Both of alpha-chymotrypsin and papain were active in hydrolysis of proteins by temperature, acid and alkali proteins. Alpha-chymotrypsin hydrolysed protein better than papain. They were effective in digestion of mouse protein in inflamed tissue by Kaolin, Dextran and Formal in different level according this increasing order: Kaolin < Dextran < Formal. -chymotrypsin was better than papaine in hydrolysis of protein in inflamed tissue. Therefore, we can explain the anti inflammatory characters of those enzymes.
Chymotrypsin ; Papain

No abstract available.
Ear* ; Papain*

The reasonable pepsin + papain mix was studied. The results showed that the proteolytic activity of the mix at 3 areas pH: 20.5, 41 and 70.5 and temperature 38O2 was compared with either agent alone in the same conditions. These mixes will be improved and applied to the treatment of malnutrition in children
Peptide Hydrolases ; Enzymology ; Pepsin A ; Papain

OBJECTIVES: This study aimed to evaluate the capacity of 2% chlorhexidine gel associated with 8% papain gel in comparison with 5.25% sodium hypochlorite in bovine pulp tissue dissolution. MATERIALS AND METHODS: Ninety bovine pulps of standardized sizes were used and fragmented into 5-mm sizes. The fragments were removed from the root middle third region. They were divided into 6 experimental groups (n = 15), 1) 8% papain; 2) 2% chlorhexidine; 3) 2% chlorhexidine associated with 8% papain; 4) 0.9% saline solution; 5) 2.5% sodium hypochlorite; and 6) 5.25% sodium hypochlorite. The pulp fragments were weighed and put into immobile test tubes for dissolution for time intervals of 30, 60, 90, and 120 min. RESULTS: The 5.25% sodium hypochlorite had greater dissolution potential than the pure papain, and when associated with chlorhexidine, both promoted greater dissolution than did the saline solution and 2% chlorhexidine groups (p < 0.05). The 2.5% sodium hypochlorite promoted dissolution to a lesser extent than the groups with papain within a period of 30 min (p < 0.05), but, was comparable to the saline solution and chlorhexidine. After 120 min, the 2.5% and 5.25% sodium hypochlorite promoted dissolution of 100% of the pulp fragments, and papain, 61%, while chlorhexidine associated with papain and chlorhexidine alone dissolved only 55% and 3%, respectively. CONCLUSIONS: The 8% papain in gel, both alone and in association with chlorhexidine, was able to dissolve bovine pulp tissue, but to a lesser extent than did 5.25% sodium hypochlorite.
Chlorhexidine* ; Endodontics ; Papain* ; Sodium Chloride ; Sodium Hypochlorite

The enzymatic synthesis of a tetrapeptide Phac-Met-Gly-Trp-Met-OEt, a fragment of the cholecystokinin C-terminal octapeptide CCK-8, was reported. This fragment was synthesized by coupling Phac-Met-OEt with Gly-OMe, Trp-OMe and Met-OEt successively. These three steps were catalyzed by alpha-chymotrpsin, Papain and alpha-chymotrpsin respectively. The results of FAB-MS showed that all the products had the correct molecular mass.
Catalysis ; Chymotrypsin ; Oligopeptides ; Papain ; Peptide Fragments ; Sincalide ; chemical synthesis

The synthesis of CCK-4 (H-Trp-Met-Asp-Phe-NH2) by using enzymes exclusively was described. As protection group for the amino group we used the Phenylacetyl group (Phac) which had been cleaved at the end of the synthesis with Penicillin G Amidase (PGA) without affecting the peptide bonds. Thus, beginning with Phac-Trp-OH we had successfully synthesized the target peptide with following 4 enzymes, alpha-Chymotrypsin, Papain, Thermolysin and PGA in four reaction steps. All reactions were carried out in aqueous buffer in reasonable yields (> 65%). FAB-MS or FD-MS verified the correct molecular mass of all peptides.
Chymotrypsin ; Enzymes, Immobilized ; Papain ; Peptides ; Tetragastrin ; chemical synthesis ; Thermolysin

The enzymatic synthesis of a tetrapeptide Phac-Met-Gly-Trp-Met-OEt, a fragment of the cholecystokinin C-terminal octapeptide CCK-8, was reported. This fragment was synthesized by coupling Phac-Met-OEt with Gly-OMe, Trp-OMe and Met-OEt successively. These three steps were catalyzed by alpha-chymotrpsin, Papain and alpha-chymotrpsin respectively. The results of FAB-MS showed that all the products had the correct molecular mass.
Catalysis ; Chymotrypsin ; *Oligopeptides ; Papain ; Peptide Fragments ; Sincalide/*chemical synthesis

The synthesis of CCK-4 (H-Trp-Met-Asp-Phe-NH2) by using enzymes exclusively was described. As protection group for the amino group we used the Phenylacetyl group (Phac) which had been cleaved at the end of the synthesis with Penicillin G Amidase (PGA) without affecting the peptide bonds. Thus, beginning with Phac-Trp-OH we had successfully synthesized the target peptide with following 4 enzymes, alpha-Chymotrypsin, Papain, Thermolysin and PGA in four reaction steps. All reactions were carried out in aqueous buffer in reasonable yields (> 65%). FAB-MS or FD-MS verified the correct molecular mass of all peptides.
Chymotrypsin ; Enzymes, Immobilized ; Papain ; Peptides ; Tetragastrin/*chemical synthesis ; Thermolysin

OBJECTIVE: To investigate the role of multiple serological methods in the identification of complex antibodies. METHODS: The blood group antigens were detected by saline and microcolumn agglutination methods. The saline method was used to screen and identify IgM-type antibodies in the patient's serum, while the polybrene, anti-globulin, microcolumn agglutination, enzymic and absorption-elution methods were used to screen and identify IgG-type antibodies. RESULTS: The patient was B/CCDee/Jk(a-b+)/Fy(a-b+) blood type. The serum reacted with panel cells, and the reaction presented anti-E pattern in the saline medium. It was fully positive in the microcolumn agglutination card, except 2 negative ones after using papain to treat the panel cells. Referring to the pattern table, it was concluded that there existed anti-c, anti-E, and anti-Jk^a antibodies, and one antibody corresponding to an antigen that was easily destroyed by papain. The red blood cells with specific phenotype were selected for absorption-elution to identify IgG-type anti-c, anti-E, anti-Jk^a and anti-Fy^a antibodies. CONCLUSION It is confirmed that IgM-type anti-E, and IgG-type anti-c, anti-E, anti-Jk^a and anti-Fy^a antibodies exist in the patient's serum by multiple serological methods.
Humans ; Papain ; Blood Group Antigens ; Erythrocytes ; Immunoglobulin G ; Immunoglobulin M

BACKGROUND: Several keratolytic agents have been used in many dirmatologic conditions such as callus, keratosis palmaris of plantaris, however the evaluation method of the effects of keratolytiic agents has not been good enough in clinical use. OBJECT: We have conducted an investigation to measure the effect of several keratolytic agents using an in vitro model. METHOD: We measured the fegraded protein of keratin by the bui iet method after adding enzymes such as trypsin, pepsin and papain, and irritants, salicylic acid and sodii m lauryl sulfate to the collected callus. RESULT: The order of the keratolytic effect of the enzymes was trypsir >pepsin>papain. It was difficult to detect the keratolytic effect of salicylic acid becaues of color hiidrance and there was an increasing tendency of keratolyti effect of sodium lauryl sulfate, however it was prominent mainly at a high concentration. CONCLUSION: These results suggested that the potency of similar types of keratolytic enzymes such as pepsin, trypsin and papain can be possible. However it was not such a sitable model to check the potency of the keratolytic effect of salicylic acid and the eoncentration tevel may be an important factor for certain kinds of chemicals such as sodium lauryl sulfate.
Bony Callus ; Irritants* ; Keratolytic Agents ; Keratosis ; Papain ; Pepsin A ; Salicylic Acid ; Sodium Dodecyl Sulfate ; Trypsin