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)

A method is proposed for observation of the interaction between charged macromolecules such as proteins. The method is based on the fact that the pK of an ionizable reporter group attached to a macromolecule can be altered by the electrostatic effect of another charged macromolecule which associates with the former. The effectiveness of the method was shown in the study of the association of bovine serum albumin with hen egg lysozyme [EC 3.2.1.17]. The errors inherent in this method in obtaining the equilibrium constant of the association reaction and procedures for their correction are discussed.
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PMID:A method for observing protein-protein interaction. 23 62

Steady-state conductivity measurements and dielectric measurements in the frequency range 10(-5) to 100 Hz are reported for samples of bovine serum albumin, casein, and lysozyme complexed with methylglyoxal. Compared with the untreated proteins, the brown complexed proteins exhibit an increased conductivity and free electron spin density, together with a low-frequency dielectric dispersion. These results can be taken as evidence that the interaction with methylglyoxal results in the proteins possessing an increased electronic activity associated with the creation of mobile electron holes within the valence band states of the protein molecules.
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PMID:Electronic properties of some protein--methylglyoxal complexes. 27 48

A model system for the partitioning of peripheral membrane proteins into membranes by ligand binding has been examined experimentally. Both bovine serum albumin and lysozyme partition between water and 1-butanol by the addition of sodium p-toluene sulfonate at pH 2.4. The partitioning is characterized by high orders of reaction: 25 and 10, respectively. Theory indicates that these high orders of reaction need not result from cooperative ligand binding in either phase, but depend primarily upon the number N of protein sites at which the transfer-promoting ligant binds, and on the difference in free energy of formation delta F0s of the protein--ligand complexes in the two phases. From the reaction orders and the experimental values of N, 80 for albumin and 11 for lysozyme, delta F0s was calculated to be --0.5 kcal/mol (--2.1 kJ/mol) and --0.8 kcal/mol (--2.5 kJ/mol) per ligand bound, respectively. Experiments measuring the dependence on ligand concentration of the rate of protein electrophoresis across the water/butanol interface are described. These rates increase by more than two orders of magnitude as the ligand concentration approaches the critical value for partition and are inversely dependent on the number of ligant sites for the two proteins studied.
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PMID:Ligand-promoted transfer of proteins between phases: spontaneous and electrically helped. 27 41

The hydration isotherms of alpha-chymotrypsin, lysozyme, pork insulin, pork pepsin and serum albumin were obtained by means of dynamic method. The values of BET-monolayers for processes of water sorption leads to (h) and desorption comes from (h) do not depend on the static or dynamic way of achieving of hydration equilibrium in spite of difference in the shape of isotherms. The values of comes from h for proteins with known tertiary structure (alpha-chymotrypsin, lysozyme and insulin) coinside with the number of exposed polar amino acid side chains. The lowering of leads to h values in comparison with comes from h is correlated with inability of omega-amido groups of Asn and Gln residues and of ion pair-forming residues to take part in the formation of sorptive BET-monolayer. These rules for the interpretation of hydration isotherms were used to evaluate the numbers of exposed and buried polar side chains in proteins with unknown tertiary structure--pepsin and serum albumin.
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PMID:[Isotherms of globular protein hydration under dynamic conditions]. 32 24

Long, nonseptate filamentous cells consisting of 5 to 40 single-cell unit lengths were formed from Escherichia coli surface mutant ONT-3 by treatment with a sublethal concentration of sodium dodecyl sylfate. As distinct from several other elongated cells (e.g., thymine-starved filaments), it was found here that stable giant spheroplasts, 5 to 10 micrometers in diameter, were produced by the action of lysozyme in the presence of bovine serum albumin via the gradual fusion of distinct spheroplasting bulbs.
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PMID:Biochemical and topographical studies on Escherichia coli cell surface. IV. Giant spheroplast formation from a filamentous cell. 37 97

A complete and authentic picture of the qualitative and quantitative composition of the milk of Homo sapiens is presented. Older original references are reexamined along with data prublished during the last 2 decades. Mature human milk is made up of 3%-5% fat, 0.8%-0.0% protein, 6.9%-7.2% carbohydrate calculated as lactose, and 0.2% mineral constituents expressed as ash. The energy content is 60-75 kcal/100ml. Protein content is considerably higher and carbohydrate content lower in colostrum than in mature milk. Fat content does not vary consistently during lactation but exhibits large diurnal variations and increases during the course of each nursing. Race, age, parity, or diet fail to have a great affect on milk composition. There is no consistent compositional difference between milks from the 2 breasts unless 1 breast is infected. The principal proteins of human milk are a casein homologous to bovine B-casein, a-lactalbumin, lactoferrin, immunoglobulin IgA, lysozyme, and serum albumin. Lactose is the principal sugar of human milk. Human milk fat is characterized by high contents of palmitic and oleic acids, the former heavily concentrated in the 2-position and the latter in the 1- and 3-positions of the triglycerides. The principal mineral constituents of human milk are Na, K, Ca, Mg, P, and C1. About 25% of the total nitrogen of human milk represents nonprotein compounds. These include urea, uric acid, creatine, creatinine, and a large number of amino acids.
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PMID:The composition of human milk. 39 66

Daily lysozyme (hen egg) injections, beginning on day 6 of Trypanosoma lewisi infections in rats, significantly reduced the number of circulating trypanosomes. The effect was dose dependent. Maximum reduction (50%) occurred 24 hours after one treatment of 80 mg was given intraperitoneally (I.P.). The same dose of lysozyme was more effective when divided equally into two injections per day. Controls consisting of appropriate buffers as well as human serum albumin had no effect on trypanosome populations. Animals receiving lysozyme exhibited a weight loss of 5% 24 hours following the first injection, but not other ill effects of the treatment were observed. In vitro experiments indicated that lysozyme did not cause lysis or immobilization alone or in combination with fibrinogen or rat antitrypanosomal serum. These results suggest that the cellular immune response of the host and lysozyme's cationic properties may be important in mediating the anti-trypanosomal response. Lysozyme may thus be an effective trypanocide against trypanosomes whose membranes resemble T. lewisi, such as T. cruzi, or as an adjunct to chemotherapy.
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PMID:Effects of lysozyme on Trypanosoma lewisi. 39 64

Ion-exchange derivatives are described. of a hydrophilic rigid macroporous glycolmethacrylate gel called Spheron, suitable for rapid high-performance liquid chromatography (HPLC) of proteins and their fragments. Their flow parameters are compared with those of ion exchange derivatives of cellulose and polydextran. The conditions for work with them are described (regeneration, cycling, equilibration, column packing) as well as the construction of a simple apparatus for medium-pressure ion exchange chromatography of proteins. The efficiency of these ion exchangers for the separation of proteins is illustrated with examples of chromatography of an artificial mixture of serum albumin, chymotrypsinogen and lysozyme. Chromatography of cyanogen bromide fragments of serum albumin and the A and B chains of oxidized insulin showed that the method can be applied in chromatography on higher molecular protein fragments. A review of all proteins, including technical enzymes, which have already been chromatographed on Spheron ion exchangers is also given. The prospects of Spheron ion exchangers for HPLC of proteins and their fragments are briefly discussed.
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PMID:Rapid separation of proteins and their higher-molecular fragments by means of Spheron ion-exchanges. 39 17

The second derivative absorption spectra of serum albumin, insulin, ribonuclease and lysozyme were measured under various conditions to determine the state and amount of their phenylalanine residues. The second derivative spectra of these proteins were very similar to that of phenylalanine in the region between 245 and 270 nm where tryptophan and tyrosine residues caused no appreciable interference. Denaturation of proteins with urea or guanidine hydrochloride caused decrease in the intensity of the second derivative spectra, but scarcely affected the positions of peaks and troughs. The amounts of phenylalanine residues in proteins calculated from a second derivative spectra of denatured proteins coincided well with those reported in the literature. The states of the phenylalanine residues in the proteins could be deduced from the change in optical intensity on denaturation.
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PMID:Estimation of state and amount of phenylalanine residues in proteins by second derivative spectrophotometry. 39 35

In the absence of carrier proteins, putative androgen receptors elute from DNA-cellulose in the range of 120 to 190 mM NaCl. However, in the presence of lysozyme, most of the receptor elutes in the range of 200 to 230 mM NaCl. This is the same range in which the lysozyme itself, a basic protein, elutes after being chromatographed in the same manner. Moreover, at low ionic strength, lysozyme also increases the sedimentation velocity of both androgen and estrogen receptors. In contrast, bovine serum albumin neither adheres to DNA-cellulose nor alters the sedimentation properties of these proteins. The lysozyme effects can account for some discrepancies reported in the literature. Thus, for qualitative elution studies, the use of lysozyme as a carrier protein is not advised, although its direct interaction with receptors might facilitate quantitative fractionation.
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PMID:Carrier protein effects on DNA-cellulose chromatography of putative steroid receptors. 44 27


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