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)

Recombinant human tumor necrosis factor-alpha (rTNF) stimulated increased generation of superoxide anion (O2-) by human neutrophils in a concentration-dependent fashion. Preincubation of human neutrophils with rTNF (2.2-2200 units/ml) for 10 min enhanced the subsequent generation of O2- in response to C5a and f-Met-Leu-Phe (FMLP). Recombinant TNF did not enhance O2- generation by neutrophils stimulated with phorbol myristate acetate (PMA). Recombinant TNF alone failed to induce release of myeloperoxidase (MPO) and lysozyme by neutrophils. However, it did enhance the release of MPO and lysozyme by neutrophils stimulated with C5a and FMLP, but not with PMA. Although rTNF alone (0.001-50,000 units/ml) was not chemotactic for neutrophils, preincubation of neutrophils with rTNF (0.001-0.1 units/ml) enhanced the chemotactic activity of suboptimal concentrations of C5a (0.1 nM) and FMLP (5 nM). Neutrophils treated with high concentrations of rTNF (100-10,000 units/ml) showed inhibition of random movement and of chemotaxis induced by C5a or FMLP. We conclude from these studies that rTNF primes neutrophils for enhanced responses to subsequent stimuli and thus may augment the inflammatory response by increased oxidant production and lysosomal enzyme release and promote down-regulation of chemotactic movement.
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PMID:Priming of human neutrophil functions by tumor necrosis factor: enhancement of superoxide anion generation, degranulation, and chemotaxis to chemoattractants C5a and F-Met-Leu-Phe. 132 30

The outer layer of the vitelline membrane from hen egg yolk consists of ovomucin, vitelline membrane outer layer protein I (VMOI) and lysozyme. Here we report the occurrence of a further basic protein (pI 11.5) in the outer layer, which was designated as vitelline membrane outer layer protein II (VMOII). It was dissociated from the outer layer in a 10% (w/v) NaCl solution and purified to homogeneity by ion-exchange chromatography. VMOII is a simple protein with a molecular mass of 6000 Da, as determined by sedimentation equilibrium analysis. The amino acid composition of VMOII was characterized by the absence of Met and high contents of cystine (half) (14%) and basic amino acids (6% Arg, 6% Lys and 3% His). Analysis of carboxymethylated VMOII indicated that all cysteine residues were involved in disulphide bonding, which appears to facilitate the binding of SDS to the protein. Sequence comparison of the N-terminal 20 residues revealed no identity with other known proteins. VMOII contained a small amount of alpha-helix and was quite resistant to heat denaturation.
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PMID:Isolation of a novel protein from the outer layer of the vitelline membrane. 152 Feb 65

Laser Raman spectroscopy was used to investigate the microcosmic and photosensitive damage of YHPD to lysozyme, of which the three-dimensional structure has been elucidated. The experimental results shown by various damages of the main-chain and side-chain of lysozyme are as follows: (i) Phe and Cys are also damaged by photosensitization of YHPD, except for Trp, Tyr, Met, 1/2Cys and His; (ii) the order of the photosensitized sensitivity of various groups of these amino acids have been described; (iii) Trp and Tyr buried in the three-dimensional structure of the protein are damaged very greatly, and (iv) the main-chain conformation of the protein has changed considerably, such as a decrease in orderly structure (alpha-helix, beta-sheet and beta-turn) and a simultaneous increase in random
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PMID:The molecular mechanism of photoporphyrin (YHPD)'s photosensitization--laser Raman spectroscopic study of microcosmic and photosensitive damage of YHPD to protein. 153 29

The state of H-bonding and the hydrophobic interaction of six tryptophan side chains in lysozyme bound to substrate-analogous inhibitors were investigated by combining H----D exchange labeling and Raman difference spectroscopy. The frequency of the W17 band due to Trp-63 shifts downward upon inhibitor binding, indicating a specific and strong H-bond formation between the N1 site of the side chain and the inhibitor molecule. On the other hand, the H-bonding state of Trp-62 in the complex is as weak as that in inhibitor-free lysozyme, suggesting no contribution of this residue to the inhibitor binding. Intensity increases of W17 and W18 bands observed upon inhibitor binding are, respectively, ascribed to an increase at Trp-28 and a decrease at Trp-111 in hydrophobic interactions with the environment. The environmental changes are explained consistently by a movement of the Met-105 side chain sandwiched by two indole rings of Trp-28 and 111 in the direction from Trp-111 to Trp-28. The sandwich structure in a core domain, hydrophobic box, and its rearrangement are considered to play an important role in the enzymatic function of lysozyme.
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PMID:Raman spectroscopic characterization of tryptophan side chains in lysozyme bound to inhibitors: role of the hydrophobic box in the enzymatic function. 164 7

To determine the energetic and structural consequences of placing a charged group within the core of a protein, two "buried charge" mutants, Met 102----Lys (M102K) and Leu 133----Asp (L133D) were constructed in phage T4 lysozyme. Both proteins fold at neutral pH, although they are substantially less stable than wild type. The activity of M102K is about 35% that of wild type, while that of L133D is about 4%. M102K could be crystallized, and its structure was determined at high resolution. The crystal structure (at pH 6.8) of the mutant is very similar to that of wild type except for the alpha-helix that includes residues 108-113. In wild-type lysozyme, one side of this helix is exposed to solvent and the other contacts Met 102. In the M102K structure this alpha-helix becomes much more mobile, possibly allowing partial access of Lys 102 to solvent. The stability of M102K, determined by monitoring the unfolding of the protein with CD, is pH-dependent, consistent with the charged form of the substituted amino acid being more destabilizing than the uncharged form. The pKa of Lys 102 was estimated to be 6.5 both by differential titration and also by NMR analysis of isotopically labeled protein with 13C incorporated at the C epsilon position of all lysines. As the pH is lowered below pH 6.5, the overall three-dimensional structure of M102K at room temperature appears to be maintained to pH 3 or so, although there is evidence for some structural adjustment possibly allowing solvent accessibility to the protonated form of Lys 102.
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PMID:Structural and thermodynamic consequences of burying a charged residue within the hydrophobic core of T4 lysozyme. 174 70

The inactivation of lysozyme caused by the radicals produced by thermolysis of 2,2'-azo-bis-2-amidinopropane can be prevented by the addition of different compounds that can react with the damaging free radicals. Compounds of high reactivity (propyl gallate, Trolox, cysteine, albumin, ascorbate, and NADH) afford almost total protection until their consumption, resulting in well-defined induction times. The number of radicals trapped by each additive molecule consumed ranges from 3 (propyl gallate) to 0.12 (cysteine). This last value is indicative of chain oxidation of the inhibitor. Uric acid is able to trap nearly 2.2 radicals per added molecule, but even at large (200 microM) concentrations, a residual inactivation of the enzyme is observed, which may be caused by urate-derived radicals. Compounds of lower reactivity (tryptophan, Tempol, hydroquinone, desferrioxamine, diethylhydroxylamine, methionine, histidine, NAD+ and tyrosine) only partially decrease the lysozyme inactivation rates. For these compounds, we calculated the concentration necessary to reduce the enzyme inactivation rate to one half of that observed in the absence of additives. These concentrations range from 9 microM (tryptophan and Tempol) to 5 mM (NAD+).
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PMID:Effect of additives on the inactivation of lysozyme mediated by free radicals produced in the thermolysis of 2,2'-azo-bis-(2-amidinopropane). 177 8

The N-terminal amino acid sequences of purified recombinant human gamma-interferon, alpha 2a-interferon and interleukin-2 expressed in E. coli were determined on an Applied Biosystems 477A Protein/Peptide Sequencer and 120A PTH Amino Acid Analyzer. From the raw chromatographic data of these samples, the identity, heterogeneity, amount of methionine-plus species remaining in the final products, and the probable process contaminants were evaluated with the help of computer methods including database searching. General methods to characterize trace contaminants in protein samples were also discussed. Among the sequenced samples, only gamma-interferon was shown to be N-terminal homogeneous. Methionine-containing species were found in interleukin-2 and alpha 2a-interferon. Chicken eggwhite lysozyme was detected in very small amounts in one batch of samples. These results provide valuable information for the development and improvement of preparation methods as well as regulatory responses to recombinant products.
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PMID:Evaluation of the purity of recombinant proteins and detection of residual protein contaminants via N-terminal microsequencing and database searching. 180 20

The lysis gene region of phage 21 contains three overlapping reading frames, designated S21, R21, and Rz21 on the basis of the analogy with the SRRz gene cluster of phage lambda. The 71-codon S21 gene complements lambda Sam7 for lysis function but shows no detectable homology with S lambda in the amino acid or nucleotide sequence. A highly related DNA sequence from the bacteriophage PA-2 was found by computer search of the GenBank data base. Correction of this sequence by insertion of a single base revealed another 71-codon reading frame, which is accordingly designated the SPA-2 gene and is 85% identical to S21. There are thus two unrelated classes of S genes; class I, consisting of the homologous 107-codon S lambda and 108-codon P22 gene 13, and class II, consisting of the 71-codon S21 and SPA-2 genes. The codon sequence Met-Lys-(X)-Met...begins all four genes. The two Met codons in S lambda and 13 have been shown to serve as translational starts for distinct polypeptide products which have opposing functions: the shorter polypeptide serves as the lethal lysis effector, whereas the longer polypeptide acts as a lysis inhibitor. To test whether this same system exists in the class II S genes, the Met-I and Met-4 codons of S21 were altered in inducible plasmid clones and the resultant lysis profiles were monitored. Elimination of the Met-1 start results in increased toxicity, and lysis, although not complete, begins earlier, which suggests that both starts are used in the scheduling of lysis by S21 and is consistent with the idea that the 71- and 68-residue products act as a lysis inhibitor and a lysis effector, respectively. In addition, the R gene of 21 was shown to be related to P22 gene 19, which encodes a true lysozyme activity, and was also found to be nearly identical to PA-2 ORF2. We infer that the 21 and PA-2 R genes both encode lysozymes in the T4 e gene family. These three genes form a second class lambdoid R genes, with the lambda R gene being the sole member of the first class. The existence of two interchangeable but unrelated classes of S genes and R genes is discussed in terms of a model of bacteriophage evolution in which the individual gene is the unit of evolution.
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PMID:Dual start motif in two lambdoid S genes unrelated to lambda S. 201 62

The partial molar volumes of various compounds that model protein constituent groups, such as tripeptides (Gly-X-Gly, where X = Gly, Ala, Val, Leu, Ile, Pro, Met, His, Ser), homopeptides (Glyn, n = 3,4,5), and simple organic analogues of amino acid side chains (methanol, acetamide, propanamide, acetic acid, propanoic acid, n-butanamine, n-butanamine nitrate, n-propylguanidine nitrate, 4-methylphenol), have been determined in aqueous solution with a vibrational densimeter in the temperature range of 5-85 degrees C. The partial molar volumes of amino acid side chains and the peptide unit were estimated from the data obtained. Assuming additivity of component groups, the partial molar volumes of polypeptide chains of several proteins over a broad temperature range were calculated. The partial molar volume functions of four proteins (myoglobin, cytochrome C, ribonuclease A, lysozyme) were compared with those determined experimentally for the unfolded and native forms of these proteins. It has been shown that the average deviation of the calculated functions from the experimental ones does not exceed 3% over the temperature range studied.
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PMID:Partial molar volumes of polypeptides and their constituent groups in aqueous solution over a broad temperature range. 208 Dec 62

The crystal structures of HCO-Met-Leu-Phe-OC(CH3)3, (CH25H39N3O5S), fMLP-OtBu, and HCO-Met psi [CSNH]-Leu-Phe-OCH3, (C22H33N3O4S2), fMS LP-OMe, have been determined by single crystal X-ray diffraction, and their conformational properties investigated by molecular mechanics energy calculations. Crystals of fMLP-OtBu are monoclinic, space group P2(1), a = 12.027(4), b = 9.492(3), c = 12.660(4) A, beta = 101.99(3) degrees, Z = 2; those of fMS LP-OMe are orthorhombic, space group P2(1)2(1)2(1), a = 7.130(1), b = 12.097(2), c = 31.060(5) A, Z = 4. The first compounds fMLP-OtBu is the t-butyl ester of the tripeptide fMLP that represents one of the most potent compounds in inducing the lysozyme release from human neutrophils that reflects the chemotactic activity. From the crystal structure, it is shown that the orientation of the phenylalanine side chain is largely affected by the presence of the bulky group. fMSLP-OMe was shown to be inactive after thionation of the methionine residue in the original tripeptide. Nevertheless, the crystal structure does not reveal any influence of the presence of the thionated peptidic bond on the backbone conformation. The X-ray results have been used to generate parameters for empirical energy calculations. Subsequently, a strategy based on random generation of conformations followed by energy-minimization was applied to investigate the conformational space of thiopeptides, in comparison with normal peptides. From molecular free energy calculations, it is shown that the main influence of the introduction of a thioamide bond on the molecular structure is to prevent the existence of C7(eq) conformations involving the thiomethionine residue. Consequently, a larger number of conformers are found to form intramolecular hydrogen bonds involving the formyl group, reducing its availability to interact with the receptor. For the first time, the theoretical prediction of the existence of C7eq conformations for fMLP is made. The resulting conformers are compared to previously active structures of these chemotactic agents.
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PMID:Crystal and molecular structure of two geometrically restricted chemotactic tripeptides, analogues of formyl-methionine-leucine-phenylalanine. 209 Jun 40


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