From Big Medical Encyclopedia

ALBUMINE (Latin albumen of squirrels) — the group name of the simple natural proteins making the main part of proteins of animal and vegetable fabrics. Typical representatives: Albumine of blood serum, lactalbumin of milk, myoalbumin of muscles of animals, and also leucosin of wheat, rye and barley, legumenin buckwheat and soy, ricin of castor beans etc. Despite a big variety of various representatives, Albumine have one general property to drop out in a deposit at full saturation of solution ammonium sulfate. And. have rather small pier. the weight and high electrophoretic mobility (see. Electrophoresis ). A seralbumin contains in blood in number of 4 — 5 g on 100 ml and makes more than 50% of proteins of blood serum. Pier. the weight of a seralbumin of cattle about 67000, horses — 70000, rats — 65000. Pier. weight serumal And. the person — 65000, an isoelectric point — within pH 4,6 — 4,7. Cross immunological reactions (see. Immunochemistry ) between serumal And. various animals weak that is explained by essential distinctions in amino-acid composition of these proteins.

The physiological role

the Physiological role of Albumine of blood serum is very big: And. in many respects define not only properties of the serum, but also a number of processes of exchange in an organism in general. E.g., And. along with other proteins supports colloid and osmotic (oncotic) pressure, and also rn blood; in this regard drugs A. are applied as blood-substituting liquids (see). At more or less expressed reduction of contents And. in blood ability of blood serum to hold water decreases that leads to strengthening of process of transition of water to extracellular space and developing of hypostases.

The molecule of Albumine is capable to formation of complexes with very large number of other connections, in particular with fatty acids or substances of the steroid nature; the negative charge of a molecule caused by existence on its surface of carboxyl groups facilitates a possibility of binding of ions of metals and positively charged dyes.

Albumine owing to existence in structure of their molecules of a large number of various reactive groups (e.g., ε-amino groups of a lysine, thiol and imidazolny groups) connects and neutralizes toxins as bacterial origin, and formed in the course of a metabolism. Ability And. to a complex formation helps And. to carry out transport function — linkng and transfer with blood of metabolic products, microelements, vitamins, medicinal substances, hormones (e.g., with And. 75 — 82% of corticosteroids and 98 — 99% of the estrogen defined in blood) etc. are connected.

Complexes A. easily dissociate at change of pH, ionic strength or existence in fabrics of any component forming stronger bonds with ingredients of a complex.

Albumine is the main reserve proteins of an organism; disintegration And. provides a possibility of synthesis globulins (see) and structural proteins of fabrics and bodies (half-life And. in a human body of 27,4 days). Synthesis serumal And. there is a hl. obr. in tissues of a liver, decrease in its concentration in blood it is observed at defeat of this body (cirrhosis, hron. hepatitis, hepatolienal syndrome etc.). Seldom found hereditary defect causing absence is described And. in blood — analbuminemiya (see). At other hereditary defect — a bisalbuminemiya — bifurcation of an electrophoretic zone A is found. Hereditary defects of synthesis And. in most cases do not involve pathological frustration, however are in certain cases observed Crocq's disease (see) and vascular frustration. At the morbid conditions connected with the strengthened disintegration of fabrics or considerable changes in a metabolism, e.g. at a diabetic ketosis doubling of a zone A can be observed. on an elektroforegramma — the so-called tranzitorny bisalbuminemiya connected with emergence in blood of big concentration of complexes of Ampere-second harmful substances and disappearing at improvement of a condition of the patient. Similar changes can be observed at reception of high doses of some drugs, e.g. penicillin; in this case the bisalbuminemiya disappears soon after the termination of administration of penicillin.

Because Albumine has rather small molecular sizes, it in bigger quantity, than other serum proteins of blood, is filtered through tubules and excreted with urine where it can be found after a condensation of urine one way or another; at inflammatory diseases of kidneys quantity excreted And., and then and other serum proteins sharply increases and And. it can be found in nekontsentrprovanny urine by means of usual albumin tests.

Albumine of tserebromozgovy liquid on chemical and antigenic properties it is identical And. blood, contents it are made by 40 — 60% of the general content of soluble proteins of cerebrospinal fluid, or 22 — 23 mg of %. Serumal And. in number of 1,5 — 4% contains also in milk, but, except it, in milk (and colostrum) contains α-lactalbumin, which on structure and antigenic properties is generally similar serumal And., differing from it only in the fact that its molecules at an electrophoresis move in a zone of α-globulins..........

Similar physical. - chemical properties have also albuminoids — the proteins of the main substance of connecting fabric connected with mucopolysaccharides (see).

K A. also the ovalbumins which are a part of proteins of egg and being one of the ingredients causing nutritional value of bird's eggs belong.

The blood-substituting drug produced under the name «albumine» is a product of fractionation of proteins of donor blood, contains up to 3% of impurity of other proteins of plasma, is applied in the form of 10 — 20% of solution.

Albumine as blood preparation

the Medical drug of complex action containing albumine of human blood. The solutions stabilized by salts fat to - t (caprylate or mendelaty sodium), atsetiltriptofany or glucose, and also drug a protein produce 5, 10, 20 and 25%.

Therapeutic effect of drugs is caused fiziol, functions: high oncotic activity of albumine, participation in transportation of products of metabolism and medicinal substances; albumine can be a source of nitrogen at a hyponutrient and deficit of protein in an organism.

Physical and chemical properties

Drugs of albumine — the transparent, deprived of opalescence solutions of amber color of various shades; depending on concentration of solution have various viscosity (from 1,5 to 4,5 according to concentration of protein from 5 to 20%); electrophoretic purity not less than 97% (an exception — isogenic plasma substitute and a protein).

In 5% solutions of albumine find stable to pasteurization alpha and beta globulins; it is so-called isogenic plasma substitute a protein (abroad — Stable plasma protein solution or SPPS, Plasmanate). Drugs contain 80 — 90% of albumine and 20 — 10% of thermostable globulins.

A technique of receiving

At industrial receiving drugs of albumine apply spirit, ammonium - sulfate, rivanolovy methods of fractionation of proteins of a blood plasma and a combination of these methods. The greatest distribution has a method of spirit fractionation in the conditions of negative temperatures.

Produce drugs of albumine on 50, 100, 250 and 500 ml in the glass bottles pressurized by rubber bungs.

Drugs of albumine subject to careful control on sterility, an apirogennost, non-toxicity, and also will pasteurize (for an inactivation of a virus of hepatitis). It is possible to store drugs of albumine 3 — 5 years at t ° 4 — 8 °.

Indications to use

use Drugs of albumine at shock (traumatic, operational, burn), blood loss, a collapse, disturbance of water exchange, a condition of proteinaceous insufficiency, diseases of kidneys, a liver, agastralny and anenteralny states. Albumine is highly effective as means of parenteral food at a hypoproteinemia and a hypoalbuminemia of various origin.

Contraindications to use: drugs of albumine are contraindicated at fibrinferments, the expressed hypertensia, the proceeding internal bleeding.

Methods of introduction and a dose

enter Drugs of albumine intravenously kapelno in combination with hemotransfusions. The dose depends on a condition of the patient. At acute circulator insufficiency jet and drop injections on 100 — 150 ml konts are shown. solution with transition, in process of emergence to lay down. effect, to drop injection of drug.

At severe injuries of a skull the concentrated solutions of albumine (10 — 20%) in a dose of 100 — 150 ml apply not only as antishock means, but also for reduction of wet brain and normalization of intracranial pressure.

At moderately severe traumatic shock enter 200 — 250 ml of 20% of solution; at the accompanying blood loss — more than 500 — 750 ml; a protein — on 500 — 2500 ml.

At operational shock pour 100 — 200 ml of albumine in combination with a whole blood. At burn shock in view of a massive plazmopotera (and, therefore, losses of albuminous fraction of plasma) intravenous administration of 20% of solution of albumine is shown. 5% solutions are more preferable to the emergency completion of volume of the circulating blood. At burns of upper respiratory tracts, at threat of a fluid lungs and sharply developing cardiovascular insufficiency enter 50 — 100 ml on 30 — 40 drops in 1 min. For the purpose of parenteral food at disturbance of passability of a gullet, stomach, after extensive operations on bodies went. - kish. a path enter 20% of solution of albumine to 500 ml.

At diffusion diseases of a liver with hypo - or a disproteinemia, hron, nephrite with dominance of a nephrotic component, an amyloid and lipoid nephrosis drugs of albumine pour repeatedly, on 50 — 100 ml of 20% of solution in 1 — 2 day.

Solution of albumine is harmless, at introduction of its side reactions is not observed.

See also Plasma substituting solutions , Antishock liquids .

See also Albumin-globulinovy coefficient , Proteins .

Bibliography: Petrovsky B. V. and Guseynov Ch. S. Transfusion therapy in surgery, page 84, M., 1971; Fromm A. A., etc. Proteins of plasma and their fractionation in production of blood preparations, M., 1974; P e t e of s T. Serum albumin, Advanc, clin. Chem., v. 13, p. 37, 1970, bibliogr.

E. G. Larsky. V. M. Rusanov.