نتایج جستجو برای: hen egg white lysozyme

تعداد نتایج: 230888  

Journal: :basic and clinical neuroscience 0
hassan ramshini department of biology, payam noor university, p. o. box: 19395-3697, tehran, iran. azadeh ebrahim-habibi tehran university of medical sciences (tums) shariati hospital, north kargar avenue tehran , 1411413137,iran sima aryanejad department of biology, payam noor university, p. o. box: 19395-3697, tehran, iran. abolfazl rad p.o.box 319, sabzevar university of medical sciences, sabzevar, iran

introduction: diagnosing and treating diseases associated with amyloid fibers remain a great challenge despite of intensive research carried out. one important approach in the development of therapeutics is the use of herbal extracts which are rich in aromatic small molecules. cinnamomum verum extract (ce) contains proanthocyanidin and cinnamaldehyde, which have been suggested to be capable of ...

Journal: :Antibody reports 2022

The recombinant antibodies AG275, AG294 and AG274 detect the hen egg-white lysozyme by ELISA.

Journal: :Infection and immunity 1982
R S Rosenthal J K Blundell H R Perkins

Peptidoglycan from Neisseria gonorrhoeae RD5 was completely degraded by hen egg white lysozyme and was not extensively O-acetylated. In contrast, peptidoglycans from gonococcal strains FA19 and FA102 (a penicillin-resistant mutant derived from FA19), were markedly resistant to digestion by hen egg white lysozyme and were extensively O-acetylated.

2005
Haruhiko Koizumi Masaru Tachibana Kenichi Kojima Irena Wolska Dorota Maciejewska

Proton tautomerism is a general phenomenon in organic molecules and plays a vital role in many fields of chemistry and biochemistry. The tautomerism of salicylideneanilines [eq(1)] has attracted a considerable attention because it is closely related to thermoand photochromism. Salicylideneanilines greatly favor the enol form over the cis-keto form in the gas phase. We demonstrate here that the ...

Journal: :The Journal of biological chemistry 1997
R Kuroki Y Ito Y Kato T Imoto

A mutant hen egg white lysozyme, D52E, was designed to correspond to the structure of the mutant T4 lysozyme T26E (Kuroki, R., Weaver, L. H., and Matthews B. W. (1993) Science 262, 2030-2033) to investigate the role of the catalytic residue on the alpha-side of the saccharide in these enzymes. The D52E mutant forms a covalent enzyme-substrate adduct, which was detected by electron ion spray mas...

Journal: :The Journal of biological chemistry 1992
I Kumagai F Sunada S Takeda K Miura

On the basis of the molecular evolution of hen egg white, human, and turkey lysozymes, three replacements (Trp62 with Tyr, Asn37 with Gly, and Asp101 with Gly) were introduced into the active-site cleft of hen egg white lysozyme by site-directed mutagenesis. The replacement of Trp62 with Tyr led to enhanced bacteriolytic activity at pH 6.2 and a lower binding constant for chitotriose. The fluor...

Journal: :Nanoscale 2021

A Hf-based NU-1000 metal organic framework as a hydrolytic nanozyme for peptide bonds in dipeptides and hen egg white lysozyme protein showed greater stability better recyclability than previous Zr-/Hf-based nanozymes.

Journal: :Chembiochem : a European journal of chemical biology 2015
Tom Z Yuan Callum F G Ormonde Stephan T Kudlacek Sameeran Kunche Joshua N Smith William A Brown Kaitlin M Pugliese Tivoli J Olsen Mariam Iftikhar Colin L Raston Gregory A Weiss

Recombinant protein overexpression of large proteins in bacteria often results in insoluble and misfolded proteins directed to inclusion bodies. We report the application of shear stress in micrometer-wide, thin fluid films to refold boiled hen egg white lysozyme, recombinant hen egg white lysozyme, and recombinant caveolin-1. Furthermore, the approach allowed refolding of a much larger protein...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 2007
Chantal Abergel Vincent Monchois Deborah Byrne Sabine Chenivesse Frédérique Lembo Jean-Claude Lazzaroni Jean-Michel Claverie

Part of an ancestral bactericidal system, vertebrate C-type lysozyme targets the peptidoglycan moiety of bacterial cell walls. We report the crystal structure of a protein inhibitor of C-type lysozyme, the Escherichia coli Ivy protein, alone and in complex with hen egg white lysozyme. Ivy exhibits a novel fold in which a protruding five-residue loop appears essential to its inhibitory effect. T...

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