About: Lysozyme is a research topic. Over the lifetime, 8773 publications have been published within this topic receiving 264505 citations. The topic is also known as: Glyco_hydro_22_lys & IPR000974.
TL;DR: Of the tested components, carvacrol and thymol decreased the intracellular ATP pool of E. coli and also inreased extracellular ATP, indicating disruptive action on the cytoplasmic membrane.
Abstract: Carvacrol, (+)-carvone, thymol, and trans-cinnamaldehyde were tested for their inhibitory activity against Escherichia coli O157:H7 and Salmonella typhimurium. In addition, their toxicity to Photobacterium leiognathi was determined, utilizing a bioluminescence assay. Their effects on the cell surface were investigated by measuring the uptake of 1-N-phenylnaphthylamine (NPN), by measuring their sensitization of bacterial suspensions toward detergents and lysozyme, and by analyzing material released from cells upon treatment by these agents. Carvacrol, thymol, and trans-cinnamaldehyde inhibited E. coli and S. typhimurium at 1-3 mM, whereas (+)-carvone was less inhibitory. trans-Cinnamaldehyde was the most inhibitory component toward P. leiognathi. Carvacrol and thymol disintegrated the outer membrane and released outer membrane-associated material from the cells to the external medium; such release by (+)-carvone or trans-cinnamaldehyde was negligible. Of the tested components, carvacrol and thymol decreased the intracellular ATP pool of E. coli and also inreased extracellular ATP, indicating disruptive action on the cytoplasmic membrane.
TL;DR: Structure of Hen Egg-White Lysozyme: A Three-dimensional Fourier Synthesis at 2 A Resolution as mentioned in this paper, 3D Fourier synthesis at 2 a resolution.
Abstract: Structure of Hen Egg-White Lysozyme: A Three-dimensional Fourier Synthesis at 2 A Resolution
TL;DR: The current understanding of different types of lysozyme and their expression and its role in fish innate immune system is reviewed.
Abstract: The innate immune system of fish is considered to be the first line of defence against a broad spectrum of pathogens and is more important for fish as compared with mammals. Lysozyme level or activity is an important index of innate immunity of fish and is ubiquitous in its distribution among living organisms. It is well documented that fish lysozyme possess lytic activity against both Gram-positive bacteria and Gram-negative bacteria. It is also known to be opsonic in nature and activates the complement system and phagocytes. It is present in mucus, lymphoid tissue, plasma and other body fluids of freshwater and marine fish. It is also expressed in a wide variety of tissues. Lysozyme activity has been shown to vary depending on the sex, age and size, season, water temperature, pH, toxicants, infections and degree of stressors. Here, we review our current understanding of different types of lysozyme and their expression and its role in fish innate immune system.
TL;DR: The 2.8 A resolution three-dimensional structure of a complex between an antigen (lysozyme) and the Fab fragment from a monoclonal antibody against lysozyme has been determined and refined by x-ray crystallographic techniques.
Abstract: The 2.8 A resolution three-dimensional structure of a complex between an antigen (lysozyme) and the Fab fragment from a monoclonal antibody against lysozyme has been determined and refined by x-ray crystallographic techniques. No conformational changes can be observed in the tertiary structure of lysozyme compared with that determined in native crystalline forms. The quaternary structure of Fab is that of an extended conformation. The antibody combining site is a rather flat surface with protuberances and depressions formed by its amino acid side chains. The antigen-antibody interface is tightly packed, with 16 lysozyme and 17 antibody residues making close contacts. The antigen contacting residues belong to two stretches of the lysozyme polypeptide chain: residues 18 to 27 and 116 to 129. All the complementarity-determining regions and two residues outside hypervariable positions of the antibody make contact with the antigen. Most of these contacts (10 residues out of 17) are made by the heavy chain, and in particular by its third complementarity-determining region. Antigen variability and antibody specificity and affinity are discussed on the basis of the determined structure.
TL;DR: The ultra-violet inactivation of lysozyme has been studied and found to conform to a first order reaction, and the relation of molecular weight to quantum yield, as well as the other findings, are discussed.