Forms of hemoglobin: types, characteristics, compounds and functions

Table of contents:

Forms of hemoglobin: types, characteristics, compounds and functions
Forms of hemoglobin: types, characteristics, compounds and functions

Video: Forms of hemoglobin: types, characteristics, compounds and functions

Video: Forms of hemoglobin: types, characteristics, compounds and functions
Video: Coagulation Cascade and Fibrinolysis - clotting factors, regulation and control mechanism 2024, July
Anonim

Hemoglobin is an essential protein for human life, it performs a number of functions, the main of which is the transport of oxygen to cells and tissues. There are several forms of hemoglobin, each with its own characteristics.

structure of hemoglobin
structure of hemoglobin

Types by protein content

Depending on the protein content of the form of human hemoglobin, there are two types. These are physiological and abnormal.

Forms of physiological type of hemoglobin occur at certain stages of human life. But pathological ones are formed in the case of an incorrect sequence of placement of a number of amino acids in globin.

blood corpuscles
blood corpuscles

Main types of hemoglobin by form

In the human body may be present:

  1. Oxyhemoglobin. This substance interacts with oxygen molecules. It is present in the blood of the arteries, which is why it has a rich scarlet color.
  2. Carboxyhemoglobin. This type of protein interacts with carbon dioxide molecules. Featured Moleculespenetrate into the tissues of the lungs, where carbon dioxide is removed and oxygen is saturated with hemoglobin. This type of protein is present in venous blood, due to which it has a darker color and greater density.
  3. Methemoglobin. This is a substance that interacts with a variety of chemical agents. The pathological form of hemoglobin, and an increase in the amount of this substance may indicate poisoning of the body, there is a violation of oxygen saturation of tissues.
  4. Myoglobin. Acts as a full-fledged analogue of red blood cells. The main difference is only that the location of this protein is the heart muscle. When muscles are damaged, myoglobin enters the bloodstream, after which it is excreted from the body due to the functioning of the kidneys. But there is a possibility of blockage of the tubule of the kidneys, which can provoke the death of its tissues. In such situations, the occurrence of kidney failure and oxygen deficiency in the tissues is not excluded.
hemoglobin blood particles
hemoglobin blood particles

Other types of hemoglobin

In various information sources, the following forms of hemoglobin are also distinguished:

  1. Glycated hemoglobin. This form is an inseparable compound of glucose and protein. This type of glucose can move through the blood for a long time, so it is used to detect sugar levels.
  2. Fetal. A form of hemoglobin is present in the blood of an embryo or newborn baby in the first few days of life. Listed as an active species in terms of oxygen transfer, under the influence of the environment is subject to rapid destruction.
  3. Sulfhemoglobin. The presented type of protein occurs in the blood when a large number of medications are consumed. As a rule, the content of this protein does not exceed 10%.
  4. Dyshemoglobin. It is formed with such bonds that completely deprive the protein of the ability to carry out its functions. This indicates that this type of hemoglobin will be transported through the blood in the form of an additional substance. After time, it will be processed by the spleen. In normal he alth, this substance is found in the body of every person, but if cases of this kind of ligaments become more frequent, then the organs involved in transporting blood throughout the body will have to function with increased intensity, as a result of which they will be exhausted and worn out more quickly.
hemoglobin model
hemoglobin model

Pathological forms of hemoglobin

Separate group stands out:

  • D-Punjab;
  • S;
  • C;
  • H.

The form of hemoglobin D-Punjab got its name due to its wide distribution in Punjab, India and Pakistan. The origin of the protein was due to the spread of malaria in various parts of Asia. According to statistics, this protein is found in 55% of cases of the total number of pathological forms of hemoglobin.

Hemoglobin S was formed in West Africa by five separate mutations.

Protein Cis one of the most common structural varieties of hemoglobin. People who have this protein may suffer from a condition called hemolytic anemia.

Hemoglobin H provokes the development of such a serious disease as alpha thalassemia.

Main Functions

Regardless of the forms and derivatives of hemoglobin, this substance has the following functions:

  1. Transportation of oxygen. When a person inhales air masses, oxygen molecules penetrate into the tissues of the lungs, and from there they move to other tissues and cells. Hemoglobin connects oxygen molecules and transports them. If this function is impaired, oxygen deficiency occurs, which is very dangerous for the functioning of the brain.
  2. Transportation of carbon dioxide. In this situation, hemoglobin already binds carbon dioxide molecules, and then transports them.
  3. Maintaining the level of acidity. With the accumulation of carbon dioxide in the blood, its acidification is observed. This should absolutely not be allowed, since the constant removal of carbon dioxide molecules must occur.
hemoglobin measurement
hemoglobin measurement

Normal performance

In order for doctors to determine the normal forms of hemoglobin in the human body, tests are carried out.

Note that the rate of free hemoglobin in the blood of people of different ages can have the following indicators:

  • men aged 18+ – 120 to 150 g/l;
  • women over the age of 18– from 110 to 130 g/l;
  • newborns and children under the age of 18 - 200 g/l.

Increase or decrease in the amount of free hemoglobin in the blood can provoke the transition of the protein to another form - pathological.

There are a number of methods for stabilizing its amount, so if the test results indicate an exceeded or reduced rate, you should immediately consult a doctor. Due to the presence of a large number of different forms of hemoglobin, only a professional doctor in the laboratory can determine what is present in the body. Its detection becomes possible with a biochemical blood test.

Recommended: