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

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

The effect of exogenous lysophosphatidylcholine on the membranes of liposomes containing protein has been studied. Lysophosphatidylcholine severely damaged liposomes prepared in the presence of membrane proteins such as glycophorin and "band 3" protein of human erythrocytes. Some basic proteins such as cytochrome c, lysozyme and polylysine also could sensitize liposomes to lysophosphatidylcholine. As described in previous papers (Inoue, K., et al. (1974) Biochim. Biophys. Acta 363, 361-372; Utsumi, H., et al. (1978) Biochemistry 17, 1990-1996), large multilamellar liposomes without protein were affected by lysophosphatidylcholine only under certain conditions where a phase boundary could exist. Sonicated liposomes without protein were almost completely insensitive to lysophosphatidylcholine. Liposomes prepared by the cholate dialysis method were also insensitive to lysophosphatidylcholine, irrespective of the incubation temperature. It is known that natural membranes such as membranes of erythrocytes and of other mammalian cells are rather sensitive to lysophosphatidylcholine. The difference observed between natural membrane and liposomal membrane seems to be removed by the introduction of proteins into lipid bilayers. The mode of interaction of lysophosphatidylcholine with membranes of liposomes containing protein is discussed.
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PMID:The interactions of lysophosphatidylcholine with protein-containing liposomes. 627 88

The effect of molecular charge of proteins on proximal tubular reabsorption was evaluated in the rat. Native and two cationized forms of albumin, native and anionized lysozyme, and native and anionized cytochrome c were iodinated with 125I. The different forms of each type of protein were alternately microinfused into the same site of proximal convoluted tubules in vivo. Tubular reabsorption was determined as the difference between the amounts of TCA-precipitable radioactivity infused and recovered in the urine. At low concentration of albumin 5 times more cationized than anionic albumin and 2.7 times more cationic than anionized lysozyme were reabsorbed by the proximal tubule. At two of four concentrations, proximal tubular uptake of cationic cytochrome c exceeded that of anionized cytochrome c. Uptake of cationic cytochrome c exceeded that of cationic lysozyme; however, the difference in uptake between native cationic and anionized species of the two proteins was much greater for lysozyme than for cytochrome c. The data reveal that a higher isoelectric point significantly enhances proximal tubular reabsorption of albumin, lysozyme, and cytochrome c and that proteins with similar molecular weight and isoelectric point are not necessarily reabsorbed to the same degree. This suggests that in addition to total molecular charge the molecular configuration and/or distribution of electrical charges on teh protein surface determine protein binding by the luminal membrane and subsequent endocytosis by the proximal tubule.
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PMID:Renal tubular uptake of protein: effect of molecular charge. 630 Dec 86

Approximately one-third of all proteins reported in the literature have a pI sufficiently high to be resolved by cation-exchange chromatography. This paper reports the preparation and use of new high-performance polymeric-bonded-phase cation-exchange columns. Starting from a very stable, covalently bonded polyamide coating on microparticulate silica, simple derivatization produces a versatile cation-exchange material useful for separations traditionally performed on classical carboxymethylated soft gel supports. Column behavior was monitored using chymotrypsinogen, cytochrome c, and lysozyme as standards. The polymeric bonded phase was stable to pH 2.5 and exhibits enhanced selectivity for proteins due to a slight hydrophobic character of the matrix. Several separations of biological interest that demonstrate the utility of these small cation-exchange columns for modern biochemical separations are shown.
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PMID:High-performance cation-exchange chromatography of proteins. 630 52

The particle volume of a protein which represents the expansion of the molecular chain is a useful probe to measure its conformation change in solution. To study the details of the conformation transition, we will report a novel device to trace the particle-volume change against increasing denaturant concentration. According to the denaturant gradient in the eluant of high-performance gel-permeation chromatography, information concerning the elution volume of proteins in the course of denaturation can be successively accessed. When a protein is injected into a denaturant solution, its effective molecular volume increases by the unfolding of a native compact structure, and the elution peak goes forward to separate from that of the native protein. Typical elution patterns were computer-simulated in an extended algorithm of the plate theory. The kinetic feature of denaturation and the effect of the denaturant gradient are discussed. The denaturation schemes of lysozyme, cytochrome c, and phosphoglycerate kinase were studied.
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PMID:Denaturant-gradient chromatography for the study of protein denaturation: principle and procedure. 631 Oct 44

Filtered proteins including the low-molecular-weight protein lysozyme are reabsorbed by the proximal tubule via adsorptive endocytosis. This process starts with binding of the protein to the brush-border membrane. The binding of 125I-labelled egg-white lysozyme (EC 3.2.1.17) to isolated brush-border membranes of rat kidney and the effect of several low-molecular weight proteins on that binding was determined. The Scatchard plot revealed a one-component binding type with a dissociation constant of 5.3 microM and 53.0 nmol/mg membrane protein for the number of binding sites. The binding of the cationic lysozyme was inhibited competitively by the addition of cationic cytochrome c to the incubation medium, while the neutral myoglobin had no effect. The anionic beta-lactoglobulin A inhibited the lysozyme binding in a noncompetitive manner. These data suggest that the binding takes place between positively charged groups of the protein molecule and negative sites on the brush-border membrane, and, the competition between the cationic cytochrome c and the cationic lysozyme for the binding sites may be responsible for the inhibitory effect of cytochrome c on renal lysozyme reabsorption. The binding step at the brush-border membrane appears to be cation-selective.
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PMID:Effect of low-molecular-weight proteins on protein (lysozyme) binding to isolated brush-border membranes of rat kidney. 632 Aug 87

Polymyxin B nonapeptide, a polymyxin B derivative which lacks the fatty acyl part and the bactericidal activity of polymyxin, was shown to sensitize smooth encapsulated Escherichia coli (O18:K1) and smooth Salmonella typhimurium to hydrophobic antibiotics (novobiocin, fusidic acid, erythromycin, clindamycin, nafcillin, and cloxacillin). The polymyxin B nonapeptide-treated bacteria were as sensitive to these antibiotics as are deep rough mutants. A lysine polymer with 20 lysine residues (lysine 20) had a largely similar effect. Larger lysine polymers and the protamine salmine were bactericidal but, at sublethal concentrations, sensitized the strains to the antibiotics mentioned above, whereas lysine4, streptomycin, cytochrome c, lysozyme, and the polyamines cadaverine, spermidine, and spermine had neither bactericidal nor sensitizing activity.
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PMID:Polycations sensitize enteric bacteria to antibiotics. 641 64

A new procedure for the analyses of tryptophan and the total amino acid composition of proteins was based on the observations that pyridine borane reduces tryptophan in trifluoroacetic acid, while other amino acids remain intact [M. Kurata, Y. Kikugawa, T. Kuwae, I. Koyama, and T. Takagi (1980) Chem. Pharm. Bull. 28, 2274-2275; W.S.D. Wong, D.T. Osuga, and R.E. Feeney (1984) Anal. Biochem. 139, 58-67]. Concentrated HCl was used instead of trifluoroacetic acid for analytical purposes. The products were stable to hydrolysis in 6 N HCl, and the reduction did not interfere with hydrolysis and subsequent analyses. Quantitative recovery was achieved with most proteins when they were subjected to acid reduction in ice-cooled concentrated HCl with two incremental additions of pyridine borane. The reaction was terminated after 10 min by dilution with an equal volume of H2O, vacuum sealing, and hydrolyzing at 110 degrees C for 22 h. The yields of the expected values for cytochrome c, catalase, bovine serum albumin, subtilisin BPN', trypsin, chymotrypsin, beta-lactoglobulin, lysozyme, and pepsin were obtained. Ovotransferrin and ovalbumin, however, yielded values for tryptophan lower than literature values. With two different ion-exchange methods, the recoveries of all other amino acids were comparable to those obtained by acid hydrolysis with 6 N HCl. Since the same hydrolysate can be analyzed for both tryptophan and all the other amino acids, the procedure is a more convenient method than those requiring separate determinations. Initial results indicate that the method may be applied to high-performance liquid chromatographic procedures with adaptations of the protocols if necessary.
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PMID:Determination of tryptophan as the reduced derivative by acid hydrolysis and chromatography. 652 98

Quantitative studies of endogenous lysozyme (low molecular weight protein) were performed in rats. Urine and plasma concentrations of lysozyme and inulin were measured spectrophotometrically. An improved lysozyme assay (standard curve established by using egg white-lysozyme) enabled us to determine the mean plasma concentration of endogenous lysozyme (4.4 micrograms X ml-1) and the urinary concentrations of endogenous lysozyme (between 0.1 and 3.8 micrograms X ml-1. The urinary concentrations of endogenous lysozyme were found to be dependent on urinary flow rate. High urinary concentrations (ULy) were found at low urinary flow rates (V). The excreted amount of endogenous lysozyme (ULy X V) was independent of urinary flow rate and yielded a constant value of 0.02 micrograms X min-1. Mean glomerular filtration rate (GFR) was 1.2 ml X min-1 while clearance of endogenous lysozyme averaged 0.0039 ml X min-1. Inhibition of endogenous lysozyme reabsorption by cytochrome c was used to estimate the glomerular sieving coefficient of endogenous lysozyme in clearance experiments. CLy/GFR increased from a mean value of 0.0053 in control rats to 0.8 at maximal inhibition of tubular reabsorption of endogenous lysozyme by cytochrome c. Knowing the glomerular sieving coefficient, GFR and the lysozyme concentrations in plasma and urine samples, the filtered, excreted and reabsorbed lysozyme amounts could be calculated: 0.5% excreted and 99.5% reabsorbed. Reabsorbed endogenous lysozyme is stored in the kidney in high amounts (1,983 micrograms X g-1 kidney).
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PMID:Renal handling of endogenous lysozyme in the rat. 664 26

1. A cell-free preparation of membrane fragments was prepared from the thermophilic blue-green alga Phormidium laminosum by lysozyme treatment of the cells followed by osmotic shock to lyse the spheroplasts. The membrane fragments showed high rates of photosynthetic electron transport and O2 evolution (180-250 mumol of O2/h per mg of chlorophyll a with 2,6-dimethyl-1,4-benzoquinone as electron acceptor). O2-evolution activity was stable provided that cations (e.g. 10mM-Mg2+ or 100mM-Na+) or glycerol (25%, v/v) were present in the suspending medium. 2. The components of the electron-transport chain in P. laminosum were similar to those of other blue-green algae: the cells contained Pigment P700, plastocyanin, soluble high-potential cytochrome c-553, soluble low-potential cytochrome c-54 and membrane-bound cytochromes f, b-563 and b-559 (both low- and high-potential forms). The amounts and midpoint potentials of the membrane-bound cytochromes were similar to those in higher-plant chloroplasts. 3. Although O2 evolution in P. laminosum spheroplasts was resistant to high temperatures, thermal stability was not retained in the cell-free preparation. However, in contrast with higher plants, O2 evolution in P. laminosum membrane fragments was remarkably resistant to the non-ionic detergent Triton X-100.
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PMID:Photosynthetic electron transport in a cell-free preparation from the thermophilic blue-green alga Phormidium laminosum. 677 63

Heterocysts of the blue-green alga Nostoc muscorum have been isolated by prolonged treatment with lysozyme. Quantitative data are presented which show the occurrence of cytochromes c-553, f-557 and b-563 in heterocysts in amounts comparable to vegetative cells. Particularly the content of the water-soluble cytochrome c-553 can be used to evaluate the intactness of a heterocyst preparation. Cytochrome f-557 has been partially purified and found to be a c-type cytochrome corresponding to cytochrome f of higher plants and other algae. Cytochrome b-559 is present in vegetative cells but not in heterocysts. The content of plastoquinone in heterocysts is reduced to 42% of the amount present in vegetative cells. These data suggest a degradation of Photosystem II during heterocyst differentiation. Measurements of photosynthetic electron transport in heterocysts proved the inability of the photosynthetic apparatus to carry out electron transport with electrons donated by water or diphenylcarbazide. In Tris-washed thylakoids from vegetative cells, however, diphenylcarbazide can act as an electron donor to Photosystem II.
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PMID:Components and activity of the photosynthetic electron transport system of intact heterocysts isolated from the blue-green alga Nostoc muscorum. 677 15


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