Disease relevance of LYZ1

• Lysozyme activity was determined via lysis of Micrococcus lysodeicticus [1].
• The growth of an organism involved in cheese-making, Lactococcus lactis, was not affected by the presence of lysozyme in milk [2].

High impact information on LYZ1

• Lysozyme was glycated by glucose or methylglyoxal in the presence of different concentrations of aged garlic extract or S-allyl cysteine with subsequent analysis of glycation-derived crosslinking using SDS-PAGE [3].
• Amadori-rich protein was prepared by dialysing lysozyme that had been glycated by ribose for 24 h [3].
• This ribated lysozyme was reincubated and the effects of aged garlic extract, S-allyl cysteine and pyridoxamine on glycation-induced crosslinking was monitored [3].
• For the first time, this newly improved method was employed to study the diffusion of protein (bovine serum albumin (BSA) and lysozyme) in agarose hydrogel at body temperature (37 degrees C) [4].
• Chromosomal fluorescence in situ hybridization of a cocktail of lysozyme genomic clones localized the lysozyme gene cluster to cattle Chr 5 band 23, corroborating the somatic cell assignment [5].

Biological context of LYZ1

• The analysis revealed three RFLP loci designated LYZ1, LYZ2 and LYZ2 [6].
• By two-dimensional pulsed-field gel electrophoresis the lysozyme genes on cattle Chr 5 were shown to be clustered on a 2- to 3-Mb DNA fragment, while the lactalbumin gene and pseudogenes that are paralogous and syntenic with the lysozymes were outside the lysozyme gene cluster [5].
• In this work, we investigate the diffusion kinetics of biomolecules, such as bovine serum albumin, interferon, and lysozyme, through microfabricated silicon membranes, having pores of nanometric size in only one dimension, in the range from few to tens of nanometers (the other dimensions are in the mum range) [7].
• The mRNA expression of the inflammatory factors tumor necrosis factor-alpha, interleukin-1beta, cyclooxygenase-2, lactoferrin, and lysozyme was measured via real-time, quantitative reverse transcription PCR [8].

Anatomical context of LYZ1

• Influence of different restorative materials on lysozyme and amylase activity of the salivary pellicle in situ [1].

Associations of LYZ1 with chemical compounds

• Three model proteins, bovine serum albumin, hen's egg lysozyme and bovine serum fibrinogen, were adsorbed from aqueous solution onto finely dispersed ceramic particles, namely different kinds of alumina and hydroxyapatite particles [9].
• Influences of animal mucins on lysozyme activity in solution and on hydroxyapatite surfaces [10].
• A variety of crowding agents were used including haemoglobin, lysozyme, various dextrans and polyethylene glycol [11].
• The amounts of negatively charged bovine serum albumin and positively charged lysozyme adsorbed on alumina, silica, titania, and zirconia particles (diameters 73 to 271 nm) in aqueous suspensions are measured [12].

Analytical, diagnostic and therapeutic context of LYZ1

• METHODS: FTIR is used to determine the melting temperature (T(m (FTIR))) of various proteins, such as bovine serum albumin (BSA), immunoglobulin (IgG1), beta-lactoglobulin (beta-LG), and lysozyme (HEWL), at different protein concentrations (5-100 mg/mL), where four data interpretation methods are discussed [13].
• The interaction of antibodies (Abs) with protein antigens (Ags) of different size, such as hen egg white lysozyme, ovalbumin, and bovine serum albumin, was examined using analytical ultracentrifugation, electrospray ionization time-of-flight mass spectrometry, and surface plasmon resonance in order to estimate regional and segmental Ab flexibility [14].

References