Blood L2 Flashcards

1
Q

what is the normal Blood PH?

A

7.35-7.47. More often an average value is named – 7.37

рН of venous blood is 0.02 lower than that of arterial

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2
Q

what is the acidosis ?

A

blood. Acidosis – рН is lower than 7.37

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3
Q

what is alkalosis ?

A

blood. Acidosis – рН is higher than 7.47

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4
Q

when is the acidosis and alkalosis is immediate life risk ?

A

рН equal to 6.8 and 7.8 is fatal.

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5
Q

So long continued vomiting or diarrhea, in both children and adults must be accompanied ?

A
by abundant (a lot of) drinking of lightly salted water 
It is better to drink salt solutions, for example, rehydrone through the vein
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6
Q

Organic substances. Proteins and the function ?

A

Proteins make 65-85 g/l (6-8 %). They are presented by
albumins (35-50 g/l or 3-5 %)
globulins (20-30 g/l or 2‑3 %)
fibrinogen (2-4 g/l or 0,2-0,4 %).

Blood plasma proteins functions:

1) ensure oncotic pressure;
2) regulate water homeostasis;
3) perform a nutritional function;
4) take part in transport of numerous substances;
5) ensure immune homeostasis;
6) determine blood viscosity and coagulation;
7) maintain acid-base balance (protein buffer).

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7
Q

explain the Albumins ?

A

low molecular weight proteins of small size, they make about a half of all plasma proteins Lat. albumen – protein . As they are numerous
and this protein on 80% defines plasma oncotic pressure.
Albumins are synthesized in the liver.

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8
Q

explain the Globulins ?

A

(Lat. globulus – ball) – are larger than albumins. Their several fractions are distinguished: alpha ‑, beta- and gamma-globulins
they are formed in the liver, bone marrow, spleen and lymph nodes
function : . A specific function of globulins is transport. Globulin molecules on their surface have active centers with the help of which biochemical or electrostatic bond with substances that are transported is carried out.

α-globulins transport hormones, vitamins, minerals, lipids. For example, a variant of alpha-globulin, binding glucose, is called glycoproteids. About 60% of all plasma glucose circulates in the composition of glycoproteids

β-globulins are involved in transport of phospholipids, cholesterol, steroid hormones, cations of metals. For example, transferrin serves as an agent of copper and iron for the synthesis of red blood cells.

γ-globulins are known as antibodies or immunoglobulins which have five classes: JgA, JgG, JgM, JgD, JgE. They are able to bind with foreign proteins, membrane structures of pathological microorganisms, thus shaping host protection against viruses and bacteria.

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9
Q

explain the Fibrinogen

A

a specific fraction of beta-globulins. It has extremely large dimensions. This is the main factor in blood coagulation. It is formed in the liver.

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10
Q

explain Oncotic blood pressure ?

A

part of osmotic pressure created by plasma proteins. Its value is 25-30 mm Hg
brought about mainly by albumins. Albumins possess a small size, therefore, a large surface area; they are able to attract intensively water.
Oncotic pressure plays an important role in regulating water distribution between plasma and tissues.

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11
Q

comparison with osmotic pressure and oncotic pressure

A
  • osmotic pressure created by electrolytes and playing a role in extracellular pressure
    oncotic pressure higher in the plasma then the extracellular
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12
Q

explain the Erythrocytes

A
  • Erythrocytes (red blood cells) are the most numerous formed elements of blood. The blood of males normally contains 4.0 – 5.5∙1012 /l, in females – 3.7-4.9∙1012 /l, it is non-rigid homeostatic constant.
  • Human erythrocytes are devoid of nucleus their cytoplasm is filled with hemoglobin They have predominantly the form of a bi-concave disk Erythrocytes of this form are called normocytes
  • A special form of erythrocytes results in increase in its surface that improves its basic function – respiratory function. They squeeze through narrow capillaries, changing their shape to ellipsoid one, which is important for hemodynamics and gas diffusion.
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13
Q

Erythrocytes of shape of bi-concave called ?

A

normocytes.

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14
Q

function of Erythrocytes ?

A

1) respiratory function – they transfer О2 from lungs to tissues and СО2 (carbon dioxide) from tissues to lungs, this is their main function;
2) regulatory function – it is related to the maintenance of blood pH due to hemoglobin as the most powerful body buffer;
3) nutritional function – transferring aminoacids on their surface from digestive organs to body cells;
4) protective function – adsorption of toxic substances on their surface;
5) participation in water-salt exchange;
6) erythrocytes define human blood group( rhesus-factor).

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15
Q

what is the most powerful body buffer ?

A

maintenance of blood pH due to hemoglobin

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16
Q

Erythrocytes synthesis ?

A

erythropoeisis is carried out in red bone marrow, which is found in flat bones.

17
Q

Erythrocytes together with blood-forming tissue are called ?

A

“red blood germ” or erythron

18
Q

explain the Hemoglobin ?

A

Hemoglobin (Hb) is a special protein that performs
1) respiratory function and
2) maintains blood pH
In men blood contains in average 130-170 g/l
in women – 120 -150 g/l.

19
Q

types of Hemoglobin ?

A

Physiological:

1) OxyHb - HbO2
2) CarbHb - HbCO2
3) MyoHb
1) Adult
2) Fetal

Pathological:

1) CarboxyHb - HbCO
2) MethaHb -MtHb

20
Q

explain the Physiological types of Hemoglobin and its function

A

1 - oxyhemoglobin (НbО2). = is transport of oxygen and carbon dioxide.
Hemoglobin which bound О2,
- deoxyhemoglobin or reduced hemoglobin (H+Нb). = Hemoglobin which gave away О2
3- carbhemoglobin (НbCО2). = Hemoglobin, coupled with СО2 Connection of hemoglobin with СО2 takes place in capillaries of body tissues. This connection is unstable as well. In the form of this compound 20% of CO2 is transported.
4- myoglobin = located In skeletal and cardiac muscle and its muscle hemoglobin , It plays an important role in supplying oxygen to the working muscles; it can be seen as a depot of O2 in muscles.
5-6 - In a fetus mainly (80%) fetal hemoglobin (HbF) is contained. It has a higher ability to bind oxygen, it has greater affinity to О2 and it gives it away harder. After birth HbF is almost completely replaced by adult hemoglobin (HbA). In erythrocytes of an adult HbA makes 95-98%.

21
Q

explain the compound between hemoglobin and carbon monoxide (CO)

A

is called carboxyhaemoglobin. its path logical compound of hemoglobin
Normally it does not exist, because there is no CO in atmosphere. HbCO is a stabile compound ,
–Hemoglobin is blocked in it by carbon monoxide and is not capable of transferring oxygen. The affinity of hemoglobin to carbon monoxide is higher than its affinity to oxygen and carbon dioxide, so even a small amount of carbon monoxide in the air is dangerous for life. At this not concentration of carbon monoxide but duration
Even extremely low levels of CO in the air, but with prolonged inhalation of it, such as during sleep, can be lethal.

22
Q

explain the Carbon monoxide poisoning

A

Carbon monoxide poisoning very often arise in drivers at their long stay in a closed garage with an working car engine. Another common source of CO are woody smoke and fumes

feature of Carbon monoxide poisoning
A feature of carbon monoxide is that it has no smell, so poisoning develops without being noticed. Often the victim is understand of his poisoning, when myorelaxing action (relaxation of skeletal muscles) of CO is manifested

23
Q

how to provide first aid for Carbon monoxide poisoning

A

The victim must be taken to “fresh air”. But this is not enough , you can using an oxygenous pillow If it is not available – make artificial ventilation «mouth-to-mouth». At this air will be forced into the victim’s lungs under higher pressure. The partial
pressure of О2 in such air turns out to be larger than normal,
. Due to this some CO get out from compound with hemoglobin. Later, the victim should be taken to the hospital.

24
Q

explain the compound between hemoglobin and strong oxidants ?

A

this compound will for methaemoglobin (MtHb) its pathological compund of the hemoglobin
it has a high affinity to О2 and СО2. MtHb tightly holds oxygen and loses the ability to give it to tissues, causing ( hypoxia) in vital organs and can lead to death
ex of strong oxidants ; oxidants are nitrates and nitrites they can be found in chemical fertilizers

25
Q

explain the Colour indicator

A

-The content of hemoglobin in erythrocytes is judged by the colour indicator (CI)
the formula : CI = Hb * 3 / first three figures of Er amount
CI – colour indicator;
Hb – amount of hemoglobin, g/l;
Er – amount of erythrocytes (first three figures).
For example, in norm Hb=166g/l, and Er=5∙1012 /l. Then
CI = 166 * 3 / 510 = 0.98,
In norm CI = 0.75-1.0 or more. Such erythrocytes are - normochromatic erythrocytes.
If CI is less than 0.7, these erythrocytes are - hypochromatic erythrocytes.
When CI is more than 1.1, they speak about - hyperchromatic erythrocytes.

26
Q

what is the Hemolysis ?

A

its destruction of the erythrocytes membrane and hemoglobin going out to the blood plasma
At this plasma turns red and becomes transparent “laky blood”.

27
Q

explain the Osmotic hemolysis ?

A

it can occur in a hypotonic environment
The concentration of NaCl solution, at which hemolysis starts, is called minimum osmotic resistance of erythrocytes. Normally it ranges between 0.48-0.46%. The concentration of NaCl solution in which complete hemolysis takes place is called maximum resistance of red blood cells. It is equal to 0.34-0.32%

Osmotic hemolysis is possible only in laboratory , as in a whole organism blood under no circumstances can reach such a low hypotonicity

28
Q

Definition of osmotic resistance ?

A

is a laboratory method of assessing maturity and functional integrity of erythrocytes

young erythrocytes have higher resistance because their outer membrane is more rigid. Old erythrocytes have a less strong outer membrane, so their resistance is lowered. At this gas-transporting activity in both is reduced,

29
Q

explain the Biological hemolysis ?

A

It occurs when some substances of animal and vegetable origin (bites of snakes, insects, mushroom poisoning) enter the blood stream. Another important reason of biological hemolysis is a transfusion of incompatible blood groups.

30
Q

explain the Chemical hemolysis

A

may be caused by chloroform, ether, solutions of acids and alkali, certain other substances, depleting protein-lipid membrane of red blood cells.

31
Q

Temperature (or thermal hemolysis)

A

occurs at blood freezing/unfreezing as a result of erythrocytes membrane destruction by ice crystals.

32
Q

Mechanical hemolysis

A

occurs at strong mechanical impacts on blood, for example, while shaking the ampoule with blood, at prolonged circulation of blood in extracorporeal circulation machines system.
In a healthy person minor mechanical hemolysis can occur during prolonged running on hard surfaces, during work involving prolonged strong shaking of the body (miners).

33
Q

explain the Erythrocyte sedimentation rate ESR Suspension stability of blood and its mechanism ?

A
  • Red blood cells in blood are contained in suspension This is ensured by a negative charge of blood cell membranes
  • The ability of erythrocytes to precipitate in a test tube with blood, devoid of opportunities to coagulate, is called erythrocytes sedimentation rate (ESR)
  • ESR in healthy males makes 1-10 mm/hour, in women the ESR is 2-15 mm/h.
  • Erythrocytes precipitate only in vitro. In a holistic organism (in vivo) owing to blood movement this does not happen
  • ESR is increased during pregnancy, stress, inflammatory and infectious
  • In case of decrease in erythrocytes amount ESR reduction occurs.
34
Q

what is main forces that determine the ESR

A
  • is the gravity , which tends to increase precipitation of erythrocytes and their electrostatic repulsion
  • Gravity is a constant value, thus ESR increasing is due to the reduction of negative charge in red blood cells and weakening of their repulsion from each other.