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)

gamma-Glutamyltransferase was solubilized from human hepatoma tissues by bromelain treatment, and some of its properties were compared with those of the normal adult liver enzyme. An electrophoretic study showed a slightly different mobility between the two enzymes before and after neuraminidase treatment. The hepatoma tissue enzyme was distinguished from the normal liver enzyme by decreased affinity to Con A. However, the enzymes from the two sources were found to be very similar or identical with respect to molecular weight, Michaelis constant, pH optimum, thermostability, effect of various L-amino acids as acceptors, behavior to divalent cations or ethylenediaminetetraacetate, inhibition by urea or sodium dodecyl sulfate, and immunological properties. These results suggest that the hepatoma tissue gamma-glutamyltransferase is largely due to altered glycosylation of this glycoprotein in hepatoma cells.
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PMID:gamma-Glutamyltransferase from human hepatoma tissue in comparison with normal liver enzyme. 611 82

Influenza virus strans A/Scotland/74, A/Hong Kong/68, A/Port Chalmers/73 and the MRC-12 recombinant were tested with immune antiserum against actomyosin. As shown by electron microscopy, the serum aggregated virus particles, but only after bromelain treatment (without haemagglutinin and neuraminidase spikes). In rocket electrophoresis the serum gave positive precipitation reaction with all the strains tested, and with virus from various hosts (chick embryo, monkey kidney cell culture, mice after adaptation). There fore the host protein presumably is present in the influenza virus structure irrespective of the strain or the host in which the virus is grown.
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PMID:Attempts at detection of actomyosin associated with influenza virus. 611 22

Methods were developed for the purification of the surface, membrane-bound glycoproteins haemagglutinin and neuraminidase of influenza virus strain 3QB, in antigenically active forms. The methods employed in the purification included selective removal of the neuraminidase with the proteinase, bromelain, and subsequent disruption of the residual virus particle with the detergent Sarkosyl to release the haemagglutinin. Using techniques for proteolytic digestion of intact, native proteins an antigenically active peptide was isolated from the purified haemagglutinin, the surface glycoprotein against which the major antigenic response is directed. The amino acid composition of this peptide was determined. This was a 16-residue peptide with amino-terminal isoleucine and composition Ile1 Val1 Asx2 Thr1 Ser2 Glx2 Pro1 Gly3 Ala1 Leu1 Lys1.
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PMID:Purification of haemagglutinin and neuraminidase from influenza virus strain 3QB and isolation of a peptide from an antigenic region of haemagglutinin. 615 31

The antineuraminidase (AN) antibody response to vaccination of chickens with intact virus and different subunit preparations of the influenza virus strains A/Sing/1/57 (H2N2), A/Hong Kong/1/68 (H3N2) and A/Pt. Chalmers/1/73 (H3N2) was tested comparatively. Using a photometric method capable of analysing mixtures of AN antibodies against antigenically different N2 neuraminidases, it was concluded that vaccination with subunits produced by treatment with bromelain and Sarkosyl can yield AN antibody response against heterologous neuraminidase. By contrast, vaccination with intact and ether-treated virus gave AN antibody response against homologous neuraminidases. The conclusion was reached that the NA's of the strains A/Sing/1/57 and A/Pt. Chalmers/1/73 share antigenic determinants and that the NA of the strain A/Hong Kong/1/68 shares antigenic determinants with that of the strains A/Sing/1/57 and A/Pt. Chalmers/1/73.
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PMID:Antineuraminidase antibody response to vaccination of chickens with intact virus and different submit preparations of the influenza virus strains A/Sing/1/57 (H2N2), A/Hong Kong/1/68 (H3N2) and A/Port Chalmers/1/73 (H3N2). 615 75

The sensitivity of highly purified human fibroblast interferon and partially purified human leukocyte interferon to several proteolytic and glycolytic enzymes was determined with respect to antiviral activity, isoelectric point, molecular weight, and thermal stability. Leucine aminopeptidase altered the distribution of isoelectric points for both interferons but produced little change in molecular weights; this enzyme somewhat reduced the activity of only leukocyte interferon. Treatment of fibroblast interferon with carboxypeptidases A and B did not greatly decrease antiviral activity, but it did slightly reduce the molecular weight of the interferon and substantially altered the distribution of isoelectric point values; similar treatment of leukocyte interferon caused some loss in activity, especially of the 17,000-molecular-weight species. Both interferons were inactivated rapidly by treatment with the endoproteases trypsin, pepsin, bromelain, and subtilisin. Chymotrypsin shifted the isoelectric points of both interferons, but only leukocyte interferon was significantly inactivated. Treatment with neuraminidase and beta-galactosidase changed the isoelectric point distribution but did not affect the activity or thermal stability of either interferon; such a treatment reduced the molecular weight of fibroblast interferon and the size heterogeneity of leukocyte interferon. Treatment with neuraminidase and then leucine aminopeptidase greatly reduced the activity of both interferons, especially leukocyte interferon. The data indicate that biologically active forms of fibroblast and leukocyte interferons can be distinguished by their relative sensitivity to certain proteases.
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PMID:Enzymatic modifications of human fibroblast and leukocyte interferons. 616 Feb 60

Attachment of [35S]methionine-labelled mammalian type 3 reovirus to murine L cells and human HeLa cells was studied under equilibrium conditions. Cellular attachment sites could be completely saturated with 35S-labelled reovirus, indicating that specific attachment sites for reovirus are present on the surface of these cells. We calculated that L cells possess about 86000-105000 attachment sites per cell while HeLa cells possess about 126000-147000 sites per cell for type 3 reovirus. Unlabelled reovirus was highly efficient in competing for attachment by 35S-labelled reovirus to the saturable attachment sites of both L and HeLa cells, further indicating the specificity of the interaction. We also found that unlabelled reovirus competed equally well for both binding and internalization of 35S-labelled reovirus into murine L cells, suggesting that the L cell attachment site may serve as a virus entry site. Phospholipase digestion of L cells had no effect on subsequent reovirus attachment, while treatment of L cells with moderate concentrations of bromelain (but not trypsin, proteinase K or pronase) and Vibrio cholerae neuraminidase reproducibly decreased subsequent reovirus attachment. These results and those of others (Epstein et al., 1984, Virology 133, 46-55) suggest that mammalian reoviruses attach to specific cell surface receptors on at least two species of mammalian cells to initiate the infectious cycle.
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PMID:Saturable attachment sites for type 3 mammalian reovirus on murine L cells and human HeLa cells. 639 64

Human plasma alpha-cysteine proteinase inhibitor (alpha CPI) was purified by a two-stage method: affinity chromatography on S-carboxymethyl-papain-Sepharose, and high-resolution anion-exchange chromatography. The protein was obtained as a form of Mr about 64 000 and material of higher Mr (about 100 000). In sodium dodecyl sulphate/polyacrylamide-gel electrophoresis with reduction, both forms showed a major component of Mr 64 000. An antiserum was raised against alpha CPI, and 'rocket' immunoassays showed the mean concentration in sera from 19 individuals to be 35.9 mg/dl. Both low-Mr and high-Mr forms of alpha CPI were confirmed to be sialoglycoproteins by the decrease in electrophoretic mobility after treatment with neuraminidase. alpha CPI was shown immunologically to be distinct from antithrombin III and alpha 1-antichymotrypsin, two serine proteinase inhibitors from plasma with somewhat similar Mr values. alpha CPI was also distinct from cystatins A and B, the two intracellular low-Mr cysteine proteinase inhibitors from human liver. Complexes of alpha CPI with papain were detectable in immunoelectrophoresis, but dissociated to free enzyme and intact inhibitor in sodium dodecyl sulphate/polyacrylamide-gel electrophoresis. The stoichiometry of binding of papain was close to 1:1 for both low-Mr and high-Mr forms. alpha CPI was found to be a tight-binding inhibitor of papain and human cathepsins H and L (Ki 34 pM, 1.1 nM and 62 pM respectively). By contrast, inhibition of cathepsin B was much weaker, Ki being about 35 microM. Dipeptidyl peptidase I also was weakly inhibited. Digestion of alpha CPI with bromelain gave rise to an inhibitory fragment of Mr about 22 000, which was isolated.
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PMID:Human plasma alpha-cysteine proteinase inhibitor. Purification by affinity chromatography, characterization and isolation of an active fragment. 654 32

Mass determinations on highly purified influenza virus preparations were performed using the technique of scanning transmission electron microscopy. The masses of the three strains, X49, B/Singapore/222/79 and B/Hong Kong/8/73 were determined. The average value was 174 X 10(6) daltons with only small differences between the three strains. The mass of virus particles after removal of the protruding spike proteins, haemagglutinin and neuraminidase by bromelain treatment was determined to be 86 X 10(6) daltons. From the mass difference and the known molecular weight of the spike proteins the number of spikes was estimated to lie in the range 400 to 500.
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PMID:Characterization of three highly purified influenza virus strains by electron microscopy. 656 Dec 34

Arylamidase (E.C. 3.4.11.2) was solubilized from renal cancer tissues by bromelain treatment, and its properties were compared with those of normal kidney and placental enzymes after partial purification. Their column chromatograms on TEAE-cellulose revealed a slight, but constant difference in the negative charge, namely, in normal kidney, renal cancer tissue, and placental enzymes in increasing order. An electrophoretic study on polyacrylamide gel showed comparable results. On the other hand, when treated with neuraminidase prior to electrophoresis, the renal cancer tissue and kidney enzymes came to have an identical mobility, while the placental enzyme still had a faster mobility than the others. The renal cancer tissue arylamidase was not clearly distinguished from the kidney and placental enzymes with respect to molecular weight, Michaelis constant, pH optimum, heat stability, behavior to divalent cations or chelating agents, susceptibility to urea or amino acids, inhibition by sulfhydryl agents, and immunological properties. These results suggest that renal cancer tissue and kidney enzymes are similar glycoproteins, simply different in sialic acid content, and that these two enzymes are different from the placental enzyme in the structure of the peptide portion and/or carbohydrate portions other than sialic acid residues.
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PMID:Arylamidase from human renal cancer tissue in comparison with normal kidney and placental enzymes. 679 1

The hemagglutination (HA) and receptor destroying enzyme (RDE) activities of a newly isolated mouse enteric coronavirus (designated as DVIM) are described. DVIM agglutinates mouse or rat red blood cells (RBC) at 4 degrees C. At 37 degrees C the agglutination was rapidly reversed. The optimal pH for HA and for RDE activities using mouse red cells were shown to be 6.5 and 7.3 respectively. Hemagglutination by DVIM was not inhibited by pretreatment of RBCs with Vibrio cholerae filtrate or by pretreatment with Influenza-A neuraminidase. Therefore, the DVIM receptors on RBCs differ from the receptors of Influenza-A, and the RDE activity of DVIM acts specifically on this receptor. In addition, an analysis of the DVIM polypeptides showed that the virions contain five major, VP1 (M.W. 139,000), VP2 (68,000), VP3 (53,000), VP4 (38,000), VP5 (22,000) and two minor, VP1a (110,000), VP1b (100,000) polypeptides. VP1 and VP1b were digested by bromelain, suggesting that they constitute the surface glycoproteins.
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PMID:Hemagglutination and structural polypeptides of a new coronavirus associated with diarrhea in infant mice. 743 41


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