Oligosaccharides containing Glucose as Substrates for Hen's Egg White Lysozyme

Nature ◽  
1968 ◽  
Vol 219 (5159) ◽  
pp. 1152-1154 ◽  
Author(s):  
URI ZEHAVI ◽  
JERRY J. POLLOCK ◽  
VIVIAN I. TEICHBERG ◽  
NATHAN SHARON
Keyword(s):  
Egg White ◽  
Egg White Lysozyme ◽  
Hen’S Egg

scholarly journals SERUM AND URINARY LYSOZYME (MURAMIDASE) IN MONOCYTIC AND MONOMYELOCYTIC LEUKEMIA

1966 ◽  
Vol 124 (5) ◽  
pp. 921-952 ◽  
Author(s):  
Elliott F. Osserman ◽  
Dolores P. Lawlor
Keyword(s):  
Biological Fluids ◽  
Agar Plate ◽  
Egg White ◽  
Small Samples ◽  
Plate Method ◽  
Egg White Lysozyme ◽  
Human Enzyme ◽  
Hen’S Egg ◽  
Sole Product ◽  
Serum And Urine

Markedly increased quantities of lysozyme have been found in the serum and urine (ranging to 2.6 g per day) of ten consecutive cases of monocytic and monomyelocytic leukemia. The enzyme has been isolated from the urine of several cases and physicochemically and immunochemically characterized. It is apparently identical to the lysozyme of normal tears, saliva, leukocytes, and serum, but structurally different from the lysozyme of hen's egg white. The activity of the human enzyme assayed with M. lysodeikticus organisms is 3 to 12 times greater than egg white lysozyme at equivalent concentrations. An agar plate method has been developed for quantitating lysozyme activity in small samples (approximately 25 µl) of serum, urine, or other biological fluids. The range and reproducibility of this method were found to be superior to previously available lysozyme assay procedures. Present evidence indicates that lysozyme is the principal, if not the sole, product of the proliferating monocytes in monocytic and monomyelocytic leukemia, and quantitation of serum and urine lysozyme should be a useful diagnostic procedure for these leukemias.

scholarly journals The precise and entire antigenic structure of native lysozyme

1978 ◽  
Vol 171 (2) ◽  
pp. 429-434 ◽  
Author(s):  
M Z Atassi ◽  
C L Lee
Keyword(s):  
Egg White ◽  
Antigenic Structure ◽  
Egg White Lysozyme ◽  
Antigenic Sites ◽  
Exact Boundary ◽  
Hen’S Egg ◽  
Antigenic Reactivity

The exact boundary, residue, conformational and directional definitions of the three antigenic sites of native hen's egg-white lysozyme are described. The results clearly reveal that the three antigenic sites account quantitatively for the total antigenic reactivity of the protein. Thus the entire antigenic structure of lysozyme has now been precisely determined and is briefly discussed here, together with the power of the surface-stimulation synthetic concept.

The disulfide bridges of hen's egg-white lysozyme☆

1965 ◽  
Vol 107 (1) ◽  
pp. 97-111 ◽  
Author(s):  
J JAUREGUIADELL ◽  
J JOLLES ◽  
P JOLLES
Keyword(s):  
Egg White ◽  
Disulfide Bridges ◽  
Egg White Lysozyme ◽  
Hen’S Egg

Detection of hen’s egg white lysozyme in food: Comparison between a sensitive HPLC and a commercial ELISA method

2010 ◽  
Vol 120 (2) ◽  
pp. 580-584 ◽  
Author(s):  
Barbara Kerkaert ◽  
Frédéric Mestdagh ◽  
Bruno De Meulenaer
Keyword(s):  
Egg White ◽  
Elisa Method ◽  
Egg White Lysozyme ◽  
Hen’S Egg

scholarly journals The purification, composition and specificity of wheat-germ agglutinin

1973 ◽  
Vol 131 (1) ◽  
pp. 155-162 ◽  
Author(s):  
A. K. Allen ◽  
A. Neuberger ◽  
N. Sharon
Keyword(s):  
Binding Site ◽  
Wheat Germ Agglutinin ◽  
Wheat Germ ◽  
Egg White ◽  
Exchange Chromatography ◽  
Hydroxyl Group ◽  
Anomeric Configuration ◽  
Egg White Lysozyme ◽  
Hen’S Egg ◽  
Derivatives Of

1. The purification of wheat-germ agglutinin from commercial wheat germ is described. By ion-exchange chromatography three active proteins (isolectins) were separated, one of which was examined in detail. 2. The amino acid composition is unusual, as 20% of residues are half-cystine and 21% are glycine. Unlike most lectins and contrary to previous reports, this protein is not a glycoprotein. 3. The efficiency of various saccharides as inhibitors of the agglutination reaction was investigated and from this the specificity of the binding site was inferred. Of monosaccharides, only derivatives of glucose with a 2-acetamido group and a free 3-hydroxyl group are effective inhibitors, and glycosides of either anomeric configuration are bound. Oligosaccharides are much more powerful inhibitors of agglutination than are monosaccharides. 4. It is proposed that the binding site consists of three or four subsites with differing specificities, in a cleft in the molecule resembling that proposed for hen's-egg-white lysozyme.

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