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)

Natural-abundance nitrogen-15 nuclear magnetic resonance spectroscopy of enzymes and other biopolymers is found to be feasible using newly available instrumentation. The long correlation times of such molecules result in short spin-lattice relaxation times, and these in turn allow rapid signal accumulation. The advantages of short T1 values are sometimes offset, however, by unfavorable nuclear Overhauser effects. The dependence of T1 and nuclear Overhauser effects upon correlation time is discussed, and preliminary nitrogen-15 nuclear magnetic resonance results for several biopolymers, including lysozyme, protamines, pepsin, hemoglobin, vitamin B 12, and tRNA, are presented.
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PMID:Applications of natural-abundance nitrogen-15 nuclear magnetic resonance to large biochemically important molecules. 110 97

Infrared absorption spectroscopy has been used to study the effect of organic solvents on the conformation of myoglobin, apomyoglobin, hemoglobin, lysozyme and ribonuclease. Beta structure can easily be induced by specific solvent effects. Films prepared from a 50% (v/v) mixture of alcohol, acetone, pyridine, tetrahydrofuran or dimethylsulfoxide/water mixtures show a high proportion of beta structure. The degree of induction of beta structure depends on the hydrocarbon content of the alcohol in the order methanol greater than ethanol greater than butanol. No beta structure was observed in films prepared from aqueous octanol solutions. Lyophilization tends to decrease secondary structure. The conformation of the proteins depends on the particular solvent system and the solvent composition. Solution studies of myoglobin in pure dimethylsulfoxide show that the conformation is a mixture of random and beta forms while in dimethylsulfoxide/2H2O mixtures the conformation is a mixture of alpha-helical and beta forms.
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PMID:Infrared spectroscopic studies of solvent-induced conformational changes in globular proteins. 114 18

The entropy of the amino acid sequences coded by DNA is considered as a measure of diversity of variety of proteins, and is taken as a measure of evolution. The DNA or m-RNA sequence is considered as a stationary second-order Markov chain composed of four kinds of bases. Because of the biased nature of the genetic code table, increase of entropy of amino acid sequences is possible with biased nucleotide sequence. Thus the biased DNA base composition and the extreme rarity of the base doublet CpG of higher organisms are explained. It is expected that the amino acid composition was highly biased at the days of the origin of the genetic code table, and the more frequent amino acids have tended to get rarer, and the rarer ones more frequent. This tendency is observed in the evolution of hemoglobin, cytochrome C, fibrinopeptide, immunoglobulin and lysozyme, and protein as a whole.
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PMID:Entropy of the genetic information and evolution. 115 81

Under defined conditions, in the presence of 10 mg/ml of bovine serum albumin, cauda epididymal rat spermatozoa displayed vigorous motility, and a high proportion (81%) of eggs were fertilized. In contrast, no fertilization was observed after omission of albumin, or replacement of the protein by 10 mg/ml of cytochrome c, beta-globulin, gamma-globulin, hemoglobin, lysozyme, and polyvinylpyrrolidone, and 5 mg/ml of ribonuclease. However, high motility occurred in suspensions containing 3 x 10(6) spermatozoa/0.1 ml of medium with cytochrome c, beta-globulin, or gamma-globulin. In medium with 1 mg/ml of ovalbumin, 7% (2/29) eggs were fertilized. Use of defatted albumin resulted in a higher rate of fertilization than unmodified albumin (87 vs 70%), and this difference approached statistical significance. No fertilization was obtained in the presence of albumin presaturated with cholesterol. These results suggest that: (a) rat sperm cells failed to capacitate in the absence of albumin; (b) the protein exerted more than a nonspecific macromolecular effect; and (c) lipids associated with albumin may modify its ability to promote sperm capacitation.
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PMID:Influence of serum albumin on the fertilizing ability in vitro of rat spermatozoa. 125 Aug 65

A method of semiempirical identification of structural domains is proposed. The procedure is based on the comparison of amino acid sequences in groups of homologous proteins. This approach was tested using 32 known protein sequences from different cytochrome b5, cytochrome c, lysozyme, hemoglobin, and myoglobin proteins. The method presented was able to identify all structural domains of these reference proteins. A consensus secondary structure provided information on structural content of these domains predicting correctly 21 of 23 (91%) of alpha-helices. We applied this method to six homologous phytochrome sequences from Avena, Arabadopsis, Cucurbita, Maize, Oryza, and Pisum. Some of the identified domains can be assigned to the known tertiary structure categories. For example, an alpha/beta domain is localized in the region known to stabilize the phytochrome chromophore in the red light absorbing form (Pr). One alpha-helical and one alpha/beta domains are localized in regions important for the chromophore stabilization in the far-red absorbing form (Pfr). From an analysis of noncovalent interaction patterns in another domain it is proposed that a phytochrome dimer contact involves two segments localized between residues 730 and 821 (using numbering of aligned sequences). Also, a possible antiparallel beta-sheet structure of this region has been suggested. According to this model, the long axis of the interacting structures is perpendicular to a twofold symmetry axis of the phytochrome dimer.
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PMID:Structural domains of phytochrome deduced from homologies in amino acid sequences. 132 84

Data are presented on the influence of prophylactic vitamin administration to schoolchildren in two schools on their health. The morbidity rate significantly decreased, the levels of lysozyme in the saliva, hemoglobin in the blood and total protein in the blood serum rose in the children who received multivitamin "Undevitum" during 5-7 months, as compared to those who were not given the vitamins. Vitamin administration did not influence the physical development of schoolchildren.
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PMID:[Effects of prophylactic vitamin administration to Tallin's schoolchildren on their health and physical development]. 151 72

A new enzyme catalyzing the deamidation of seed storage proteins was found in germinating wheat grains and was partially purified. It also acts on egg lysozyme, horse hemoglobin and reduced RNAse, glutamine and Gly-L-Gln-L-Tyr. No activity was observed when using ovalbumin, serum albumin, RNAse, insulin, asparagine and an asparagine-containing peptide. Only glutaminyl residues appear to be deamidated by this enzyme. It differs from transglutaminase and proved to be a true protein deamidase.
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PMID:Protein deamidase from germinating wheat grains. 163 50

The antigen which has alpha 2-globulin mobility was identified immunochemically in leukolysate and pus extract. This antigen was localized in polymorphonuclear leukocytes by the immunofluorescence technique in the blood of healthy donors. The alpha 2-globulin of granulocytes (alpha 2GG) is not identical to lactoferrin, lysozyme, granulocyte elastase, fibronectin, fetal hemoglobin, amyloid P-component of the serum. The molecular mass of alpha 2GG is equal to 50 +/- 8 Kd. in the pus extract. The biological role of alpha 2GG is unknown.
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PMID:[Immunochemical identification and physico-chemical characteristics of specific alpha 2 globulin of human granulocytes]. 169 38

Of the interactions that govern protein adsorption on polymer surfaces, solvation interactions (repulsive hydration and attractive hydrophobic interactions) are thought to be among the most important. The solvation interactions in protein adsorption, however, have not been dealt with in theoretical calculation of the adsorption energy owing to the difficulties in modelling such interactions. We have evaluated the solvation interaction energies using the fragment constant method of calculating the partition coefficients of amino acids. The fundamental assumption of this approach is that the partition coefficients of amino acids between water and organic solvent phases are related to the free energies of transfer from bulk water to the polymer surface. The X-ray crystallographic protein structures of lysozyme, trypsin, immunoglobulin Fab, and hemoglobin from the Brookhaven Protein Data Bank were used. The model polymer surfaces were polystyrene, polypropylene, polyethylene, poly(hydroxyethyl methacrylate) [poly(HEMA)], and poly(vinyl alcohol). All possible adsorption orientations of the proteins were simulated to study the effect of protein orientation on the solvation interactions. Protein adsorption on either hydrophobic or hydrophilic polymer surfaces was examined by considering the sum of solvation and other interaction energies. The results showed that the contribution of the solvation interaction to the total protein adsorption energy was significant. The average solvation interaction energy ranged from -259.1 to -74.1 kJ/mol for the four proteins on the hydrophobic polymer surfaces, such as polystyrene, polypropylene, and polyethylene. On the other hand, the average solvation interaction energies on hydrophilic surfaces such as poly(HEMA) and poly(vinyl alcohol) were larger than zero. This indicates that repulsive hydration interactions are in effect for protein adsorption on hydrophilic polymer surfaces. The total interaction energies of the proteins with hydrophobic surfaces were always lower than those with more hydrophilic surfaces. This trend is in agreement with the experimental observations in the literature. This study suggests that consideration of the solvation interaction energies is necessary for accurate calculation of the protein adsorption energies.
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PMID:Calculation of solvation interaction energies for protein adsorption on polymer surfaces. 176 35

When assayed in vitro, the activity of the photosynthetic enzyme ribulose 1,5 bisphosphate carboxylase oxygenase is both enhanced and protected from spontaneous decay by exogenous proteins such as hemoglobin, serum albumin, and aldolase. Other proteins and amino acids tested are either ineffective (lysozyme, ferritin, lysine, and cysteine) or afford only partial protection (catalase, glycine, and phenylalanine). Protective proteins do not bind to, or exchange disulfides with, ribulose 1.5 bisphosphate carboxylase/oxygenase. Since their effect can be mimicked by reductively treated detergents such as Triton X-100, it appears that proteins protect from decay by quenching the spontaneous oxidative degradation and inhibiting surface adsorption which could lead to enzyme unfolding. Release of adsorbed molecules from the container surface is likely to be the cause of carboxylase activity enhancement.
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PMID:Protection and enhancement of ribulose 1,5 bisphosphate carboxylase activity by exogenous proteins. 191 Apr 60


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