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PubMed2000

Identification and molecular cloning of cathepsin P, a novel human putative cysteine protease of the papain family.

A cDNA encoding a novel human putative member of the papain family of cysteine peptidases has been cloned. The protease, named cathepsin P, is synthesized as a preproprotein. The presumed propeptide of 38 amino acids is followed by a 242-residue mature protein. The mature protease region is 30% identical to human papain-like cathepsins, with all the residues important for catalysis conserved. No similarity was observed in the propeptide region. On the contrary, the proenzyme shares 51-87% residues with some precursors of cysteine proteases from other species that have not yet been characterized. They all show a nearly completely conserved "CYTRED motif" in the propeptide region, not present in other members of the family, and could therefore constitute a distinct subfamily.

Amino Acid Sequence↗
PubMedDate not supplied

[Anti-inflammatory activity of domestic papain].

The influence of domestic papain to the course of experimental inflammation due to formalin, dextrane, histamine, serotonin and infectious arthritis has been studied. The domestic papain in doses of 0.325 and 0.75 mg/kg possesses strongly marked antiinflammatory activity and this ability is no less than that of butadion and indomethacin.

Animals↗
PubMed1975

Subfragments of the papain solubilized TL antigen.

TL antigen was solubilized from the tumor ASLI (TL. 1,2,3) by papain digestion. The subfragments of 125I-labeled TL were examined by two methods. The first involved immune precipitation followed by electrophoresis on SDS-acrylamide gels. This treatment yielded three bands of molecular weight 39,000 and 19,000, as well as material which migrated with the tracking dye. In the second procedure the papain digested material was partially purified on Sephadex G-200. The active fraction from G-200 was labeled with 125Iodine, mixed with alloantiserum and rechromatographed on G-200. The isolated immune complexes were boiled in SDS and 2-mercaptoethanol, then separated on a SDS-Sephadex G-150 column. Two radioactive peaks were eluted indicating an absence of the 19,000 m.w. component following the latter method of purification.

Animals↗
PubMed2004

[Immobilization and stabilization of papain on SiO2 particles containing amine groups].

Numerous approaches and materials have been explored for preparation of immobilization enzymes because they have considerable advantages over enzyme in bulk solution. Among present enzyme carriers inorganic materials have lower cost and more stability than organic materials. But the present inorganic materials contain less active sites and have to undergo some complicated processes before binding enzyme. So it is necessary to explore a new kind of inorganic enzyme carrier. Papain, a well characterized thiol protease kinetically and structurally, is a suitable model to compare the efficiency of various immobilization procedures. SiO2 particles containing amine groups were synthesized by synchronous hydrolysis of tetraethylorthosilicate (TEOS) and N-(2-aminoethyl)-3-aminopropyltrimethoxysilane (AEAPS) in W/O Microemulsion of Triton X-100/cyclohexane/ammonium hydroxide system. The obtained particles have a diameter range from 0.3 microm to 0.5 microm, and their average size is 0.37 microm and can be controlled by adjusting water to surfactant molar ratio and water to TEOS and AEAPS molar ratio. Compared with traditional porous silica beads, these particles contain much more amine groups and their amine group content can be easily changed in the process of synthesis. Papain was immobilized on the particles which were treated by glutaraldehyde with covalent method. The optimum immobilization conditions of enzyme were as follows: enzyme load was 15 mg/g carrier, pH was 6.5. The pH and temperature optima were 6.5 and 70 degrees C for immobilized enzyme. All above indicate this kind of particle can be a good enzyme immobilization carrier.

Amino Acids↗
PubMed1991

Recombinant Q53E- and Q53N--chicken egg white cystatin variants inhibit papain, actinidin and cathepsin B.

A cloned synthetic gene coding for (AEF S1M M29I M89L) chicken egg white cystatin was modified site-specifically at position Q53 by cassette mutagenesis. Two recombinant variants were isolated from a pIN-III-ompA E. coli expression system and purified by Cm-papain affinity chromatography. The mutations at the position 53 were confirmed by amino acid composition and amino acid sequence analysis of the appropriate tryptic peptides. The complexes of both cystatin variants, the Q53E- and Q53N-variant with papain, display Ki values similar to those determined with native chicken cystatin. However, the Ki values of the complexes with actinidin are hundredfold and with cathepsin B three hundredfold higher than with the native chicken cystatin. The different inhibition kinetics of these variants compared to wild type chicken cystatin emphasizes the specificity of single amino acid substitutions for optimal contacts between the binding segments of enzyme and inhibitor.

Amino Acid Sequence↗
PubMed1991

Deletion of the carboxy terminal part of stefin B does not have a major effect for binding to papain.

Determination of crystal structures of chicken cystatin and human stefin B complexed with papain revealed a novel model of protease inhibition and also structural differences between two cysteine proteinase inhibitor (CPI) families. According to the 3D alignment, stefins have an extension of 9 amino acids on their carboxy terminus in comparison with cystatins. The extension was not expected to make a major contribution to interaction with the enzyme. A deletion mutant of stefin B, corresponding in length to the carboxy terminal sequence of chicken cystatin, was constructed by the use of polymerase chain reaction (PCR). This (C3S, delta 89-98) human stefin B, 10 amino acids shorter, inhibited papain with a Ki of 0.012 nM which is comparable to the Ki of 0.03 nM for authentic, nondeleted recombinant stefin B. This finding thus confirms the tertiary structure-based alignment.

Amino Acid Sequence↗
PubMed1990

Inhibitory activity of papain on facultative pathogens--short communication.

Papain, a proteolytic enzyme obtained from papaya was found inhibitory on few facultative pathogens. While Escherichia coli, Staphylococcus albus, Klebsiella pneumoniae and Enterobacter cloacae were inhibited at concentration from 200 ppm on the cell density of Staphylococcus faecalis decreased only at higher concentration of papain (400-800 ppm).

Enterobacter↗
PubMed1990

[Papain phonophoresis in the treatment of suppurative wounds and inflammatory processes].

The authors studied the effect of papain and dimethyl sulfoxide (DMSO) phonophoresis on the course of purulent wounds and inflammatory processes in patients. It is shown that the use of 1% papain solution together with DMSO by means of phonophoresis is a very effective and promising method for the treatment of purulent wounds and inflammatory infiltrates. The terms of restoration of the structure of the injured tissues are reduced by 1.8 times on the average.

Bacterial Infections↗
PubMedDate not supplied

[Papain immobilization on a fibrous polymer of polyvinyl alcohol].

The paper discusses papain immobilization on modified polyvinyl alcohol fibers by the ion fixation technique. The effect of the chemical structure of polyvinyl alcohol fibers on the basic properties of the bound enzyme has been examined. The level of activity and tolerance to pH changes of the resultant immobilized enzymes have been shown to depend on the papain arrangement in the polymer molecule.

Enzymes, Immobilized↗
PubMed1989

[Treatment of patients with lung abscess by local administration of papain].

Under study were results of treatment of 109 patients with lung abscess aged from 17 to 76 years. All the patients were treated by active antiinflammatory therapy, bronchosanitation measures. In addition, local treatment by transthoracal punctures and drainage of the abscess cavity was used. Patients of the main group (52 patients) were given transthoracal injections of 0.5% solution of papain. The inclusion of papain in the complex therapy of patients with a lung abscess allowed to improve results of the treatment of this severe disease. The method may be recommended for wide use in pulmonology.

Adolescent↗
PubMed1988

Effect of papain digestion on the specificity of fluorescein-labeled immunoglobulins.

During initial studies, we found that many fluorescein isothiocyanate-labeled anti-immunoglobulin conjugates were unstable and tended to aggregate and precipitate when used for indirect immunofluorescence microscopy. In some instances, the precipitate was extensive enough to interfere with interpretation of the test results. Attempts to resolve this problem resulted in a procedure by which such conjugates were digested with papain to Fab and Fc fragments before use. Aggregation and precipitation were prevented, while desired antibody activity was retained. Digestion with papain also reduced the diffuse background fluorescence (commonly referred to as nonspecific fluorescence or staining) that is often associated with conjugates before they are sorbed with tissue powders or chromatographed to remove highly labeled immunoglobulin molecules.

Animals↗
PubMed1975

Common antigenic structures of HL-A antigens. VI. Common antigenic determinants located on the 33,000 Dalton alloantigenic fragment portion of papain-solubilized HL-A molecules.

HL-A 33,000 Dalton fragments were isolated from three papain-solubilized HL-A preparations carrying different HL-A allospecificity by the dissociation induced in the reaction with rabbit antibodies to HL-A 11,000-Dalton fragment (i.e. human beta2-microglobulin). By assaying the binding activity with rabbit antisera against papain-solubilized HL-A molecules and against each of the HL-A component fragments and also with a battery of HL-A alloantisera, the 'antibody-dissociated' 33,000-Dalton fragments were shown to retain not only the HL-A alloantigenic determinants but also the HL-A common antigenic determinants that are native to the 33,000-Dalton fragment portion of undissociated HL-A molecules and to be devoid of the cryptic HL-A common antigenic determinants that are found on HL-A 33,000-Dalton fragments obtained by dissociation with chemical reagents including acid. However, on exposure to acid, the antibody-dissociated 33,000-Dalton fragments were found to lose their HL-A alloantigenic and common antigenic characteristics and gain the cryptic HL-A common antigenic determinants. The greater part of the HL-A common antigenic determinants found here appears to be primate cross-reacting determinants.

Animals↗
PubMed1984

[Experimento-clinical basis for using papain in purulent surgery].

Experimental injections of a home-made proteolytic enzyme of vegetative origin--papain--in doses 5 to 36 mg/kg have not provoked any toxic effect upon the body and the serous membranes. The clinical use of 0.2-0.5% papain solution for the local treatment of purulent processes has proved its high proteolytic activity and its ability to shorten the first phase of the wound process. The preparation does not cause any local or general complications and can be successfully used in purulent surgery in hospital and in out-patient practice.

Abscess↗
PubMed1983

Effects of papain treatment of lymphocytes on the expression of their membrane surface markers.

Surface marker characteristics of normal and CLL lymphocytes were often considerably modified by treatment with papain. E-SRBC of normal lymphocytes were markedly increased while those of the CLL lymphocytes remained unchanged except in occasional instances. By comparison, EA gamma of normal lymphocytes were unaffected while those of the CLL lymphocytes were markedly increased in most instances. These changes were consistent with reclustering of these receptor sites induced by papain. EAC and E-MRC were destroyed in both groups but SmIg remained unchanged.

Animals↗
PubMed1978

Suppression of CFU-s activity by rabbit-anti-mouse brain serum can be overcome by treatment with papain.

The suppression of CFU-s activity which is observed after incubation with rabbit-anti-mouse brain sera (RAMB) can be reversed by incubating the antibody coated cells with papain. Papain treatment does not alter the CFU-s membrane since pre-treatment with the enzyme does not protect CFU-s from the lethal effect of RAMB. This technique should allow the use of fluoresceinated or otherwise labelled RAMB for the selection of CFU-s.

Animals↗
PubMed1982

Mechanism of enhanced complement-dependent cytotoxicity of papain-treated lymphocytes: evidence for increased stability of classical pathway C3 convertase.

The mechanisms of enhanced antibody-mediated, complement-dependent cytotoxicity caused by proteolytic treatment of cells was studied in a model system based on HLA microlymphocytotoxicity methods. In this model, papain treatment of lymphocytes resulted in a) no change in antibody binding, b) a slight decrease in initial binding of C4, c) a marked increase in stability of cell-bound C4b, resulting in d) an increase of cell-bound C3, and e) no increase in lytic efficiency of the C5b-9 membrane attack complex. We conclude that the most important step in papain enhancement of lysis of lymphocytes is an increased stability of cell-bound C4b, possibly through decreased surface binding of C4-bp. This mechanism may be relevant to the pathologically increased lysis of cells occurring in patients with hereditary erythroblastic multinuclearity with a positive acidified-serum test (HEM-PAS).

Anemia, Dyserythropoietic, Congenital↗
PubMed1981

[Creation of experimental emphysema by the intratracheal administration of papain].

The authors formed lung emphysema in white rats under experimental conditions by intratracheal application of various concentrations of papaine at different intervals. In the performed experiment the most suitable dose for formation of emphysema was two fold administration of 2 milligrams of papaine. The following indices were observed in the experimental and control animals: body weight, weight coefficient of the internal organs, indices of lipid and nucleinic metabolism in homogenates of lung as well as histomorphologic examination of lung.

Animals↗