The hemoglobin molecule is composed of four polypeptide chains of the protein globin. In addition, all of these chains contain nonprotein ferruginous material - heme, which has a direct role in the binding and transport of oxygen.

Globinat is a protein such as albumin, that contain amino acid residues. Hema and globinat influence. Globinat alters the properties of heme so as to bind the oxygen. HEMA provides stability of globin against the action of acids, temperature, the action of enzymes and specific features of the crystallization thereof.

In adults, 98% of the hemoglobin type A (HbA), in the fetus and newborn is mostly type F (HbF), which in the first days after birth, changes in HbA.

Congenital disorders and diseases of the hematopoietic system appear abnormal types of hemoglobin as methemoglobin, which is unable to carry oxygen. In blood of healthy persons methaemoglobin in minor amounts. Methaemoglobin binds with hydrocyanic (senile) acid and other substances, so is used in medicine in such poisoning.

Normal hemoglobin levels in men ranged from 135-160 g / l in women - 120-140 g / l

Formation and decomposition of hemoglobin
The biosynthesis of hemoglobin was obtained in young erythrocytes, which penetrate into the iron atoms. Globinat formed from amino acids, i.e. at the usual time of synthesis of proteins.

Disintegration of hemoglobin begins in erythrocytes, which are at the end of their life cycle. In the process of decomposition to yield derivative verdoglobin having green color. It is unstable and falls apart easily. Heme disintegrates in cells of the liver, bone marrow and spleen to form yellow pigments. In this process, the iron atoms were removed, which again is connected with the erythrocytes to form new molecules heme.

Properties of hemoglobin
The main biological role of hemoglobin is its participation in the process of exchange of gaseous substances from the environment and the body. Hemoglobin provides oxygen transport in the blood from the lungs to the tissues and transport of carbon dioxide from the tissues to the lungs. The similarity of the hemoglobin molecule oxide is three times greater than with the oxygen molecules, which determines the properties of high toxic carbon monoxide. Therefore, when the concentration of carbon monoxide in the air of 0,1% more than half of hemoglobin in the blood is not bound with oxygen and carbon monoxide. In this form carboxyhemoglobin which can not transport oxygen.

Another important function of hemoglobin is that of maintaining the acid-base balance in the body.

Changes in hemoglobin
Upon failure of the hemoglobin in erythrocytes disrupting metabolism in cells. Low hemoglobin specific for iron deficiency anemia, which most commonly are caused by chronic blood loss or poor nutrition, especially when excludes the consumption of animal protein.

High hemoglobin may be normal or physiological phenomenon feature of the disease. For example, in people living in high mountains register compensatory increase in the level of hemoglobin in the blood, due to the reduced content of oxygen in the air.

Deficiency of some B vitamins leads to changes in the blood with high hemoglobin and decrease the number of red blood cells - malignant anemia. In certain cardiovascular and pulmonary disorders also can be observed high hemoglobin (the number of red blood cells but does not change), since disturbed blood flow in tissues do not receive oxygen.

Hemoglobin is one of the most important health indicators and indicators of change should seek competent medical opinion.

A new study published in the Proceedings of the National Academy of Sciences USA, PNAS, conducted by researchers at the Ruhr University in Bochum, shows how peptides can be designed so that attack bacterial cells.

Researchers believe that the disposal of pathogenic bacteria could be done without harming human cells.

Moreover, this type of therapy would reduce the risk of resistance that developed most pathogens to previously applied drugs.

Previous studies have already shown that many antimicrobial peptides interact with cell membranes of the bacteria and thus perform its microbicidal effect.

RUB team has turned his attention to the study of a peptide called MP196, which is a group of very small positively charged peptides consisting of four to ten amino acids.

From previous studies it is known that the MP196 can cope with a variety of bacteria including some that are multi - drug-resistant, but it is unclear exactly how this process is carried out.

Researchers have demonstrated that prevents MP196 proteins in the cell membrane of the bacteria and thereby distort two key cellular processes: cell wall biosynthesis and cell breathing.

Through disruption of cell wall biosynthesis, the peptide interferes with the integrity of the bacterial cell, and by interfering with the cellular respiration, distorts the production of ATP, the molecule that stores the energy used by the cell.

Scientists are confident that the MP196 offers a starting point for developing new drugs that attack specific classes of bacteria without harming human cells, but to be confirmed in their findings need to go a long way.

The study is part of the development of innovative antibiotics.

To solve new drugs, federal authorities need detailed information about the procedure and the effects of drugs on both pathogens and on human cells.