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PubMed1992

[Extracorporeal immunosuppressive effect of papain].

Exposure of allogenic erythrocytes to papain induced their immunosuppressing properties within relatively narrow ranges of the incubation medium temperature (42 but not 37 or 40 degrees C) and the papain concentration (10 but not 2 or 50 micrograms/ml). Markedly pronounced immunosuppressing properties were acquired by the erythrocyte light fraction after heating and exposure to papain. The supernatant layer of adhesive spleen cells incubated in the presence of erythrocytes heat treated and exposed to papain suppressed development of the humoral immune response and DTH during the allogenic transfer and accelerated and increased excretion of the antigen specific immunosuppressing factor by the nonadhesive spleen cells of hyperimmunized sheep red blood cells.

Animals↗
PubMed2005

[Oriented immobilization of papain on metal chelating carriers].

Based on the technology of protein separation with immobilized metal ion affinity chromatography (IMAC), a method for oriented immobilization of papain has been selected. Papain was successfully immobilized on magnetic agarose carriers. Cu2+ with iminodiacetate (IDA) was used as the chelating ligand to be correlated with the histidine on papain (His-81). The optimum immobilization conditions of enzyme were as flows: Cu2+ 0.15 x 10(-2) mol/g carriers, time was 4h, enzyme load was 30 mg/g carrier, pH was 7.0, respectively. The pH and temperature were 8.0 and 70 degrees C for immobilized enzyme. The recovery activity of immobilized enzyme was retained 68.4%. The carrier could be recovered from the spent immobilized enzyme, to be reused. After 5 times, the reimmobilization of papain on the regenerated matrix was 79.71% effective with the retention of maximum enzyme activity. The cost of carriers used for industrial applications is very important. The regenerability of carriers is therefore, relevant. The mild conditions used for immobilization, the high recovery of immobilized preparations, the stability and the regenerability of the matrix are the main features of the method reported here. All above indicate this method can be applicable and promising in enzyme immobilization field.

Catalysis↗
PubMed1991

Papain-inhibitory activity of oryzacystatin, a rice seed cysteine proteinase inhibitor, depends on the central Gln-Val-Val-Ala-Gly region conserved among cystatin superfamily members.

Oryzacystatin, a cysteine proteinase inhibitor occurring in rice seeds, contains a particular glycine residue (Gly5) near the NH2-terminal position, and the sequence Gln53-Val54-Val55-Ala56-Gly57 in a central part of the molecule. Both are conserved among most members of the cystatin superfamily. We have found from Escherichia coli expression studies that the NH2-terminal 21 residues of oryzacystatin are not essential for its papain-inhibitory activity, and that the conserved pentapeptide region may be indispensable [Abe, K., Emori, Y., Kondo, H., Arai, S., & Suzuki, K. (1988) J. Biol. Chem. 263, 7655-7659]. Here we present more detailed data based on quantitative analyses of the inhibitory activities of NH2- and COOH-terminally truncated oryzacystatin and site-directed mutants at the Gln-Val-Val-Ala-Gly region. The data indicate the following results. (1) The truncated mutants lacking the NH2-terminal 21 residues or the COOH-terminal 11 residues exhibit potent papain-inhibitory activity equivalent to the activity of wild oryzacystatin. (2) However, neither the mutant lacking the NH2-terminal 38 residues nor that lacking the COOH-terminal 35 residues is completely able to inhibit papain. (3) Site-directed mutants at the Gln residue of the Gln-Val-Val-Ala-Gly region have drastically reduced papain-inhibitory activities: the Gln----Pro mutant is completely inactive and the Gln----Leu mutant has an approximately 150 times higher Ki value than wild-type oryzacystatin.(ABSTRACT TRUNCATED AT 250 WORDS)

Amino Acid Sequence↗
PubMed1988

The NH2-terminal 21 amino acid residues are not essential for the papain-inhibitory activity of oryzacystatin, a member of the cystatin superfamily. Expression of oryzacystatin cDNA and its truncated fragments in Escherichia coli.

Oryzacystatin, a proteinaceous cysteine proteinase inhibitor (cystatin) in rice, is comprised of 102 residues (Met1-Ala102) (Abe, K., Emori, Y., Kondo, H., Suzuki, K., and Arai, S. (1987) J. Biol. Chem. 262, 16793-16797). We constructed an expression plasmid containing a full length oryzacystatin cDNA at the multi-cloning site of pUC18 and produced a lacZ'-oryzacystatin fusion protein in Escherichia coli. The partially purified expressed protein efficiently inhibits papain activity assayed using N-benzoyl-DL-arginine-2-naphthylamide as a substrate. We also constructed expression plasmids lacking the 5'- and 3'-regions of cDNAs that encode NH2- and COOH-terminally truncated oryzacystatins. An N-truncated oryzacystatin lacking Gly5 and retaining Gln53-Val54-Val55-Ala56-Gly57 inhibited papain as efficiently as the full length oryzacystatin, although both Gly5 and Gln53-Gly57 (oryzacystatin numbering) are conserved among members of most cystatin superfamilies. However, another N-truncated oryzacystatin lacking the NH2-terminal 38 residues was almost completely inactive. On the other hand, a COOH-terminally truncated oryzacystatin lacking the COOH-terminal 11 residues possesses potent papain-inhibitory activity, whereas another COOH-terminally truncated oryzacystatin lacking 35 residues shows much less inhibitory activity, although it retains the two well conserved features Gly5 and Gln53-Gly57. These results indicate that the NH2-terminal 21 residues containing Gly5 and the COOH-terminal 11 residues are not essential, suggesting that a portion of the polypeptide segment containing Gln53-Gly57 is necessary for oryzacystatin to elicite its papain-inhibitory activity efficiently.

Amino Acid Sequence↗
PubMed1977

Characterization of two species of Fc fragments obtained from rat IgG2a by prolonged papain digestion.

Prolonged papain digestion of rat IgG2a produced two molecular species of Fc fragments, termed Fc(I) and Fc(II). Studies by gel filtration chromatography and polyacrylamide gel electrophoresis in SDS/urea indicated that the two subunit polypeptide chains in each Fc preparation were associated by non-covalent bonds only. By analytical ultracentrifugation Fc(I) was found to have a m.w. of 47,100 and a sedimentation coefficient of 4.08S. Fc(II) had a m.w. of 39,800 and a sedimentation coefficient of 3.83S. The m.w. for the subunit chains of Fc(I) and Fc(II) were 25,300 and 20,300, respectively, as determined by analytical ultracentrifugation under dissociating conditions. Calculation of the frictional coefficient ratios indicated that both Fc fragments possessed compact globular structures. The difference in size between these two Fc fragments probably was due to a loss of some carboxy-terminal residues in Fc(II). Both Fc fragments possessed nearly identical amino-terminal amino acid sequences. Papain cleavage occurred primarily between residues 233/234 and 234/235. The carbohydrate compositions of the two species of Fc fragments were similar. It was concluded that under acid and reducing conditions papain cleavage of rat IgG2a occurred to the carboxy-terminal side of the hinge region. Prolonged papain digestion led to secondary attack in the carboxy-terminal end of the CGAMMA3 domain at an unidentified site, or sites, producing a stable second species of Fc fragments.

Amino Acids↗
PubMed1977

On the enhanced catalytic activity of papain towards amide substrates.

According to the scanty literature data papain (EC. 3.4.4.10) reacts with ester and corresponding amide substrates at a similar rate (Glazer, Smith, 1971) despite a considerable difference in the reactivities of the ester and amide bonds. An explanation for the similar rates may be an increased acylation rate of amides relative to that of esters owing to hydrogen bond formation between the amide group of an amide substrate and Asp-158 carbonyl oxygen as it is apparent from the three-dimensional structure of papain. This possibility was confirmed by comparing the second-order rate constants of acylation of papain with the ester and amide derivatives of N-benzoylglycine and O-benzoylglycolic acid. The rate enhancement with amides is not an equally important factor with all substrates of papain: the amides of N-acyl-L-phenylalanylglycine are hydrolyzed at a considerably lower rate than the corresponding esters. It is concluded from the above data that the binding mode is somewhat different with various substrates.

Amides↗
PubMed1995

[Observations on antibody determination and differentiation with papain test erythrocytes using the gel centrifugation technique (ID-Microtyping System)].

BACKGROUND: The gel centrifugation system (ID Microtyping System, Fa. Diamed, Bensheim, FRG) is one of several new methods, which has become commercially available within the last few years for the detection of antibodies against red blood cell antigens. MATERIALS AND METHODS: During 1 year we used the gel centrifugation method for antibody screening in our routine laboratory by performing 3 tests each time: 1. NaCl card (room temperature) with untreated red cells; 2. NaCl card (37 degrees C) with papain-treated red cells, and 3. Liss-Coombs card (37 degrees C) with untreated red cells. RESULTS: The two-stage papain test revealed some interesting phenomena: 1. In some cases the sensitivity of the papain gel test is higher than that of all other methods tested in this study, namely in the gel centrifugation technique and in the tube centrifugation technique. 2. There are reactions which seem to be directed against patients' own antigens (in the Rhesus or Kidd system), but there are no positive direct antiglobulin test and no clinical signs of hemolysis. 3. Some sera show reaction patterns which seem to have a distinct specificity, but they cannot be assigned to any of the antigens in the manufacturer's antigenogram. CONCLUSIONS: Before a general recommendation for antibody screening with the two-stage papain test in the gel centrifugation method can be given, further investigations about the clinical value of those antibodies which are detectable only by this technique are necessary. For antibody identification further declarations in the work sheet of the panel would be desirable.

Adult↗
PubMed1998

Apoptosis-like changes in the lungs induced by cyclophosphamide and papain. I. An ultrastructural study.

An ultrastructural study was made to analyze the structural and cellular features of the pulmonary lesions produced in Wistar rats by the administration of cyclophosphamide (CP) and/or papain (P). Combined administration of cyclophosphamide and papain caused severe damage to lung tissue including necrosis, particularly to alveolar epithelial and endothelial cells. Some of the damaged type II cells showed nuclear and cytoplasmic features that are considered indicative of apoptosis. Apoptosis-like changes were also observed in endothelial and mesenchymal cells in the interstitium of interalveolar septa. Phagocytosis of apoptotic bodies by macrophages was found too. Apoptosis-like changes were not revealed in those areas of lung tissue where fibroplasia processes prevailed. Nor were they observed in the animals receiving papain only. Occasionally apoptosis-like changes were found in type II cells and in endothelial cells in rats given cyclophosphamide only. The results obtained also suggest the possibility of active participation of type II alveolar epithelial cells in the fibroplasia process in the course of lung rebuilding in acute lung tissue damage induced with simultaneous administration of cyclophosphamide and papain.

Animals↗
PubMed1993

Methyl Jasmonate Induces Papain Inhibitor(s) in Tomato Leaves.

Leaves of 18- to 24-d-old tomato (Lycopersicon esculentum) plants exposed to gaseous methyl jasmonate (MJ) for 24 h at 30[deg]C in continuous light contained high levels of soluble protein that inhibited papain. Chromatographic analysis demonstrated that the active protein had a molecular mass of 80 to 90 kD. Induction of papain inhibitor was directly related to the concentration of air-borne MJ up to a maximum of 0.1 [mu]L MJ per treatment and depended on the duration of exposure up to 18 h. Inhibitor activity in plants treated for less than 18 h increased with time after treatment. Levels remained constant for up to 4 d after treatment, after which time activity decreased. The youngest leaf, leaf 5, consistently lost activity at a faster rate than older, lower leaves. Inhibitor concentration in all leaves was reduced to minimum levels by 11 d after MJ treatment, but did not return to control levels. Treatment with MJ in the dark did induce inhibitor activity, but at a significantly lower rate. Polyclonal antibodies raised to purified potato tuber skin cysteine proteinase inhibitors (CPI) cross-reacted with the tomato inhibitor, suggesting that the tomato papain inhibitor and the potato CPI are closely related. No papain inhibitor activity was observed in extracts from wounded tomato leaves, nor was there any immunoreactivity with antibodies raised to potato tuber skin CPI.

Journal Article↗
PubMed2004

The ribbon of hydrogen bonds in globular proteins. IV. The example of the papain family.

A study of the role of the hydrogen-bonding side chains in the ribbon of hydrogen bonds in globular proteins, using the papain family as an example, suggests that these side chains may be divided into three categories depending on their position in the molecule. In the first category, they form part of the local ribbon, in the second they form part of the ribbon at a site remote along the main chain, and in the third they play no role in the formation of the ribbon. The second case is particularly interesting because it provides a natural mechanism for the formation of the tertiary structure of the globular proteins. The results suggest that the robustness of the globular proteins towards mutations arises from the fact that many mutations that involve hydrogen-bonding side chains either leave the hydrogen bonding of the ribbon essentially unchanged or their hydrogen bonding plays no part in the formation of the ribbon in the first place. The results show that it is possible to obtain the ribbon of hydrogen bonds for a family of proteins whose data set's are of intermediate quality by studying the ribbons of several members of such a family and then taking an average over the different partial ribbons to create a standard ribbon of hydrogen bonds for the family as a whole. This method is used here to derive the standard ribbon for the papain family with papain itself, actinidin, and human liver cathepsin B as the representatives of the family. All three members of the family fit the standard ribbon with an accuracy of 85-91%. This result opens up the use of this technique for the study of a large number of globular proteins whose recorded data sets are of intermediate quality.

Cathepsin B↗
PubMed2007

Cysteine-specific, covalent anchoring of transition organometallic complexes to the protein papain from Carica papaya.

Site-directed and covalent introduction of various transition metal-organic entities to the active site of the cysteine endoproteinase, papain, was achieved by treatment of this enzyme with a series of organometallic maleimide derivatives specially designed for the purpose. Kinetic studies made it clear that time-dependent irreversible inactivation of papain occurred in the presence of these organometallic maleimides as a result of Michael addition of the sulfhydryl of Cys25. The rate and mechanism of inactivation were highly dependent on the structure of the organometallic entity attached to the maleimide group. Combined ESI-MS and IR analysis indicated that all the resulting papain adducts contained one organometallic moiety per protein molecule. This confirmed that chemospecific introduction of the metal complexes was indeed achieved. Thus, three novel reagents for heavy-atom derivatization of protein crystals, which include ruthenium, rhenium and tungsten, are now available for the introduction of electron-dense scatterers for phasing of X-ray crystallographic data.

Carica↗
PubMed1992

LC20 and kinetics of gizzard myosin subfragment-1: digestion with papain vs. S. aureus protease.

Previous reports have shown that papain-digested gizzard subfragment-1 (PAP-S1) has a cleaved regulatory light chain (LC20), and Vmax similar to phosphorylated heavy meromyosin (HMM) (Greene et al., Biochemistry 22:530-535, 1983; Sellers et al., J. Biol. Chem. 257:13880-13883, 1982; Umemoto et al., J. Biol. Chem. 264:1431-1436, 1989], while S. aureus protease-digested S-1 (SAP-S1) has intact LC20, but Vmax closer to that of unphosphorylated HMM [Ikebe and Hartshorne, 1985]. To determine whether intact LC20 inhibits ATPase activity for subfragment-1 (S1), we compared the kinetic properties and structures of unphosphorylated PAP-S1 and SAP-S1. SDS-PAGE showed that SAP-S1 had 68 and 24 KDa heavy chain and 20 and 17 KDa light chain components. PAP-S1 (15 minutes digestion at 20 degrees C) also had 68 and 17 KDa bands, but the single 24 KDa band (24HC) was replaced by a group of 22-24 KDa fragments and LC20 was cleaved to a 16 KDa fragment. At 13 mM ionic strength, both PAP-S1 and SAP-S1 had Vmax similar to phosphorylated HMM (1.1-1.5 s-1). SAP-S1 had the same KATPase as phosphorylated HMM (38 microM actin), but KATPase for PAP-S1 was 3-fold stronger (11 microM actin). Subsequent digestion of SAP-S1 with papain did not significantly change Vmax, but as LC20 and 24HC were cleaved, both KATPase and Kbinding strengthened 3- to 5-fold. Thus, intact LC20 did not inhibit, and cleavage of LC20 did not increase Vmax for S1. Rather, papain cleavage of LC20 and 24HC was associated with strengthened actin binding.

Actins↗
PubMed1990

The refined 2.4 A X-ray crystal structure of recombinant human stefin B in complex with the cysteine proteinase papain: a novel type of proteinase inhibitor interaction.

A stoichiometric complex of human stefin B and carboxymethylated papain has been crystallized in a trigonal crystal form. Data to 2.37 A resolution were collected using the area detector diffractometer FAST. The crystal structure of the complex has been solved by Patterson search techniques using papain as search model. Starting from the structure of chicken cystatin, the stefin structure was elucidated through cycles of model building and crystallographic refinement. The current crystallographic R factor is 0.19. Like cystatin, the stefin molecule consists of a five stranded beta-sheet wrapped around a five turn alpha-helix, but with an additional carboxy terminal strand running along the convex side of the sheet. Topological equivalence of stefin and cystatin reveal the previous sequence alignment to be incorrect in part, through deletion of the intermediate helix. The conserved residues form a tripartite wedge, which slots into the papain active site as proposed through consideration of the tertiary structures of the individual components (Bode et al., 1988). The main interactions are provided by the amino terminal 'trunk' (occupying the 'unprimed' subsites of the enzyme), and by the first hairpin loop, containing the highly conserved QVVAG sequence, with minor contributions from the second hairpin loop. The carboxyl terminus of stefin provides an additional interaction region with respect to cystatin. The interaction is dominated by hydrophobic contacts. Inhibition by the cysteine proteinase inhibitors is fundamentally different to that observed for the serine proteinase inhibitors.

Amino Acid Sequence↗
PubMed2006

Physicochemical characterization of papain entrapped in ionotropically cross-linked kappa-carrageenan gel beads for stability improvement using Doehlert shell design.

This work examines the influence of various process parameters on papain entrapped in cross-linked kappa-carrageenan beads for improvement of its stability. A Doehlert shell design (DSD) was employed to investigate the effect of three process variables, namely kappa-carrageenan concentration, KCl concentration, and hardening time, on the entrapment, time required for 50% enzyme release (T50), time required for 90% enzyme release (T90), and particle size. The beads were prepared by dropping the kappa-carrageenan containing papain into a magnetically stirred KCl solution. Topographical characterization was carried out by scanning electron microscopy and entrapment was confirmed by Fourier transform infrared spectroscopy and differential scanning calorimetry. Stability testing was carried out according to the International Conference on Harmonization (ICH) guidelines for zone III and IV. A polymeric matrix was prepared with kappa-carrageenan (3.5% w/v) and potassium chloride (0.5 M) using the ionotropic gelation method, with a hardening time of 20 min. Beads characterized by a spherical disc shape with a collapsed center, an absence of aggregates, an entrapment of 82.75%, a T90 value of 55.36 min, and a composite index of 88.55 were produced. The shelf-life of the enzyme-loaded beads was found to increase to 3.63 years compared with 1.01 years for the conventional formulation. It can be inferred that the proposed methodology can be used to prepare papain-loaded kappa-carrageenan beads for stability improvement.

Algorithms↗
PubMed1996

A theoretical study of the active sites of papain and S195C rat trypsin: implications for the low reactivity of mutant serine proteinases.

The serine and cysteine proteinases represent two important classes of enzymes that use a catalytic triad to hydrolyze peptides and esters. The active site of the serine proteinases consists of three key residues, Asp...His...Ser. The hydroxyl group of serine functions as a nucleophile and the imidazole ring of histidine functions as a general acid/general base during catalysis. Similarly, the active site of the cysteine proteinases also involves three key residues: Asn, His, and Cys. The active site of the cysteine proteinases is generally believed to exist as a zwitterion (Asn...His+...Cys-) with the thiolate anion of the cysteine functioning as a nucleophile during the initial stages of catalysis. Curiously, the mutant serine proteinases, thiol subtilisin and thiol trypsin, which have the hybrid Asp...His...Cys triad, are almost catalytically inert. In this study, ab initio Hartree-Fock calculations have been performed on the active sites of papain and the mutant serine proteinase S195C rat trypsin. These calculations predict that the active site of papain exists predominately as a zwitterion (Cys-...His+...Asn). However, similar calculations on S195C rat trypsin demonstrate that the thiol mutant is unable to form a reactive thiolate anion prior to catalysis. Furthermore, structural comparisons between native papain and S195C rat trypsin have demonstrated that the spatial juxtapositions of the triad residues have been inverted in the serine and cysteine proteinases and, on this basis, I argue that it is impossible to convert a serine proteinase to a cysteine proteinase by site-directed mutagenesis.

Animals↗
PubMed2002

Overlapping binding sites for trypsin and papain on a Kunitz-type proteinase inhibitor from Prosopis juliflora.

Proteinase inhibitors are among the most promising candidates for expression by transgenic plants and consequent protection against insect predation. However, some insects can respond to the threat of the proteinase inhibitor by the production of enzymes insensitive to inhibition. Inhibitors combining more than one favorable activity are therefore strongly favored. Recently, a known small Kunitz trypsin inhibitor from Prosopis juliflora (PTPKI) has been shown to possess unexpected potent cysteine proteinase inhibitory activity. Here we show, by enzyme assay and gel filtration, that, unlike other Kunitz inhibitors with dual activities, this inhibitor is incapable of simultaneous inhibition of trypsin and papain. These data are most readily interpreted by proposing overlapping binding sites for the two enzymes. Molecular modeling and docking experiments favor an interaction mode in which the same inhibitor loop that interacts in a canonical fashion with trypsin can also bind into the papain catalytic site cleft. Unusual residue substitutions at the proposed interface can explain the relative rarity of twin trypsin/papain inhibition. Other changes seem responsible for the relative low affinity of PTPKI for trypsin. The predicted coincidence of trypsin and papain binding sites, once confirmed, would facilitate the search, by phage display for example, for mutants highly active against both proteinases.

Amino Acid Sequence↗
PubMed1997

Monitoring papain digestion of a monoclonal antibody by electrospray ionization mass spectrometry.

Electrospray ionization mass spectrometry (ESI-MS) has been used to examine the Fab, F(ab')2 and deglycosylated Fc fragments obtained from the murine IgG1 B72.3 monoclonal antibody (MAb) by digestion with the sulfhydryl protease papain, in an attempt to determine the sites of cleavage and thus to clarify the mode of action of this enzyme on MAbs. ESI analysis of the Fab and F(ab')2 subunits indicated that the predominant site of papain cleavage occurred at C221 of the B72.3 MAb heavy chain. Reduction of the intra- and interchain disulfide bridges of these fragments by 1,4-dithiothreitol and subsequent electrospray analysis showed a loss of C221 from the C-terminal end of the Fd subunit. ESI analysis of the cleaved Fab fragment indicated that there was an apparent loss of amino acid residues from this fragment. Edman sequencing of the cleaved subunit revealed an intact light chain and the loss of QVQ from the N-terminal of the Fd subunit. Reduction of this subunit gave a Fd fragment approximately 32 Da greater than the predicted mass, which we have attributed to oxidation of the heavy chain methionine residues (M81 and M136). Removal of the carbohydrate portion from the Fc fragment by N-glycosidase F indicated that papain cleavage had occurred at C223 of the B72.3 MAb heavy chain. In addition, it was observed that the C-terminal lysine residue (K438) was absent from the deglycosylated Fc fragment, presumably due to carboxypeptidase B activity that occurs during the in vivo production of the B72.3 MAb in murine hosts. These data clearly illustrate the power of ESI-MS for determining small changes in mass on large proteins as well as providing a rapid and sensitive technique for assessing MAb fragments prior to use in radioimaging or radiotherapy.

Amino Acid Sequence↗
PubMed2001

A cystatin-based affinity procedure for the isolation and analysis of papain-like cysteine proteinases from tissue extracts.

Cysteine-proteinases (CP) of the papain family can be affinity-adsorbed by egg white cystatin C coupled to Sepharose 4B, thus allowing their selective isolation from either tissue or cultured cell extracts as well as biolological fluids and culture media. CP complexed by immobilized cystatin are further analyzed by means of SDS-PAGE and Western blot followed by serial or parallel immunological detection. The single-step affinity adsorption of papain-like enzymes has the advantage, over immunoprecipitation techniques, of yielding the simultaneous and comprehensive picture of most CP, as both precursor and mature forms, in a given sample. Moreover, cell extraction in the presence of immobilized cystatin ensures a fast complexation of CP, avoiding artifacts, due to conversion, degradation, and, eventually, subtraction of constitutive enzymes from the sample because of their interactions with endogenous inhibitors. This will provide a pattern that might reflect more closely the real CP levels in intact cells. The method may be useful in the field of biochemistry, cell biology, and, possibly, clinical chemistry to perform rapid analyses of papain-like enzymes and to monitor changes in both cellular and extracellular CP profiles along with different physiopathological conditions.

Adsorption↗