Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

---

Query: EC:3.2.1.17 (lysozyme)
21,489 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A culture of Streptococcus dysgalactiae (C 26) was shown to bind only to 125I-IgG, whereas another S. dysgalactiae culture (C 12) bound both 125I-IgG and 125I-albumin. The IgG-binding proteins could be readily solubilized by lysozyme treatment of the bacteria and isolated by affinity chromatography on IgG Sepharose. The purified IgG-binding protein from S. dysgalactiae C 26, which lacked simultaneous albumin binding activity, precipitated with IgG preparations from man, cow, horse, pig and mouse but not with chicken IgG. This IgG-binding protein was coupled to CNBr-activated Sepharose and subsequently used for the purification of IgG from both bovine and human serum. SDS-PAGE and immunoelectrophoretic studies confirmed the purity of the eluted proteins.
...
PMID:Isolation of immunoglobulin G by affinity chromatography using an IgG Fc receptor protein from Streptococcus dysgalactiae coupled to a solid phase. 250 67

The specificity of the basic bactericidal/permeability increasing protein (BPI) of polymorphonuclear leukocytes (PMN) for gram-negative bacteria is attributable to its strong attraction for the negatively charged envelope LPS. The antibacterial activity of PMN homogenates or extracts toward Escherichia coli corresponds to their BPI content and is blocked by anti-BPI IgG, suggesting that BPI action is unaffected by the presence of other PMN proteins. To test if BPI is preferentially bound to E. coli when other antibacterial proteins are present, we have measured binding in buffered (pH 7.5) balanced salts solution of [125I] human BPI to E. coli J5 in the presence and absence of other human PMN granule proteins. BPI binding is saturable with an apparent K = 23 nM and 2.2 million binding sites/cell. While binding of [125I] human BPI is competitively inhibited by human or rabbit BPI, it is only weakly inhibited by myeloperoxidase, lysozyme, or cathepsin G. In contrast, myeloperoxidase binding to E. coli is strongly inhibited by BPI. Moreover, incubation of E. coli with crude extracts of PMN or CML spleen results in near quantitative binding of BPI, identified by silver staining and immunoblotting after SDS-PAGE of the washed E. coli pellet, without recognizable binding of other leukocyte proteins (greater than 98% of added total protein is recovered in supernatant). After addition of 200 mM MgCl2, approximately 80% of bound BPI is released as fully active and pure protein (as judged by SDS-PAGE and HPLC). Thus the selective and reversible binding of BPI in crude PMN extracts to target bacteria provides a one-step "affinity" purification procedure.
...
PMID:Preferential binding of the neutrophil cytoplasmic granule-derived bactericidal/permeability increasing protein to target bacteria. Implications and use as a means of purification. 253 11

There are no published methods on plasmid isolation from Peptostreptococcus spp., therefore two methods of plasmid isolation from this genera were analysed: the boiling and alkaline-SDS methods. Plasmid DNA was not recovered by the boiling method, however, with the alkaline-SDS method, cryptic plasmid DNA was detected in two P. asaccharolyticus and one P. magnus strains. To achieve optimum lysis, Peptostreptococcus cells were treated with lysozyme (2 mg/ml) for 15 min. at 37 degrees C followed by proteinase K (0.2 mg/ml) for 1 h at 37 degrees C. In addition we report, the occurrence of clindamycin or metronidazole-resistant peptostreptococci, but these phenotypes were not correlated with plasmid carriage.
...
PMID:Plasmid analysis and antimicrobial susceptibilities of Peptostreptococcus species. 259 60

1. Lysozyme and alpha-lactalbumin from the milk of the common ringtail possum have been purified and partially sequenced. 2. The lysozyme had similar enzymic activity to the c-type lysozyme of the domestic hen and 43% homology over the N-terminal 49 residues. 3. alpha-Lactalbumin was present in the milk in two biologically active forms; the more acidic form had 66% sequence homology with the N-terminal 35 residues of red-necked wallaby, 54% with human and 43% with bovine alpha-lactalbumin. 4. SDS polyacrylamide-gel electrophoresis of milk samples showed that alpha-lactalbumin was present in the milk throughout lactation but that lysozyme first appeared only in mid-lactation. The implications of this functional adaptation are discussed.
...
PMID:Isolation, partial sequence and asynchronous appearance during lactation of lysozyme and alpha-lactalbumin in the milk of a marsupial, the common ringtail possum (Pseudocheirus peregrinus). 260 16

A method for determination of amino acid composition of proteins separated by SDS-polyacrylamide gel electrophoresis and transferred to polyvinylidene difluoride (PVDF) membranes is described. A single blotted band containing 50 to 200 pmoles of protein was cut out and submitted to acid hydrolysis with HCl followed by derivatization with phenylisothiocyanate. The amino acid derivatives were separated by reverse phase high-performance liquid chromatography. Bovine serum albumin, lysozyme, myoglobin, ovalbumin, soybean trypsin inhibitor and carbonic anhydrase were analyzed; the results revealed a good correspondence with reported values. This can be considered an analytical method to determine the amino acid composition of samples from microquantities of protein mixtures, particularly in those cases in which SDS-polyacrylamide gel electrophoresis is the most suitable separation system.
...
PMID:Micro-determination of amino acid composition of proteins electroblotted onto polyvinylidene difluoride membranes. 263 61

A group A streptococcal strain demonstrated binding activities for 125I-murine IgG3 and 125I-human IgG. This 125I-murine IgG3 binding could be inhibited by unlabelled equine IgG but not by IgG from cattle, chickens and dogs, indicating binding properties of IgG Fc-receptors of type II. In contrast to binding sites of Streptococcus dysgalactiae (serogroup C) carrying type III IgG Fc-receptors, the binding sites of the group A streptococcus appeared to be antigenically different, extremely sensitive to trypsin and did not show any cross reactions with human albumin. The group A and group C streptococcal binding sites could be solubilized by lysozyme treatment of the bacteria and subsequently isolated by affinity chromatography on human IgG-Sepharose. Further analysis of the group A and group C streptococcal binding proteins by SDS-PAGE and Western blotting revealed numerous, almost identical protein bands with binding activities for 125I-murine IgG3.
...
PMID:Interaction of type II IgG Fc-receptors from streptococci of serological group A with murine IgG. 268 6

The cell-bound sialidase of Actinomyces viscosus DSM 43798 was solubilized by mechanical cell disruption and lysozyme treatment. The enzyme was enriched 30,000-fold by cation-exchange chromatography, gel-filtration, and FPLC ion-exchange chromatography, thus obtaining 10 micrograms sialidase protein from 26 g wet cells with a specific activity of 680 U/mg protein. Since sialidase activity was also found in the culture medium, this enzyme was isolated as well, requiring the additional application of FPLC gel-filtration. Both sialidase preparations were apparently homogenous on SDS-PAGE and have similar properties. The substrate specificity of the A. viscosus sialidase was tested with 16 sialoglycoconjugates: The enzyme showed a higher activity with serum glycoproteins than with gangliosides, mucins or sialyllactoses. 4-O-Acetylated N-acetylneuraminic acid was not cleaved from equine submandibular gland mucins or serum glycoproteins in contrast to N-acetyl- and N-glycoloylneuraminic acid. 9-O-Acetyl-N-acetylneuraminic acid was released from bovine submandibular gland mucin, as confirmed by TLC. The sialidase hydrolyses alpha(2----6)-linkages more rapidly than alpha(2----8)- and alpha(2----3)-bonds. Cations, except Hg2+, or chelating agents have no influence on enzyme activity. The sialidase has a relatively high molecular mass of 150 kDa, but consists of only one unit. The enzyme is labile towards freezing and thawing, but can be stored at 4 degrees C in 0.1 M acetate buffer, pH 5.
...
PMID:Properties of sialidase isolated from Actinomyces viscosus DSM 43798. 274 53

The protein content of normal human tears from five subjects was examined by molecular weight separation using SDS-polyacrylamide gel electrophoresis (PAGE) and by charge separation using agarose isoelectric focusing (IEF) gels. After separation, specific proteins were identified by immunoblot and immunofixation. Tear proteins examined included albumin, IgA, IgG, prealbumin, lactoferrin, lysozyme, secretory component and transferrin. These techniques required 1 to 14 microliters unconcentrated tears. We found SDS-PAGE superior to agarose IEF to examine total tear protein pattern, and silver stain almost ten-fold more sensitive than Coomassie blue stain. Immunologic staining markedly enhanced protein detection in all tear samples and appeared to offer the definitive method to probe for a specific protein in tears. In this study prealbumin and a portion of the IgG were present in normal tears at higher than expected molecular weight, suggesting they were present in complexed form. Prealbumin and secretory component staining showed marked variability between subjects. These techniques should be applicable to examine tear proteins in a variety of ocular disease states.
...
PMID:Electrophoresis combined with immunologic identification of human tear proteins. 275 2

Two extraction procedures of non-purulent sputum for the isolation of human mucus proteinase inhibitor (MPI) in its free and bound forms have been assayed. The dissociating procedure involved sputum homogenization in 1M NaCl and 4% (w/v) trichloroacetic treatment. When the soluble material was applied to a CM-Trisacryl column, a non-negligible, MPI-related inhibitory activity was recovered with the highly glycosylated constituents not retained on the column; the amount of MPI released in a free form was retained and eluted from the column according to the basic character of this inhibitor. The non-dissociating procedure consisted in a high water dilution (1:12) of sputum, known to bring into solution the macromolecular, fibrillar constituents, which was followed by ultrafiltration on selected Mr cut-off membranes. All the inhibitory activity was recovered with the high Mr (greater than 100,000) fraction which was shown on SDS-PAGE to be essentially composed of strongly glycosylated material; on electrophoretic analysis under non-reducing conditions, the MPI activity was visualized as three bands which corresponded to the inhibitor released from this high Mr fraction in the presence of SDS. As mucin-type molecules are the major, highly glycosylated constituents of bronchial secretions, it is suggested that they are responsible for the entrapping of MPI within their macromolecular network; it would appear that, as well as for lysozyme, electrostatic interactions occur between the acid charges of mucins and the basic charges of MPI. The possible in vivo consequences of these interactions on MPI activity are discussed.
...
PMID:Evidence for the tight binding of human mucus proteinase inhibitor to highly glycosylated macromolecules in sputum. 277 94

We have identified previously two transcription factors, COUP (chicken ovalbumin upstream promoter) and S300-II, from HeLa cell nuclear extracts. In this paper, the purine base and the phosphate backbone contact sites for the COUP transcription factor were defined. These studies indicate that the COUP box transcription factor interacts with specific base residues in the major groove of the DNA helix. In addition, we have purified the S300-II factor over 100,000-fold. The polypeptide possessing functional transcriptional activity has been identified by SDS-PAGE followed by gel-slice elution and a renaturation assay. It is absolutely required for in vitro function of the ovalbumin promoter. In addition, S300-II stimulates transcription from the MMTV and lysozyme promoters. Kinetic studies probing the interaction of S300-II with COUP factor suggest that it may stabilize COUP-promoter complexes by slowing their rate of dissociation.
...
PMID:Interactions between a DNA-binding transcription factor (COUP) and a non-DNA binding factor (S300-II). 304 Feb 58


<< Previous 1 2 3 4 5 6 7 8 9 10 Next >>

---