scholarly journals The reaction of penicillin with proteins

1975 ◽  
Vol 149 (2) ◽  
pp. 357-364 ◽  
Author(s):  
P H Corran ◽  
S G Waley
Keyword(s):  
Egg White ◽  
Amino Group ◽  
Neutral Solution ◽  
Egg White Lysozyme ◽  
Hen’S Egg ◽  
N Terminus ◽  
High Concentrations ◽  
A Chain ◽  
A Site ◽  
Hydrolysis Of

The mode of reaction of benzylpenicillin with two proteins was studied, with particular reference to the allergenicity of penicillin. These reactions, with pig insulin, and with hen's-egg-white lysozyme, were carried out in neutral solution at 37°C. High concentrations of penicillin are needed to label the proteins, owing to concurrent hydrolysis of penicillin. Evidence has been obtained that the penicillin-reactive sites on the insulin molecule are the α-amino group at the N-terminus of the A chain and the ε-amino group of the lysine residue; whereas a site of reaction with lysozyme appears to be the ε-amino group of lysine-116.

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
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