel
and form clusters to plug the wound until it heals.
PLASMA
Plasma is the liquid portion of your blood. Plasma is yellowish in
color and is made up mostly of water, but it also contains proteins,
sugars, hormones and salts. It transports water and nutrients to
your body’s tissues.
What is hemoglobin?
Hemoglobin is the protein molecule in red blood cells that carries
oxygen from the lungs to the body's tissues and returns carbon
dioxide from the tissues back to the lungs.
Each globulin chain contains an important iron-containing porphyrin
compound termed heme. Embedded within the heme compound is an
iron atom that is vital in transporting oxygen and carbon dioxide in
our blood. The iron contained in hemoglobin is also responsible for the
red color of blood.
Hemoglobin also plays an important role in maintaining the shape of
the red blood cells. In their natural shape, red blood cells are round
with narrow centers resembling a donut without a hole in the middle.
Abnormal hemoglobin structure can, therefore, disrupt the shape of
red blood cells and impede their function and flow through blood
vessels.
STRUCTURE
Hemoglobin is made up of four protein molecules (globulin chains)
that are connected together. The normal adult hemoglobin
(abbreviated Hgb or Hb) molecule contains two alpha-globulin chains
and two beta-globulin chains. In fetuses and infants, beta chains are
not common and the hemoglobin molecule is made up of two alpha
chains and two gamma chains. As the infant grows, the gamma chains
are gradually replaced by beta chains, forming the adult hemoglobin
structure.
SYNTHESIS
Hemoglobin (Hb) is synthesized in a complex series of steps. The heme
part is synthesized in a series of steps in the mitochondria and
the cytosol of immature red blood cells, while the globin protein parts
are synthesized by ribosomes in the cytosol. Production of Hb
continues in the cell throughout its early development from
the proerythroblast to the reticulocyte in the bone marrow. At this
point, the nucleus is lost in mammalian red blood cells, but not
in birds and many other species. Even after the loss of the nucleus in
mammals, residual ribosomal RNA allows further synthesis of Hb until
the reticulocyte loses its RNA soon after entering the vasculature (this
hemoglobin-synthetic RNA in fact gives the reticulocyte its reticulated
appearance and name).
Oxyhemoglobin
Oxyhemoglobin is formed during physiological respiration when
oxygen binds to the heme component of the protein hemoglobin in
red blood cells. This process occurs in the pulmonary
capillaries adjacent to the alveoli of the lungs. The oxygen then travels
through the blood stream to be dropped off at cells where it is utilized
as a terminal electron acceptor in the production of ATP by the process
of oxidative phosphorylation. It does not, however, help to counteract
a decrease in blood pH. Ventilation, or breathing, may reverse this
condition by removal of carbon dioxide, thus causing a shift up in pH.
Hemoglobin exists in two forms, a taut (tense) form (T) and a relaxed
form (R). Various factors such as low pH, high CO2 and high 2, 3-BPG at
the level of the tissues favor the taut form, which has low oxygen
affinity and releases oxygen in the tissues. Conversely, a high pH, low
CO2, or low 2, 3 BPG favors the relaxed form, which can better bind
oxygen .The partial pressure of the system also affects O2 affinity
where, at high partial pressures of oxygen (such as those present in
the alveoli), the relaxed (high affinity, R) state is favoured. Inversely,
at low partial pressures (such as those present in respiring tissues), the
(low affinity, T) tense state is favoured. Additionally, the binding of
oxygen to the iron(II) heme pulls the iron into the plane of the
porphyrin ring, causing a slight conformational shift
Deoxygenated hemoglobin
Deoxygenated hemoglobin is the form of hemoglobin without the
bound oxygen. The absorption spectra of oxyhemoglobin and
deoxyhemoglobin differ. The oxyhemoglobin has significantly lower
absorption of the 660 nm wavelength than deoxyhemoglobin, while at
940 nm its absorption is slightly higher. This difference is used for the
measurement of the amount of oxygen in a patient's blood by an
instrument called a pulse oximeter. This difference also accounts for
the presentation of cyanosis, the blue to purplish color that tissues
develop during hypoxia. Deoxygenated hemoglobin is paramagnetic;
it is weakly attracted to magnetic fields. In contrast, oxygenated
hemoglobin exhibits diamagnetism, a weak repulsion from a
magnetic field
Respiration and Hemoglobin
OXYGEN TRANSPORT PHYSIOLOGY
THE CELLS OF THE HUMAN BODY USE OXYGEN MOLECULES (TWO OXYGEN ATOMS
FORMING AN O2) AS A VITAL COMPONENT OF THEIR BASIC METABOLISM. MOST
CAN SURVIVE BRIEFLY WITHOUT OXYGEN, BUT NOT FOR LONG AND NOT WELL.
JUST LIKE IN THE PEPSI, THE AMOUNT OF OXYGEN YOUR BLOOD CAN DISSOLVE IS
LIMITED BY THE PO2 OF THE GAS SURROUNDING IT . THE TROUBLE IS THAT AMOUNT
OF OXYGEN YOU BREATHE IN CAN ONLY PRODUCE A VERY LOW P AO2 — NOWHERE
NEAR ENOUGH BLOOD BORNE OXYGEN TO SUSTAIN HUMAN LIFE . (THE KINDS OF
LIFE THAT CAN SURVIVE ON DISSOLVED OXYGEN ALONE ARE THE LUMPY ONES THAT
JUST KIND OF ROLL AROUND FROM PLACE TO PLACE .) SO ANIMALS LIKE HUMANS
HAVE DEVELOPED A METHOD OF CARRYING FAR MORE OXYGEN IN THEIR BLOOD
THAN THE FLUID ITSELF CAN ABSORB. WE CALL IT HEMOGLOBIN .
EACH HEMOGLOBIN HAS FOUR BINDING SITES WHERE OXYGEN MOLECULES LIKE TO
ATTACH. EACH SITE CAN BIND ONE OXYGEN, AND ONLY ONE . FOUR OXYGEN PER
HEMOGLOBIN IS MAXIMUM OCCUPANCY .
THE PROCESS GOES LIKE THIS : WE BREATHE OXYGEN INTO OUR LUNGS . IT DISPERSES
ACROSS THE THIN MEMBRANES OF THE ALVEOLI , ENTERING THE CAPILLARIES, WHERE
IT DISSOLVES INTO THE BLOODSTREAM. THIS DISSOLVED OXYGEN IS THEN BOUND BY
CIRCULATING HEMOGLOBIN, LIKE A FLEET OF BUSES. THESE DRIFT DOWNSTREAM
UNTIL THEY ARRIVE AT THE TISSUE BEDS — MUSCLE, SKIN, HEART, LIVER , BRAIN,
ANYTHING AND EVERYTHING — WHERE THE PROCESS HAPPENS IN REVERSE . THE
HEMOGLOBIN UNLOAD THEIR OXYGEN , WHICH DIFFUSES ACROSS THE CELL WALLS ,
AND IS TAKEN UP BY THE CELLULAR MACHINERY FOR CONVERSION INTO ENERGY BY
AEROBIC METABOLISM .
LATER, AFTER THE AEROBIC CYCLE HAS USED UP THE OXYGEN, THE WASTE FUEL THAT
COMES FROM THE OTHER END WILL BE CARBON DIOXIDE . THIS WILL DIFFUSE BACK
INTO THE BLOOD , WHERE SOME IS BOUND BY HEMOGLOBIN , BUT THE MAJORITY
REMAINS IN SOLUTION (EITHER UNCHANGED OR IN THE FORM OF SODIUM
BICARBONATE ); IT RETURNS TO THE LUNGS, REENTERS THE ALVEOLI , AND IS EXHALED.
THE CYCLE IS COMPLETE .
OXYGEN DELIVERY
THIS WHOLE PROCESS IS OBVIOUSLY CRITICAL. THE DELIVERY OF OXYGEN FROM THE
LUNGS TO THE TISSUE BEDS REQUIRES ADEQUATE FUNCTION OF THE LUNGS, OF THE
BLOOD ITSELF, AND OF THE SURROUNDING ENVIRONMENT THAT ALLOWS FOR OXYGEN
BINDING AND UNLOADING.
IN THE BLOOD ITSELF, OTHER PROBLEMS CAN OCCUR. FIRST, UNDERSTAND THAT THE
TOTAL AMOUNT OF OXYGEN DELIVERED TO YOUR BODY IS NOT ONLY DETERMINED BY
HOW MUCH IS BOUND TO THE HEMOGLOBIN, BUT ALSO BY HOW MANY HEMOGLOBIN
ARE AVAILABLE. A LOW BLOOD VOLUME — SUCH AS IN HYPOVOLEMIA — WILL
COMPROMISE THIS. A NORMAL BLOOD VOLUME, BUT LOW HEMOGLOBIN COUNT — AS
IN ANEMIA — WILL ALSO COMPROMISE THIS. AN ADEQUATE VOLUME AND
HEMOGLOBIN COUNT, BUT INADEQUATE CIRCULATION — LOW BLOOD PRESSURE AND
POOR CARDIAC OUTPUT — WILL RESULT IN A “TRAFFIC JAM,” WITH PLENTY OF BUSES
AND PLENTY OF PASSENGERS, BUT NOT ENOUGH MOVEMENT FROM POINT A TO POINT
B.THERE CAN ALSO BE PROBLEMS WITH EITHER THE BINDING OR UNLOADING OF
OXYGEN.
THE OXYHEMOGLOBIN DISSOCIATION CURVE
ADEQUATE OXYGEN DELIVERY DEPENDS ON THE HEMOGLOBIN BINDING,
TRANSPORTING , AND ULTIMATELY UNLOADING O2 MOLECULES . AS WE SAW,
ALTHOUGH OXYGEN DOES DISSOLVE INTO THE PLASMA ITSELF , IT IS NOT NEARLY
EACH HEMOGLOBIN CAN BIND ZERO OXYGENS , ONE, TWO, THREE, OR FOUR. HOW
MANY IT BINDS IS DIRECTLY RELATED TO HOW MUCH OXYGEN IS DISSOLVED IN THE
BLOOD; THE MORE OXYGEN IN SOLUTION (PAO2), THE MORE WILL BIND ONTO
HEMOGLOBIN (SAO2). IF 50% OF OUR TOTAL BINDING SITES WERE OCCUPIED BY
OXYGEN (FOR INSTANCE , IF ALL OF OUR HEMOGLOBIN HAD TWO BOUND OXYGEN
EACH), WE WOULD SAY OUR ARTERIAL BLOOD IS 50% “SATURATED ” — AN SAO2 OF
50%.
IF WE GRAPH THE PAO2 ON ONE AXIS , AGAINST THE SAO2 ON THE OTHER , WE GET
A LINE CALLED THE OXYHEMOGLOBIN DISSOCIATION CURVE . THIS DESCRIBES WHAT
PRESSURE OF OXYGEN WE NEED TO ACHIEVE IN THE BLOOD IN ORDER TO REACH A
GIVEN SATURATION OF HEMOGLOBIN .
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