Radioimmunoassay for urinary lysozyme in human serum from leukemic patients.

1978 ◽  
Vol 24 (12) ◽  
pp. 2155-2157 ◽  
Author(s):  
T L Peeters ◽  
Y R Depraetere ◽  
G R Vantrappen
Keyword(s):  
Human Serum ◽  
Monocytic Leukemia ◽  
Human Lysozyme ◽  
Normal Volunteers ◽  
Separation Step ◽  
Lysozyme Concentration

Abstract We present a radioimmunoassay for lysozyme in human serum, based upon human lysozyme isolated from the urine of leukemic patients and antiserum prepared against this lysozyme in the goat. In the separation step, a second antibody is used. By properly adjusting the concentrations of unlabeled and 125I-labeled lysozyme and of the antibodies, maximal precision (SD, 0.04 mg/litre) was obtained in the range 0.00 to 2.00 mg/litre. In 20 normal volunteers the lysozyme concentration was 4.6 +/- 0.8 mg/litre (mean +/- SD), in 13 patients with monocytic leukemia 34.4 +/- 8.6 mg/litre. Correlation with lysoplate determinations was excellent in leukemic sera (r = 0.97) but was poor in normal sera (r = 0.35), possibly owing to the existence of isoenzymes.

scholarly journals Sequential metabolic expressions of the lethal process in human serum-treated Escherichia coli: role of lysozyme

1980 ◽  
Vol 28 (3) ◽  
pp. 735-745
Author(s):  
R J Martinez ◽  
S F Carroll
Keyword(s):  
Escherichia Coli ◽  
Human Serum ◽  
Membrane Integrity ◽  
Response To Treatment ◽  
Gram Negative Bacteria ◽  
Human Lysozyme ◽  
E Coli ◽  
Normal Human ◽  
Hydrolysis Of

Several metabolic parameters indicative of Escherichia coli function and integrity were kinetically examined in response to treatment with normal human serum in the presence and absence of functional human lysozyme. Specific inhibition of this enzyme in bacteriolytic and bactericidal reactions was accomplished by using purified rabbit anti-human lysozyme immunoglobulin G. Initiation of the complement-mediated alterations of cytoplasmic membrane integrity, as judged by the leakage of 86Rb from prelabeled cells or the hydrolysis of o-nitrophenyl-beta-D-galactopyranoside by a cryptic strain, was found to be independent of lysozyme action. Furthermore, inhibition of macromolecular synthesis by E. coli in response to serum treatment occurred at the same time regardless of the functional state of lysozyme. Although the rate and extent of bacteriolysis were reduced in the absence of lysozyme, the bactericidal kinetics was unaffected. These results demonstrate that the lethal events associated with the action of antibody and complement on gram-negative bacteria are independent of lysozyme, suggesting an accessory role for this enzyme in immune reactions. A possible temporal sequence of complement-induced effects occurring at the cell surface is presented.

Disposition and metabolism of the flavonoid chrysin in normal volunteers

2001 ◽  
Vol 51 (2) ◽  
pp. 143-146 ◽  
Author(s):  
T. Walle, ◽  
Y. Otake, ◽  
J. A. Brubaker, ◽  
U. K. Walle ◽  
P. V. Halushka
Keyword(s):  
Normal Volunteers

Development of a method to determine caffeine in human serum by HPLC

2015 ◽  
Vol 48 (06) ◽  
Author(s):  
C Rothammer ◽  
E Haen
Keyword(s):  
Human Serum
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