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.

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 binding of platinum hexahalides (Cl, Br and I) to hen egg-white lysozyme and the chemical transformation of the PtI6octahedral complex to a PtI3moiety bound to His15

2014 ◽  
Vol 70 (9) ◽  
pp. 1132-1134 ◽  
Author(s):  
Simon W. M. Tanley ◽  
Laurina-Victoria Starkey ◽  
Lucinda Lamplough ◽  
Surasek Kaenket ◽  
John R. Helliwell
Keyword(s):  
Heavy Atom ◽  
Egg White ◽  
Hen Egg White Lysozyme ◽  
Egg White Lysozyme ◽  
Density Maps ◽  
Square Planar ◽  
Chemical Behaviour ◽  
Hen Egg White ◽  
Derivatives Of ◽  
Hen Egg

This study examines the binding and chemical stability of the platinum hexahalides K2PtCl6, K2PtBr6and K2PtI6when soaked into pre-grown hen egg-white lysozyme (HEWL) crystals as the protein host. Direct comparison of the iodo complex with the chloro and bromo complexes shows that the iodo complex is partly chemically transformed to a square-planar PtI3complex bound to the Nδatom of His15, a chemical behaviour that is not exhibited by the chloro or bromo complexes. Each complex does, however, bind to HEWL in its octahedral form either at one site (PtI6) or at two sites (PtBr6and PtCl6). As heavy-atom derivatives of a protein, the octahedral shape of the hexahalides could be helpful in cases of difficult-to-interpret electron-density maps as they would be recognisable `objects'.

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
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