Isoelectric focusing of gamma globulins in cerebrospinal fluid from patients with multiple sclerosis.

1977 ◽  
Vol 23 (12) ◽  
pp. 2213-2215 ◽  
Author(s):  
J L Trotter ◽  
G Banks ◽  
P Wang

Abstract The technique of isoelectric focusing has been adapted for rapid clinical analysis for globulins in cerebrospinal fluid with use of commercially prepared horizontal-slab acrylamide gels. The globulin fraction is concentrated by ammonium sulfate precipitation, which allows more of the relevant protein to be applied, use of a wider range of total protein concentrations, and higher resolution than is true for previously described methods. Critical variables include a constant concentration and volume of IgG, a constant low temperature of the acrylamide gel, and sensitive staining with Coomassie Brilliant Blue G-250. The apparatus used is adaptable for other electrophoretic procedures in the clinical laboratory, and the use of commercially prepared gel slabs is more convenient, more reproducible, and requires less time than other methods.

1978 ◽  
Vol 24 (11) ◽  
pp. 1931-1933 ◽  
Author(s):  
J A Johnson ◽  
H A Lott

Abstract Coomassie Brilliant Blue G-250 can be used to quantitatively determine proteins in cerebrospinal fluid. When the dye combines with protein, the absorption maximum of the dye shifts. The dye-protein color forms almost instantaneously and is stable for at least 1 h. The procedure is also insensitive to changes in temperature in the range of 20--30 degrees C. The absorptivities of the dye complexes with human albumin or globulin differ, thus a pure albumin or pure globulin standard is unsuitable; a standard containing 70% albumin and 30% globulins is the most appropriate for this application. A bichromatic approach to standardization increases the range of linearity of a calibration curve. The method gives values that are about 9% higher than a sodium sulfate-sulfosalicylic turbidimetric procedure for cerbrospinal fluid proteins.


1991 ◽  
Vol 65 (1) ◽  
pp. 62-66
Author(s):  
S. M. A. Abidi ◽  
W. A. Nizami

ABSTRACTThe protein content of fresh homogenates and their corresponding TCA precipitated fractions of 10 different species of helminths was estimated by the methods of Lowry et al. and Spector using the Folin phenol reagent and Coomassie brilliant blue G-250 respectively. The former method gives exaggerated values as compared to the latter method. The parasite phenols, phenolic proteins and catecholamines could be responsible for interference in the Lowry's procedure. The TCA non-precipitable moieties also give colour only with the Folin phenol assay. The pronounced intra-specific differences in the total protein content of helminths reflect their metabolic variations and adaptations. Habitat does not appear to influence the protein content of parasites, however, the effect of host variation was evident in the pouched amphistome G. crumenifer. It is concluded that the dye binding method gives more consistent results and it can be conveniently applied to crude tissue homogenates of helminths.


1973 ◽  
Vol 56 (2) ◽  
pp. 245-NP ◽  
Author(s):  
P. G. SALUJA ◽  
M. GRONOW ◽  
J. M. HAMILTON

SUMMARY Isoelectric focusing in polyacrylamide gel followed by staining with Coomassie brilliant blue was used for the densitometric estimation of ovine prolactin standard and canine pituitary prolactin. The results were compared with those obtained by conventional polyacrylamide gel electrophoretic procedures and isoelectric focusing was found to be a valid technique for the estimation of prolactin and to offer greater technical convenience. The mobility of ovine and canine prolactin was similar in isoelectric focusing and gel electrophoresis. The isoelectric point of ovine and canine prolactin was found to be 6·17 and 6·61 respectively. Constant levels of prolactin were found in the pituitaries of bitches at oestrus.


1981 ◽  
Vol 113 (1) ◽  
pp. 197-201 ◽  
Author(s):  
Kiyoko Sano ◽  
Kiyoko Kanamori ◽  
Akihiko Shiba ◽  
Makoto Nakao

Sign in / Sign up

Export Citation Format

Share Document