Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.2.1.17 (lysozyme)
 21,489 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A case of primary splenic angiosarcoma with involvement of two accessory spleens is presented. The tumor cells are immunoreactive for endothelial markers (CD 31, CD 34, factor VIII associated antigen) and express also histiocytic antigens (CD 68, lysozyme, Cat-hepsin D, alpha-1-antitrypsin, alpha-1-anti-chymotrypsin) as well as CD 8. This marker profile suggests that the presented angio-sarcoma originates from sinus cells with histiocytic and endothelial differentiation and may be regarded as the malignant variant of littoral cells angioma.
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PMID:[Littoral cell angiosarcoma of the spleen. Morphologic, immunohistochemical findings and consideration of histogenesis of a rare splenic tumor]. 943 77

Cationic proteins, such as lysozyme, ribonuclease A, and human IgG, impaired the detection of endotoxins with the Limulus amebocyte lysate assay (LAL assay) through formation of endotoxin-protein complexes, demonstrating pronounced masking of endotoxins. Methods, such as phenol extraction, dilution heating, and perchloric acid treatment failed to demask the endotoxins. Also, digestion with trypsin, chymotrypsin, or pronase recovered only 10 to 20% of the applied endotoxins. However, endotoxin recoveries up to 100% were obtained with proteinase K digestion of the samples prior to the LAL assay. This method was then applied to examine the impact of endotoxin masking on endotoxin removal from protein solutions by selective adsorption on membrane adsorbers. It was found that poly-L-lysine and poly(ethyleneimine) as endotoxin-selective ligands were able to pull endotoxins off the proteins studied, thereby guaranteeing successful decontamination.
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PMID:Proteinase K digestion of proteins improves detection of bacterial endotoxins by the Limulus amebocyte lysate assay: application for endotoxin removal from cationic proteins. 960 41

Soluble chitosan and poly-L-lysine are readily hydrolysed using lysozyme or chitosanase for chitosan, and trypsin, chymotrypsin or proteinase K for poly-L-lysine. For similar amounts of enzyme, chitosanase hydrolysed 57% of the chitosan, compared to 35% for lysozyme. In the case of poly-L-lysine, chymotrypsin and trypsin exhibited similar activities, hydrolysing approximately 41% of the polymer compared to proteinase K at only 16%. In contrast, chitosan and poly-L-lysine membranes, coating alginate beads, were almost totally inert to the respective hydrolytic enzymes. Less than 2% of the membrane weight was hydrolysed. It appears that either membrane material would be stable for in vivo application, and in particular in the protection of DNA during gastrointestinal transit. At chitosanase concentrations of 1.4 mg/ml and in the presence of sodium ions, 20% of the total double-stranded DNA was released from chitosan coated beads. An exchange of calcium for sodium within the bead liquefied the alginate core releasing DNA. The presence of calcium stabilized the alginate bead, retaining all the DNA. Highly pure DNA was recovered from beads through mechanical membrane disruption, core liquefaction in citrate and use of DNA spin-columns to separate DNA/alginate mixtures in a citrate buffer. DNA recovery efficiencies as high as 94% were achieved when the initial alginate/DNA weight ratio was 1000.
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PMID:Stability of chitosan and poly-L-lysine membranes coating DNA-alginate beads when exposed to hydrolytic enzymes. 997 4

An analysis of the temperature factors of an abenzyme has been performed to gain information on the possible role of deterministic chaos in the catalytic mechanism of such artificial proteins. The H-chain displayed a regular attractor of the dimension 3.0 +/- 0.3, whereas the L-chain showed one of <d> = 7.5 +/- 0.5. The abenzyme also displayed a stochastic attractor of the dimension ca. 0.9. The H-chain attractor has one dimension more than those of the native hydrolases chymotrypsin and lysozyme. The additional degree of freedom of the abenzyme offers a likely explanation of the low specific catalytic activities of these artificial enzymes. The dimension of the attractor in the L-chain falls in the range found for other antibodies. Hence, a clear dichotomy seems to rule in this abenzyme; the H-chain displays the vibrational properties of an enzyme and the L-chain those of an antibody. The new data supports the hypothesis of an important role of attractors in biochemical mechanisms by reduction of the number of degrees of freedom (entropy) of reaction partners. A hierarchy of attractors is associated with specific protein functions.
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PMID:An esterolytic antibody with vibrational properties of a catalytic H-chain and a non-catalytic L-chain. 1004 28

A quick and simple method has been developed for the recovery of proteins from water-in-oil microemulsions (w/o-MEs), which is needed to further the use of liquid-liquid extraction in bioseparations. By adding a small portion (0.1 v/v or less) of cosurfactant (e.g., 1-alkanol) to w/o-ME solution, proteins were readily expelled, sometimes as solids, while most or all of the surfactant (Aerosol OT) remained in solution. The release of proteins increased with the further addition of cosurfactant and was greater when the molar ratio of protein to w/o-ME or fractional occupancy (f) was high. However, protein expulsion was also significant when f was small. The addition of cosurfactant released ribonuclease, lysozyme, alpha-chymotrypsin, pepsin, bovine serum albumin (BSA), and catalase from w/o-ME solution, but the expulsion was greater for BSA relative to chymotrypsin and lysozyme. Protein expulsion also increased with cosurfactant chain length for the homologous series of 1-alkanols starting at 1-butanol; however, water was also coexpelled in significant amounts. An exception to the latter rule was 1-butanol, which readily promoted the release of protein, but not encapsulated water. The addition of 1-butanol to a w/o-ME solution containing alpha-chymotrypsin and BSA selectively released the former protein, with chymotryptic activity occurring in the recovered protein. Possible mechanisms for the cosurfactant-mediated release of protein are discussed. Copyright 1998 John Wiley & Sons, Inc.
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PMID:Expulsion of proteins from water-in-oil microemulsions by treatment with cosurfactant 1009 72

Replication and storage of virus are characteristic features of hyperplastic lymphoid tissues in HIV infection. In opportunistic infections, HIV is synthesized by phagocytic mononuclear and Langhans'-type multinucleated macrophages that coexpress the dendritic cell-associated S-100 and p55 antigens. However, similar cells in hyperplastic tonsils and adenoids from HIV+ individuals were alternatively identified as macrophages or, on the basis of the same S-100 and p55 staining, as dendritic cells. To consider establishing the role of these HIV-rich cells in HIV disease, it is important to reconcile this apparent discrepancy in identity. Hyperplastic tonsils and adenoid specimens were analyzed by HIV RNA in situ hybridization (ISH), light and transmission electron microscopy (TEM), and immunohistochemistry (IHC) (HIV Gag p24 protein, S-100, p55, CD68, HAM56, lysozyme, alpha-1-anti-trypsin, and alpha-1-anti-chymotrypsin). In HIV+ pediatric and adult surgical specimens (n = 11), the giant cells and their mononuclear counterpart were positive for both macrophage and p55 and S-100 IHC markers. In addition, TEM, p24 IHC, and ISH showed HIV expression by cells with typical features of macrophages. Furthermore, these cells were not unique to HIV+ specimens, being seen in 20% of hyperplastic T&A surgical specimens (n = 57) lacking HIV as well as in several types of granulomatous processes, such as sarcoidosis. These cells appear to represent an activated phenotype that can develop independent of HIV, but that may represent a viral host in HIV-infected individuals. Thus, the giant and mononuclear cells that produce striking amounts of HIV in tonsils and adenoids are of macrophage origin, yet, as in opportunistic infections, share dendritic cell-associated antigens, reflecting a common CD34+ bone marrow progenitor.
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PMID:The macrophage origin of the HIV-expressing multinucleated giant cells in hyperplastic tonsils and adenoids. 1036 2

The hepatitis B virus X protein (HBX) is essential for the establishment of HBV infection in vivo and exerts a pleiotropic effect on diverse cellular functions. The yeast two-hybrid system had indicated that HBX could interact with two subunits of the 26S proteasome. Here we demonstrate an association in vivo of HBX with the 26S proteasome complex by coimmunoprecipitation and colocalization upon sucrose gradient centrifugation. Expression of HBX in HepG2 cells caused a modest decrease in the proteasome's chymotrypsin- and trypsin-like activities and in hydrolysis of ubiquitinated lysozyme, suggesting that HBX functions as an inhibitor of proteasome. In these cells, HBX is degraded with a half-life of 30 min. Proteasome inhibitors retarded this rapid degradation and caused a marked increase in the level of HBX and an accumulation of HBX in polyubiquitinated form. Thus, the low intracellular level of HBX is due to rapid proteolysis by the ubiquitin-proteasome pathway. Surprisingly, the proteasome inhibitors blocked the transactivation by HBX, and this effect was not a result of a squelching phenomenon due to HBX accumulation. Therefore, proteasome function is possibly required for the transactivation function of HBX. The inhibition of protein breakdown by proteasomes may account for the multiple actions of HBX and may be an important feature of HBV infection, possibly in helping stabilize viral gene products and suppressing antigen presentation.
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PMID:Hepatitis B virus X protein is both a substrate and a potential inhibitor of the proteasome complex. 1043 10

A pulse sequence is proposed to select water magnetization with enhanced specificity through a synergetic combination of several filtering principles. This approach relies on a constant-time evolution period implemented without quadrature detection, which results in a square root 2 increase in signal-to-noise ratios as compared to traditional non-selective methods for water filtration. In addition, the quadrature-free constant-time block facilitates the implementation of the water flip-back strategy, which leads to further gains in sensitivity. The proposed experiment was applied to unlabeled HEW lysozyme and to 15N-labeled chymotrypsin inhibitor 2 which was partially or non 13C-enriched. Water molecules belonging to a spine of hydration between two pseudo beta-sheet strands were identified, solving previously reported discrepancies between the X-ray and refined NMR structure of CI2. The proposed experiment in particularly suitable for hydration studies of mixtures of labeled and unlabeled components, such as ligand-macromolecule complexes.
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PMID:Water-macromolecule interactions by NMR: a quadrature-free constant-time approach and its application to CI2. 1067 22

Although the conformational changes accompanying the oxidation of ferrocytochrome c by the transfer of an electron to cytochrome a are small, they may contribute to the regulation of the electron transfer by transient storage of the liberated energy as strain and atomic vibrations. Both the electron transfer and the conformational changes seem to be controlled by an attractor, i.e. by a manifestation of a deterministic chaos. The putative attractor is regular and is, for the reaction involving the inner monomer of ferricytochrome c (I), of the order of 3.03 +/- 0.03. The conformational changes involving the outer monomer of ferricytochrome c (O) seem also to be controlled by a regular attractor, but its order is 4.2 +/- 0.2. The low order of the coupled reactions of electron transfer and conformational change suggests that it is essential to the electron transfer process in the respiratory chain. Since the order of attractors of other proteins correlates with the vectorial description of the function (1.0 for myoglobin, 2.0 for chymotrypsin and lysozyme, 3.0 for an abenzyme), the value for cyt. c indicates that not only the electron transfer, but also an additional reaction, e.g. the conformational change, are essential for the function of this protein. Hence, the study of protein attractors may yield information on important details, which could not be obtained by other methods.
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PMID:Attractor control of the redox reactions of bovine cytochrome c. 1069 Nov 90

Insulin-degrading enzyme (IDE) was detected by immunoblot analysis in highly purified rat liver peroxisomes. IDE in the peroxisomal fraction was resistant to proteolysis by trypsin and chymotrypsin under conditions where the peroxisomal membranes remained intact. After sonication of the peroxisomal fraction, IDE was recovered in the supernatant fraction. Further, the localization of IDE in the peroxisomes was shown by immunoelectron microscopy. In addition, IDE isolated from peroxisomes degraded insulin as well as oxidized lysozyme as a model substrate for oxidized proteins. These results suggest that IDE exists in an active form in the matrix of rat liver peroxisomes and is involved in elimination of oxidized proteins in peroxisomes.
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PMID:Insulin-degrading enzyme exists inside of rat liver peroxisomes and degrades oxidized proteins. 1123 99


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