Protein digestion begins in the stomach. Pepsin

(SF) from the mucous membrane of the fourth section (abomasum) of the stomach of a calf. SF contains two main milk-clotting enzymes - chymosin and pepsin.

The relative content of these enzymes in gastric juice varies widely, depending on the age of the animal and the diet. SF of milk-drinking calves (light calves) contains 80-95% chymosin, while similar preparations isolated from abomasums of calves fed roughage (heavy calves) contain from 70 to 100% pepsin. It is important to note that natural SF preparations always contain an admixture of pepsin, which begins to be synthesized in the abomasum of a calf in the prenatal period.

Pepsin and chymosin have specific and non-specific proteolytic activity (PA). Specific PA or milk-clotting activity is the ability of pepsin and chymosin to hydrolyze the key peptide bond 105 (Phe) - 106 (Met) in the kappa-casein molecule. Hydrolysis of this bond leads to destabilization of casein micelles and starts the process of milk clot formation. During nonspecific proteolysis, hydrolysis occurs not only of the 105 (Phe) – 106 (Met) bond in the kappa-casein molecule, but also of other peptide bonds in alpha-, beta-, and kappa-caseins. The non-specific proteolytic activity of pepsin in the pH range from 2 to 6 is much higher than that of chymosin, which affects the yield and quality of cheeses. Chymosin is synthesized to ensure the coagulation of milk and therefore hydrolyzes mainly the key peptide bond. In contrast, pepsin, which is synthesized to break down proteins, attacks a large number of peptide bonds, both in casein and in proteins from solid foods. Chymosin breaks down casein with the formation of large fragments, which subsequently become substrates for proteases of lactic acid bacteria. Pepsin, which has a much higher proteolytic activity, hydrolyzes proteins to form short peptides that can cause bitterness in cheese.

Today, cheese-making enterprises are offered a wide range of milk-clotting enzymes, both domestic and foreign. The main ones are domestic drugs developed VNII butter and cheese industries, as well as a number of newly created producers. Of the imported enzymes, the market is represented mainly by preparations manufactured by Hr. Hansen (Denmark), drugs from the Dutch company DSM-Food Specialties (DSM-FS), Caglificio Clerici SPA (Italy), etc.

Due to the shortage of natural rennet powder in cheese making, other preparations began to be widely used, which can be divided into two groups: pepsins - gastric proteases of ruminants and some other animals - and acid proteases of microbial origin. Of the first group, beef and pork pepsins are most widely used. Pepsins are most often used in mixtures with rennet powder.

A wide range of milk-clotting preparations, the lack of objective information about their composition and properties sometimes confuses the masters of cheese-making enterprises, and they often make the choice of a preparation, guided only by its price, and not by quality. At the same time, few people select an enzyme preparation taking into account the range of cheeses produced. For the cheese industry, specialized companies supply milk-clotting enzyme preparations with an established ratio of chymosin and pepsin. The purpose of the work was to determine compliance with the criteria declared by the manufacturers, namely: milk-clotting activity and the ratio of the two main enzyme components: beef pepsin and chymosin. Milk-clotting enzyme preparations were studied, which are in the greatest demand at the cheese-making enterprises of the Altai Territory, namely: edible beef pepsin according to OST 10-023-94, production date 24.03.05, rennet (SF) and rennet-beef enzyme ( VNIIMS SG-50) according to OST 10-288-2001, production date 03/29/06; as well as milk-clotting rennet preparations Clerici 96/4 (production date 05/2006, batch number 604 141 174), Clerici 70/30 (production date 06/2005, batch number 506 164 550), Clerici 50/50 (production date 05/2006, batch number 605 084 530) manufactured by Caglificio Clerici SPA, Italy. To determine the ratio of beef pepsin and chymosin in the study of milk-clotting enzyme preparations, the method for determining the share of activity of beef pepsin from the total milk-clotting activity of the preparation according to OST 10 288-2001 was used.

To determine the milk-clotting activity, 5 ml of the substrate was poured into thin-walled glass tubes, heated in a water bath at 35 0C and kept for three minutes, then 0.1 ml of the studied enzyme preparation was added, the stopwatch was immediately started, and the contents of the tube were immediately mixed. The start of the coagulation reaction was determined by the formation of flakes in a drop of milk applied to the walls of the test tube with a glass rod. After determining the start of clotting, the stopwatch was immediately turned off. Milk-clotting activity (MA) was calculated by the formula: MA = A*T1/T2, where: A – certified activity of OKO SF; Т1 – clotting time with OKO SF; T2 is the clotting time with the test sample. When preparing milk-clotting preparations, 1 g of the test sample of the enzyme preparation was dissolved in 80.0 cm3 of distilled water at a temperature of 35 0C, stirred for 30 minutes, the total volume was adjusted to 100.0 cm3 and infused in a water bath at a temperature of 35 0C for 15 minutes . The preparation of an industry control sample (ICC) of bovine pepsin was carried out in a similar manner. Raw milk served as a substrate in determining the proportion of beef pepsin activity and milk-clotting activity. The preparation of the substrate was carried out as follows: raw combined unpasteurized milk was heated in a water bath to a temperature of 72 0C, incubated at this temperature for 10 minutes and quickly cooled under running tap water to 20-25 0C. Calcium chloride was added to chilled milk to a final concentration of 30 mM. If necessary, the active acidity of milk was adjusted to 6.5 units. pH with 1.0 M HCl solution. The milk thus prepared was used for further research. The results of the work carried out are presented in table 1.

* - according to OST 10 288 [clause 8.2.2.6, p.19] the error of the method used is 5000 units. from the total milk-clotting activity of the drug

When evaluating the suitability of milk-clotting preparations for cheese production, milk-clotting activity must be taken into account. Optimal milk-clotting activity is one of the main characteristics that affect the quality of the curd during cheese production. As can be seen from table 1, milk-clotting activity VNIIMS SG-50, GP and Clerici 70/30 are slightly higher than declared. The availability of this information at the enterprises of the cheese-making industry can contribute to a more optimal consumption of drugs.

The action of rennet in the process of coagulation of milk is determined primarily by the action of chymosin and, to a lesser extent, pepsin. An increase in the relative content of pepsin in SF leads to the formation of a looser clot during milk coagulation, which is accompanied by a decrease in cheese yield due to loss of protein and fat with whey. As can be seen from Table 1, SF contains a small amount of pepsin. When using SF containing mainly chymosin, cheeses of the best quality are obtained, with a maximum yield of products.

Classical rennet has found wide application in the cheese industry. Information about the use of pepsin in cheese making and mainly for the production of certain types of cheese is different. Especially successful were experiments on the production of cheese using a mixture of 50% chymosin and 50% pepsin. The use of this mixture allows you to get results that are much better than using pure pepsin. From the data in Table 1, it can be seen that in the VNIIMS SG-50 and Clerici 50/50 preparations, the relative content of pepsin is slightly higher than the declared one.

In the milk-clotting enzyme preparation and Clerici 70/3, the ratio of chymosin and beef pepsin corresponds to the declared one. In Clerici 96/4, the relative content of pepsin is slightly higher than the declared one. A higher proportion of the milk-clotting activity of beef pepsin from the total milk-clotting activity of the drug may be due to a number of factors. One of them may be a violation of storage conditions. The manufacturer "Caglificio Clerici SPA" (Italy) guarantees a loss of activity of no more than 4% during two years of storage in a cool place at a temperature of 4 to 8 0C.

Milk-clotting enzyme preparations must be stored in a packaged form in a dry place protected from light, at a temperature not exceeding 10 0C and relative humidity not more than 75% [OST 10 288, clause 9.2.1, p.44]. These temperature regimes could be violated during transportation or storage of goods in a warehouse. The second factor may be the error of the method used, in which the limits of the permissible value of the absolute measurement error are 5% in terms of the share of activity of beef pepsin from the total milk-clotting activity of the drug [OST 10 288, p. 8.3.5, p. 26].

Thus, cheese-making enterprises, choosing one or another preparation, must take into account its features and control, first of all, the yield of cheese and its quality.

The site provides reference information for informational purposes only. Diagnosis and treatment of diseases should be carried out under the supervision of a specialist. All drugs have contraindications. Expert advice is required!

What is pepsin?

Pepsin is an enzyme that is part of the gastric juice and is produced by the gastric mucosa. Pepsin breaks down almost all proteins of animal and vegetable origin. The enzymes of the pancreas - trypsin and chymotrypsin - also participate in the breakdown of proteins. But pepsin, unlike these enzymes, does not have a strict specificity for cleavable proteins.

The action of pepsin is manifested only in an acidic environment. The optimal activity of pepsin is noted at a concentration of free hydrochloric acid of at least 0.15-0.2%, the maximum activity of pepsin is at pH = 1.5-2.0.

In some diseases, there is a complete absence (achilia) or a decrease in the production of hydrochloric acid in the stomach (hypoacid state). The consequence of this pathology is the lack of digestive activity of pepsin and, consequently, gastric juice. In such cases, substitution therapy is used - taking pepsin or preparations containing pepsin.

The pharmaceutical preparation pepsin is prepared from the stomachs of pigs, cattle, chickens and chickens. Digestive activity of chicken pepsin is observed in a larger pH range (2-4) than porcine pepsin. This allows you not to prescribe additional hydrochloric acid for admission.

It is used for oral administration and the enzymatic preparation Acidine-pepsin. Betaine hydrochloride, which is part of it, is converted in the stomach into free hydrochloric acid, which activates pepsin.

Release form

• Pepsin is produced in the form of a powder, which should be stored in closed jars, in a dark place, at a temperature of +2 to +15 o C. The powder has a yellowish or white color, sweet and sour taste, dissolves well in water and ethyl alcohol ( 20%). In a pharmacy, a solution of pepsin and hydrochloric acid in water is prepared from the powder.
• Pepsin K (chicken pepsin) - tablets of 0.1 g; the tablet contains 0.04 g of pepsin; in the package of 25 or 50 tablets.
• Acidin-pepsin (a combination preparation consisting of 1 part of pepsin and 4 parts of betaine hydrochloride) is available in the form of tablets of 0.25 or 0.5 g, 50 pieces per pack.
• Ointment with pepsin is not produced by pharmaceutical factories, but is prepared in pharmacies by prescription (5-10% ointment: pepsin with hydrochloric acid on a vaseline or lanolin basis).

Instructions for use of pepsin and acidin-pepsin

Indications for use

Ingestion of pepsin is indicated for diseases of the gastrointestinal tract with reduced secretory function of the stomach:

• hypoacid gastritis (reduced production of hydrochloric acid in the stomach), anacid gastritis (inflammation of the stomach in the absence of hydrochloric acid production);
• akhiliya (lack of production of hydrochloric acid and digestive enzymes in the stomach) with atrophic gastritis, lack of proteins and vitamins in the diet, malignant anemia, cirrhosis of the liver, endocrine disorders (increased levels of thyroid hormones), etc .;
• condition after removal of part of the stomach;
• dyspepsia (indigestion).

Externally, pepsin can be used to treat keloid scars, necrotic ulcers that do not heal for a long time in the form of an ointment.

Contraindications

Pepsin and Acidine-pepsin are not prescribed for an allergic reaction to the drug, for gastric ulcer, erosive gastritis (superficial, shallow ulcers on the gastric mucosa), with increased acid and enzymatic function of the stomach.

Side effects

When using Pepsin and Acidine-pepsin, in rare cases, it may be noted:

• allergic reaction;
• violation of the stool (diarrhea or constipation);

Treatment with pepsin and acidin-pepsin

How to use?
Pepsin and Acidine-pepsin are taken orally during or after a meal. Before taking a tablet of Acidin-pepsin, you must first dissolve it in 100 ml of water, and pepsin in the form of a powder should be dissolved in water or in a 1-3% hydrochloric acid solution.

Ointment dressings are applied (strictly as prescribed by the doctor) for a day.

Pepsin is destroyed by alcohol, so alcohol should be avoided while taking this drug.

Dosage
Inside, pepsin is prescribed to adults at a dose of 0.2-0.5 g during or after a meal in the form of a powder or in a 1-3% solution of diluted hydrochloric (hydrochloric) acid 2-3 times a day. The duration of the course is set by the doctor. Usually prescribed for 2-4 weeks.

For children, pepsin is prescribed only by a doctor at a dose of 0.05 to 0.3 g 2-3 times a day or in a 1-2% hydrochloric acid solution, depending on age.

Pepsin K is taken 1-2 (maximum 3) tablets after meals for a course of 2 to 4 weeks.

Acidin-pepsin for adults is prescribed 0.5 g 3 times a day. Children are prescribed half or a quarter of a tablet (0.25 each), depending on age.

Compatibility with other drugs

The effectiveness of pepsin-containing drugs is reduced with the simultaneous use of acid-reactive drugs, tannin, antacids (baking soda, burnt magnesia, Bourget mixture, Rennie, Tams, Andrews antacids and others), or with the use of drugs containing salts of heavy metals (Collargol, Salicylic-sulfur - zinc paste, etc.).

Pepsin analogs

Acidine-pepsin analogs are produced abroad: Beta-pepsin, Betacid, Pepsamine, Acidol-pepsin, Acipepsol, Solgar, etc.

Drugs that have a similar effect:
Festal, Abomin, Penzital, Longidaza, Panolez.

This article will focus on an essential enzyme found in the stomach of every mammal, including humans. General information about the enzyme pepsin, information about its isomers and the role of the substance in digestion will be considered.

General representations

First, let's find out what class of enzymes pepsin belongs to. This will allow you to delve deeper into the topic itself.

The pepsin enzyme belongs to the proteolytic class of hydrolases and is produced by the gastric mucosa, and its main task is to break down proteins that come with food to peptides. Pepsin - in It is produced by the organisms of all mammals, as well as reptiles, representatives of the class of birds and many fish.

The presented enzyme belongs to the type, has a molecular weight of approximately 34500. The molecule itself is presented in the form of a polypeptide chain and consists of three hundred and forty amino acids. It also contains HPO3 and three disulfide bonds in its composition.

Pepsin is widely used in medicine and cheese making. In laboratories, it is used for the purpose of a more detailed study of protein compounds, namely, the primary protein structure. Pepsin has a natural inhibitor - pepstatin.

Enzyme Diversity

Pepsin has twelve isoforms. The differences between all pepsin isomers are in electrophoretic motor ability, inactivation conditions, pepsin code - CF 3. 4. 23. 1.

In humans, the stomach juice contains seven types of pepsin, and five of them differ sharply in some qualities:

1. Pepsin itself (A) has the maximum activity in the medium pH = 1.9, and when it rises to 6, it is inactivated.
2. Pepsin 2 (B) is maximally active in pH = 2.1.
3. Type 3 shows the highest degree of activity at pH = 2.4-2.8.
4. Type 5, also known as gastrixin, has the highest degree of activity at a pH of 2.8-3.4.
5. Type 7 at pH = 3.3-3.9 has the highest activity.

The importance of the enzyme in digestion

Pepsin is secreted by the gastric glands in an inactivated form (pepsinogen), and hydrochloric acid activates the enzyme itself. Under its influence, he goes into a workable form. A prerequisite for the activity of the pepsin enzyme is the presence of an acidic environment, which is why when pepsin passes into the duodenum, it loses its activity, since the environment in the intestine is alkaline. The pepsin enzyme occupies one of the key roles in the digestion of the entire class of mammals, and in particular humans. This substance breaks down food proteins into smaller peptide chains and amino acids.

Men and women produce this enzyme differently. Men excrete about twenty to thirty grams of pepsin per hour, while women have twenty to thirty percent less. The basal cells, sites of pepsin production, secrete it in the non-working form of pepsinogen. After cleavage of a certain amount of peptides from the N-terminus, pepsinogen passes into its active form. Hydrochloric acid acts as a catalyst in this chemical transformation reaction. Pepsin has protease and peptidase properties and is responsible for the disaggregation of proteins.

Medical business

In medicine, pepsin is widely used as a drug for some diseases associated with a lack of production of this enzyme in the patient's stomach. Pepsin is obtained from the mucous membranes of the stomach. The drug is available in the form of tablets, arranged in blisters, with an admixture of acidin or in the form of powders. Pepsin is also part of some combined drugs. It has ATC code A09AA03. An example of a pathology in which pepsin-containing drugs are prescribed is Menetrier's disease.

Beef pepsin is...

Beef rennet pepsin is one of the well-known and most commonly used forms of this substance. The enzyme itself is produced in the fourth stomach of the calf. The preparation used in production is formed by two enzymes: pepsin and chymosin in natural proportional amounts. Rennet is used in cheese making, and its main functions are the formation of a clot of milk and participation in the process of maturation of cheese and curd products.

Beef pepsin is isolated from the stomachs of cattle and, in the manufacture of products for sale, goes through two stages of purification of the enzyme from fat and impurities that are insoluble. The process of making beef pepsin goes through several stages: extraction process, salting out and freeze drying.

Other applications

The enzyme pepsin is added to the sourdough. It is also used in cheese making. The rennet enzyme pepsin paired with chymosin form the same enzyme used to curdle milk.

The process of curdling milk is called its protein coagulation, namely casein, with the formation of a milk-based gel. Casein has a specific structure, and only one peptide bond is responsible for the enzymatic type of protein folding. The complex of pepsin with chymosin is actually responsible for breaking that very bond and leading to milk curdling.

Conclusion

Summing up, we can say that this biologically active substance is one of the most important enzymes involved in the digestion of food in the stomach in representatives of many classes of living beings. In production and medicine, the substance is mainly used as a medicine and is added to rennet for the production of dairy and cheese products.

) And pepsin.

Additional components: povidone, sorbitol, colloidal silicon dioxide, calcium stearate.

Release form

Acidin-Pepsin is produced in the form of powder, solution and tablets 250 and 500 mg, 50 pieces per pack. Also, in some pharmacies, you can purchase a specially prepared ointment with pepsin 5-10%, on a lanolin or vaseline basis.

pharmachologic effect

This drug has combined action. Improves digestion food in the stomach.

Pharmacodynamics and pharmacokinetics

Pepsin - what it is?

According to the Pharmacopoeia, pepsin - this is part of the gastric juice, which is produced by the mucous membrane of the stomach. It has also been found that this enzyme ensures the breakdown of almost all proteins of plant and animal origin. In addition, and, which are pancreatic enzymes, take part in this process. However, it is this enzyme that breaks down proteins without showing particular specificity to them, that is, it acts in an acidic environment.

Some diseases of the gastrointestinal tract cause a significant decrease or lack of production of hydrochloric acid leading to poor digestion pepsin and, accordingly, gastric juice. Therefore, patients are prescribed replacement therapy in the form of drugs based on it. For example, when taking the enzymatic preparation Acidin-Pepsin, one of its components is betaine hydrochloride converted in the stomach to hydrochloric acid , which activates an enzyme that improves digestion.

Indications for use

The main indications for the appointment of Acidin-Pepsin are various gastrointestinal diseases , which are characterized by reduced secretory function of the stomach. Therefore, the drug is recommended for:

• hypoacid gastritis;
• anacid gastritis;
• achilia - the absence of the synthesis of hydrochloric acid and other digestive enzymes in atrophic gastritis, nutrition with a lack of proteins and, a malignant form of anemia, endocrine disorders;
• period after removal of part of the stomach.

Preparations for external use are used in the treatment of keloid scars or necrotic, long-term healing wounds and ulcers.

Contraindications for use

• hypersensitivity ;
• hyperacidity of gastric juice, for example: erosive gastroduodenitis, And .

Side effects

When taking the drug may develop , nausea, abdominal pain.

Acidin-Pepsin, instructions for use (Method and dosage)

According to the instructions for Acidin-Pepsin, the drug in tablets is intended for oral administration at the same time or after meals. To do this, the tablets must be dissolved in 50-100 ml of water. Adult patients are recommended a daily dosage of 2 tablets taken 3-4 times. Children's dosage is a quarter or half a tablet to be taken 3-4 times a day.

The duration of the therapeutic course depends on the course of the disease and the effectiveness of the treatment, which the specialist can determine.

Overdose

Usually this drug is well tolerated by patients, therefore, cases of overdose have not been described in clinical practice. It is possible to develop: nausea, gastralgia, vomiting, diarrhea And various allergic reactions.

Interaction

Simultaneous use of enzyme preparations and acid-reactive agents,

Pepsin- the main proteolytic enzyme of gastric juice, belongs to the group of peptide hydrolases. Cleaves proteins mainly to polypeptides, although among the cleavage products there are low molecular weight peptides and amino acids. In some pathological conditions, the activity of pepsin in gastric juice is one of the diagnostic signs. The content of the proenzyme P. - pepsinogen - in the urine (uropepsin) serves as an additional diagnostic test in the study of the secretory ability of the gastric mucosa. Pepsin It is also used in the food and meat and dairy industry. The molecular weight of pepsin is about 35,000, the isoelectric point is at a pH below 1.0. Pepsin most stable at pH around 5.0-5.5. In a more acidic environment, autolysis of the enzyme occurs; at a pH above 6.0, its rapid and practically irreversible inactivation occurs (pepsin is also inactivated at temperatures above 60 °).

In the gastric juice of humans and higher mammals, along with P., there is gastrixin, an enzyme that has properties similar to pepsin and a homologous structure.

P. is synthesized by the main glandulocytes of the gastric mucosa in the form of an inactive precursor, the pepsinogen proenzyme, which, in the presence of hydrochloric acid of gastric juice, is converted into an active enzyme. In the urine of mammals, incl. a person, pepsinogen is normally detected (level pepsin).

The process of digestion of proteins in the gastrointestinal tract begins with the action of P. It breaks down almost all proteins of plant and animal origin, with the exception of protamines and keratins. The optimum action of pepsin is at pH 2.0. At a pH of about 5.0, pepsin curdles milk, causing the conversion of caseinogen to casein. P. is able to hydrolyze a number of low molecular weight synthetic peptides and esters, which include aromatic amino acids. The optimum for pepsin hydrolysis of many synthetic substrates is at pH 4.0. Pepsin also catalyzes the transpeptidation reaction (transfer of an amino acid residue from one synthetic substrate to another).

To determine the activity of pepsin, the Anson method is used, which consists in the splitting of denatured hemoglobin, followed by the determination of the amount of tyrosine in the protein-free filtrate. To study P.'s activity in gastric juice and the content of uropepsin in the urine, the Pyatnitsky method, based on determining the curdling activity of the enzyme, is widely used.

With a number of diseases of the gastrointestinal tract - chronic gastritis, gastric and duodenal ulcers (see. peptic ulcer), stomach cancer, as well as pernicious anemia, hypochromic anemia (see. anemia) pepsin secretion is impaired. In this regard, the determination of pepsin in gastric juice, along with hydrochloric acid, has significant diagnostic value. The determination of uropepsin in urine is also used, the content of which is believed to reflect the level of secretory ability of the gastric mucosa.

Pepsin(Pepsinum), used as a medicine, is obtained from the gastric mucosa of pigs. The drug is a white or cream powder of sweet taste with a specific odor, soluble in water, in 20% ethyl alcohol and insoluble in ether and chloroform.

Usually pepsin has a rather low proteolytic activity: 1 G the drug contains only 5 mg pure enzyme. To ensure the optimal effect of the drug, the reaction of the medium in the stomach should be acidic, and the concentration of free hydrochloric acid should not be lower than 0.15-0.2%.

Pepsin used for replacement therapy for digestive disorders, accompanied by secretory insufficiency of the stomach (achilia, hypoacid and anacid gastritis, dyspepsia, etc.). It should be borne in mind that the main glandulocytes of the gastric mucosa usually secrete endogenous P. in excessive quantities, as well as other digestive enzymes. Therefore, a decrease in the digestive capacity of gastric juice with a decrease in its acidity is often the result of insufficient release of hydrochloric acid, and not a decrease in the activity or intensity of pepsin formation. Thus, in hypoacid conditions, the main thing is to provide optimal conditions for the digestion of gastric contents, and the use of pepsin is of secondary importance. In anacid conditions, when the acid-forming function of the stomach is reduced, it is advisable to use P. in combination with diluted hydrochloric acid.

Pepsin appoint inside: adults 0.2-0.5 G for reception 2-3 times a day before meals or during meals in powders or in 1-3% hydrochloric acid solution (10-15 drops in half a glass of water); children 0.05-0.3 G in 0.5-1% hydrochloric acid solution.

Contraindications to taking pepsin are hyperacid gastritis, exacerbation of stomach ulcers. The drug used in therapeutic doses does not have side effects.

Release form: powder. Storage: in well-closed jars in a cool (from 2 to 15 °), protected from light place.

The drug acidine pepsin(Acidin-pepsinum) contains 1 part of pepsin and 4 parts of betaine hydrochloride, which is hydrolyzed in the stomach to form free hydrochloric acid (0.4 G betaine corresponds to about 16 drops of dilute hydrochloric acid). Tablets of acidin-pepsin (0.5 and 0.25 G) is dissolved in half a glass of water and taken 3-4 times a day with meals. Similar tablets produced abroad - "Acidol- pepsin”, “Betacid”, “Acipepsol”, “Pepsamine”.

Bibliographer.: Antonov V.K. Chemistry of proteolysis, p. 31, M., 1983; Mosolov V.V. proteolytic enzymes, p. 101, M., 1971, Radbil O.S. Pharmacological bases for the treatment of diseases of the digestive system, p. 78, M., 1976.