Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.4.22.32 (bromelain)
 1,025 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Agglutinability of red blood cells against anti-D increased remarkably when the cells were treated with proteolytic enzymes, such as bromelain, chymotrypsin, ficin, papain, pronase and trypsin. When stroma prepared from normal red blood cells was treated with any of proteolytic enzymes, however, Rh-Hr blood type activities were completely abolished. The similar results were obtained from stroma solubilized with detergents which was treated with enzymes after being prepared. Of all the enzymes, ficin acted more slowly than the others did. Neuraminidase or phospholipase A2 had no effect on Rh-Hr activities at all. SDS-polyacrylamide gel electrophoretic pattern of stroma prepared from bromelain, ficin and pronase-treated red blood cells were quite different from that of normal stroma.
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PMID:Rh0(D) activity of red blood cells and stroma treated with proteolytic enzymes. 643 38

Development of mitochondrial and microsomal glycerophosphate acyltransferase in the fetal guinea pig lung was investigated. Mitochondrial and microsomal enzyme activity gradually increased from 45 days to 55 days of gestation. The specific activity in the microsomal fraction (8.2 nmol/min per mg protein) then declined until term, but increased again in the 24-h newborn from 2.5 to 6.1 nmol/min per mg protein. Glycerophosphate acyltransferase activity in the mitochondrial fraction declined after 55 days (3.5 nmol/min per mg) to a minimum level at 60 days (1.8 nmol/min per mg), but increased again in the 24-h newborn (4.0 nmol/min per mg). The specific activity of both mitochondrial and microsomal enzyme declined after 24 h after birth until adult levels were attained. Glycerophosphate acyltransferase activity in mitochondria and microsomes from adult lung was 0.8 and 2.0 nmol/min per mg, respectively. Microsomal enzyme activity was consistently inhibited (over 95%) throughout gestation and adulthood by exposure to any one of several proteinases: trypsin, chymotrypsin, papain, bromelain, pronase and nagarse. Although mitochondrial enzyme activity was also inhibited by these proteinases, there was a continuous increase in proteinase-resistant glycerophosphate acyltransferase activity between 45 days of gestation and term. In contrast, adult mitochondrial enzyme activity was stimulated by all the proteinases studied. These results suggest that early in gestation, glycerophosphate acyltransferase lies more exposed on the cytoplasmic side of the mitochondrial outer membrane and as gestation progresses it becomes embedded into the phospholipid bilayer.
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PMID:Development of glycerophosphate acyltransferase in guinea pig lung mitochondria and microsomes. 643 51

Ovalbumin is partially homologous in sequence with the proteinase inhibitors alpha 1-proteinase inhibitor and anti-thrombin III. The region of sequence in ovalbumin which corresponds to the reactive sites of these proteinase inhibitors is susceptible to attack by subtilisin, elastase, thermolysin, bromelain, and Bacillus cereus protease. The esterase activity of elastase is not inhibited by ovalbumin, but ovalbumin is efficiently cleaved by elastase. In contrast with these proteases, trypsin does not cleave ovalbumin.
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PMID:Ovalbumin is an elastase substrate. 656 26

Activation of bovine plasma prekallikrein was investigated with several proteinases. Highly purified bovine plasma prekallikrein was rapidly activated to kallikrein [EC 3.4.21.8] by bovine activated Hageman factor, trypsin [EC 3.4.21.4] and Pronase P (proteinases from Streptomyces griseus) and more gradually by papain [EC 3.4.22.2] and ficin [EC 3.4.22.3]. Activation of prekallikrein was also observed with bovine plasmin [EC 3.4.21.7], but not with bovine clotting factors Xa (Stuart factor) [EC 3.4.21.6] and IXa (Christmas factor) or thrombin [EC 3.4.21.5]. Urokinase [EC 3.4.99.26], Reptilase, collagenase [EC 3.4.24.3], elastase [EC 3.4.21.11], alpha-chymotrypsin [EC 3.4.21.1], Nagarse [EC 3.4.21.14], and stem bromelain [EC 3.4.22 4] did not convert prekallikrein to kallikrein. Plasma kallikrein activated to Hageman factor released kinin rapidly from bovine high molecular weight (HMW) kininogen. However, from bovine low molecular weight (LMW) kininogen, liberation of kinin was extremely slow. The kallikrein activity was inhibited by soybean trypsin inhibitor (SBTI), Trasylol, diisopropylfluorophosphate (DFP), and N-alpha-tosyl-L-lysine chloromethylketone (TLCK), but not by egg-white trypsin inhibitor (EWTI), lima bean trypsin inhibitor (LBTI), heparin or hexadimethrine bromide (Polybrene). The kallikrein formed an enzyme-inhibitor complex with SBTI and Trasylol, but not with LBTI. Prekallikrein did not react with SBTI. Prekallikrein consists of a single polypeptide chain of molecular weight about 90,000, as estimated by sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis. Activation of prekallikrein by Hageman factor was found to involve cleavage of the single peptide bond on the disulfide-bridged polypeptide chain, and no change of molecular weight was observed during the activation. The peptide bond cleaved in prekallikrein by the activation was an Arg-X peptide bond on a disulfide-bridged polypeptide chain.
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PMID:Studies on prekallikrein of bovine plasma. II. Activation of prekallikrein with proteinases and properties of kallikrein activated by bovine Hageman factor. 676 24

The brush border of the enterocytes of the rat was isolated by the method of differential centrifugation with CaCl2 according to Schmitz. This material was solubilized with papain, trypsin and Triton X-100. The greatest amount of membrane enzymes was released to the supernatant (105 000 X g) with the use of Triton X-100. The tritonized supernatant was treated in the next step by papain, bromelain, ficin and trypsin (individually or in combinations). After simultaneous proteolysis with papain and bromelain a partial separation of the aminopeptidase from the endopeptidase by Sephadex G-200 chromatography was observed. These two enzyme activities were distinctly separated by isoelectric focusing at pH 4--6. Two enzymatically active bands (RF 0.13 and 0.24) in the aminopeptidase fraction and one single active band (RF 0.16) in the endopeptidase fraction using polyacrylamide gel electrophoresis were found. Co-migrating proteins to all of these activities were detected. Endopeptidase activity splits 3-carboxypropionyltrialanin-4-nitroanilide (SucAla3NAp) in the position P2-P1. Liberated aminoacyl-NAP may be further split to generate chromogenic 4-nitroaniline through aminopeptidase activity. Endopeptidase of the brush border of the rat enterocytes is characterized by the following properties: 1) molecular mass 130000 +/- 15 000 dalton; 2) Km value (substrate: SucAla3NAp) 1.1 X 10(-3) M; 3) pI 5.23; 4) ph optimum 8.5; 5) 50% activity remains after 15 min of preincubation at 50 degrees C; 6) activity is strongly inhibited by EDTA, p-chloromercuribenzoate, Mn2 and Co2.
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PMID:Endopeptidase of the brush border membrane of rat enterocyte. Separation from aminopeptidase and partial characterization. 700 58

Polymorphonuclear neutrophils (PMN) can be primed for enhanced release of reactive oxygen species (ROS) by exposure to cytokines and biological response modifiers. ROS are considered to possess tumoricidal activity. The polyenzyme preparation Wobenzym (WE) contains pancreatin, papain, bromelain trypsin and chymotrypsin and is used in adjuvant tumor therapy. We investigated killing of WE-exposed PMN against tumor cells and analyzed WE influence on ROS production in a chemiluminescence assay in PMN in vitro and in vivo. Depending on dose WE stimulates the cytotoxic capacity of PMN in vitro against tumor cells (50 micrograms/ml:p < 0.01). Exposure of PMN to Wobenzym caused a time-dependent significant (p < 0.02) increase in release of ROS. Similarly, oral administration of Wobenzym to healthy volunteers (n = 28) resulted in significant increases (p < 0.01) in ROS production, depending on dose (peak with 20 tablets) and time (peak 4 hours after Wobenzym administration). In contrast, ROS production was not elevated in the PMN of healthy volunteers receiving placebo (n = 8) or no treatment (n = 16). These findings point to an immunomodulatory capacity of WE in adjuvant tumor therapy.
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PMID:Stimulation of reactive oxygen species production and cytotoxicity in human neutrophils in vitro and after oral administration of a polyenzyme preparation. 766 74

Pharmaceutical preparations containing mixtures of various proteolytic and nonproteolytic enzymes have been suggested for use in the treatment of malignant diseases. However, the mode of action of such preparations was not clear. We have shown before that intact bromelain, papain or amylase, which are components of a commercial polyenzyme preparation, induce cytokine production in peripheral blood mononuclear cells in vitro. IFN-alpha and IFN-gamma which had no effect alone, synergistically increased TNF production when applied together with the enzymes. Here we show that trypsin alone had only a small inducing effect. The tryptic but not the autolytic fragments of papain and bromelain have a higher (10- to 40-fold) inducing capacity for TNF production than the untreated enzyme. Additionally we demonstrate that after ingestion of milligram doses of the polyenzyme preparation (as recommended for clinical use), PBMNC of healthy donors acquire the ability to produce TNF-alpha, IL-1 beta and IL-6 when incubated ex vivo with IFN-gamma. Our results indicate that the biological effects observed after oral administration of polyenzyme preparations are related to their ability to induce cytokine production. This may explain the antitumor effects of such enzymes. Our results also suggest that polyenzyme preparations may have a stronger immunomodulary effect when used in combination with IFN-gamma.
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PMID:Cytokine synthesis in human peripheral blood mononuclear cells after oral administration of polyenzyme preparations. 769 16

Pigeon-pea seed extracts have been analyzed for the protease inhibitors using a new, sensitive and simple method for visualization of electrophoretically separated protease inhibitors. The visualization involves equilibrating the gel successively in the protease assay buffer, protease solution, rinsing the gel in protease assay buffer, and exposing it to an exposed, undeveloped X-ray film. Gelatin on the film in places corresponding to the inhibitor bands remains unhydrolyzed. By this method the pigeon-pea seed extract was found to contain nine trypsin and at least seven chymotrypsin inhibitors but no papain or bromelain inhibitors.
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PMID:Detection of electrophoretically separated protease inhibitors using X-ray film. 806 16

Lymphocytes constitute a critical component of host defenses against cryptococcosis. Previously, we demonstrated that human lymphocytes cultured with interleukin-2 formed conjugates with, and directly inhibited the growth of, Cryptococcus neoformans. Here, we explore the anticryptococcal activity of freshly isolated, highly purified populations of human peripheral blood lymphocytes. Lymphocytes were incubated with encapsulated C. neoformans for 24 h, after which the lymphocytes were lysed, dilutions and spread plates were made, and CFU were counted. Fungistasis was determined by comparing growth in wells with and without lymphocytes. Nylon wool-nonadherent peripheral blood mononuclear cells (NWNA PBMC) were highly fungistatic, even if either T cells or natural killer (NK) cells were depleted by panning. A mixed population of T cells and NK cells, obtained by rosetting NWNA PBMC with sheep erythrocytes, completely inhibited cryptococcal growth, whereas the nonrosetting cells had little fungistatic activity. CD4+, CD8+, and CD16/56+ lymphocytes, isolated by positive immunoselection, had potent growth-inhibitory activity. In contrast, purified B cells had no activity. Fungistasis was seen even in the absence of opsonins. Antifungal activity was markedly diminished when surface receptors on NWNA PBMC were cleaved by treatment with trypsin or bromelain. Supernatants from stimulated lymphocytes or concentrated lymphocyte sonicates were not active. Lymphocyte-mediated fungistasis was seen with two different strains of C. neoformans. CD4+, CD8+, and CD16/56+ lymphocytes formed conjugates with C. neoformans, as observed under Nomarski differential interference contrast microscopy and videomicroscopy. These data demonstrate that freshly isolated peripheral blood T cells and NK cells have the capacity to bind and directly inhibit the growth of C. neoformans.
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PMID:Direct activity of human T lymphocytes and natural killer cells against Cryptococcus neoformans. 826 27

A fully active form of hydroxylamine oxidoreductase from Nitrosomonas has been purified with high recovery and shown by reverse-phase high performance liquid chromatography and N-terminal analysis to contain only a 63-kDa subunit and to lack the 11-kDa protein previously thought to be a second subunit. Based on the previously published values of molecular weight in solution, hydroxylamine oxidoreductase probably has an alpha 2 or alpha 3 oligomeric structure. The enzyme was digested separately with trypsin and chymotrypsin and peptides which contained covalently bound heme were separated by high performance liquid chromatography and their amino acid sequences determined. A total of seven heme-containing peptides of unique amino acid sequence were obtained. Six of these heme-containing peptides clearly contained a single c-heme with optical properties indistinguishable from the tryptic heme-containing peptide from horse heart cytochrome c. No noncovalently bound heme was observed. One of the seven heme-containing peptides (T7) was unusual in that it released 2 amino acid residues after each cycle of the Edman degradation due to a nondisulfide cross-link and exhibited a Soret band that was broadened in both the ferric form at neutral pH and the pyridine ferrohemochrome. Subdigestion of peptide T7 with nonspecific proteases (Pronase, bromelain, or pepsin) resulted in the isolation of two smaller heme-containing peptides of unique sequences. One of these was spectrally identical to the other c-heme containing peptides, whereas the second was still apparently cross-linked, again releasing 2 amino acid residues after each Edman cycle. This second peptide possessed a heme-like chromophore with absorption bands (Soret, alpha and beta) red-shifted about 6 nm relative to the spectrum of c-heme-containing peptides. Thus, hydroxylamine oxidoreductase contains a total of eight covalently bound hemes per subunit, seven of which are c-hemes. The eighth, which is attached to a cross-linked peptide, is probably the unusual P460 heme which is unique to hydroxylamine oxidoreductase and thought to be at the active site.
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PMID:Hydroxylamine oxidoreductase from Nitrosomonas europaea is a multimer of an octa-heme subunit. 832 41


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