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At least 163 records · Page 9Linked to original sources

Isoelectric focusing of cerebrospinal fluid proteins in the diagnosis of multiple sclerosis.

Isoelectric focusing was adapted for analysis of cerebrospinal fluid (CSF) proteins with commercially available materials. CSF from cases of multiple sclerosis or chronic neurologic infections showed abnormal populations of IgG, verified by immunofixation, particularly in the high-alkaline regions (high-alkaline bands). Agarose electrophoresis showed a similar number of abnormal specimens, but patterns were more clearly defined by isoelectric focusing. Despite increased sensitivity, isoelectric focusing is too complex to replace agarose electrophoresis, but it may be useful in clinically difficult cases when agarose electrophoresis patterns are questionable.

Central Nervous System Diseases↗

[Ventriculo-lumbar gradient of concentration of total cerebrospinal fluid proteins: 1 - mechanisms of origin].

In normal conditions there is a concentration gradient of proteins along the neuraxis. From a low level in the ventricles, ranging from 5 to 15 mg/10C ml, to an intermediate level in the cisterna magna, the protein content reaches its highest level in the lumbar sac, 12 to 44 mg/100 ml. Several mechanisms were considered to elucidate the origin of this gradient but many investigators think that the progressive increase of the protein concentration is best explained by the transfer of proteins from serum to the cerebrospinal fluid due to the relatively raised permeability of blood-cerebrospinal fluid barrier in the spinal subarachnoid space. This paper presents a study of the protein concentrations in cisternal and lumbar cerebrospinal fluid samples of patients with neurocysticercosis in activity. The 11 patients of the first group had free subarachnoid space communication between the cisterna magna and the lumbar sac; the 6 patients of the second group had a complete block of the subarachnoid space between these two levels. In every cerebrospinal fluid specimen the quantitative complement fixation test for cysticercus was performed and the titer determined in order to make an assessment of the central nervous system humoral immune response. The analysis of the data of this investigation shows that the concentration gradient of proteins is evident in the cerebrospinal fluid of patients with patency of the spinal subarachnoid space, and the ratio of concentrations of protein contents in simultaneous cisternal and lumbar samples was similar to that one observed in normal individuals. This gradient is also detected when the intensity of the humoral immune response is determined by quantitative complement fixation test for cysticercus in simultaneous cisternal and lumbar specimens. After the onset of spinal subarachnoid block, the confront of the results of the tests in cerebrospinal fluid samples, obtained before and after the blockage, shows a large increase both in the total protein content as well as the intensity of the humoral immune response, in the lumbar level. The similar increases both in protein concentration and titer of cysticercus complement fixation test in the lumbar fluid, in comparison with the cisternal fluid, in patients with patent spinal subarachnoid space, and the large simultaneous and similar increases in both protein content and titer of the cysticercus complement fixation test in the lumbar fluid of patients with spinal subarachnoid block are in disagreement with the usual explanation of the origin mechanisms of the gradient.(ABSTRACT TRUNCATED AT 400 WORDS)

Antibody Formation↗

[Value of cerebrospinal fluid protein study by the polyacrylamide gel electrophoresis method].

The methods of cerebrospinal fluid electrophoresis used as yet are surveyed briefly with particular reference to the method using polyacrylamide gel. In the light of own results it has been found that the method is superior because only small amounts of material are required and the sensitivity and separating ability of the method are much higher.

Cerebrospinal Fluid Proteins↗

Study of human cerebrospinal fluid proteins by size exclusion-high performance liquid chromatography and two-dimensional gel electrophoresis.

Cerebrospinal fluid (CSF) proteins were separated into three main fractions by size exclusion-high performance liquid chromatography (SE-HPLC). Subsequent analysis of each fraction by two-dimensional gel electrophoresis (2-DE) facilitated the detection of trace components in CSF and additionally provided more information about the native properties of various proteins. Certain proteins are present in a polymeric form and appear in the high molecular weight SE-HPLC fraction. In the middle molecular weight SE-HPLC fraction we found a CSF-specific transthyretin-related protein by immunoblotting with polyclonal antibodies to transthyretin. Possible interpolypeptide disulfide bonds of such polymeric proteins were studied using a nonreducing 2-DE system. This procedure revealed that all apolipoprotein E monomers in CSF, which are synthesized in astrocytes, are linked by disulfide bonds. In the CSF from a patient with clinically definite multiple sclerosis (MS), novel proteins appeared in the high molecular weight SE-HPLC fraction, which are obscured by other proteins if total CSF is analyzed.

Cerebrospinal Fluid Proteins↗

Polyacrylamide gel electrophoresis of cerebrospinal fluid proteins in children with nontumoral hydrocephalus.

The changes occurring in the electrophoretic pattern of the cerebrospinal fluid (CSF) proteins in 37 children with nontumoral hydrocephalus, and the protein pattern of 12 children without organic neurological disease, were studied with polyacrylamide gel electrophoresis. In nontumoral hydrocephalus protein was frequently increased in lumbar and ventricular fluid, in this condition, in intraventricular obstruction, the protein fractions showed a decrease in the prealbumin and an increase in the gamma-globulin fractions, and in extraventricular obstruction, the protein fractions showed a decrease in the prealbumin and an increase in the gamma-globulin and alpha 2-globulin fractions. With CSF proteins within normal ranges we found that in intraventricular obstruction, the proteins of the ventricular-CSF showed an increase in the prealbumin and/or albumin fractions, and in extraventricular obstruction, the proteins of the ventricular CSF showed an increase in the prealbumin and beta-globulin fractions, and the proteins of the lumbar CSF showed an increase in the prealbumin fraction. The diagnostic implications of these findings are discussed.

Albumins↗

Effect of sample preparation on cerebrospinal fluid protein patterns in polyacrylamide gels.

The method of preparing CSF and dilute serum samples for polyacrylamide gel electrophoresis has a marked effect on the pattern of the resolved proteins. The incorporation of sucrose or glycerol into the sample seriously impairs the quality of the resolution and affects the actual number of bands resolved and the relative mobility of certain proteins. The use of sucrose as an anti-convection medium in dense samples such as serum and CSF is not recommended.

Blood Protein Electrophoresis↗

An alternative method for assaying cerebrospinal fluid protein in the presence of methotrexate.

Therapeutic concentrations of methotrexate can cause significant positive interference in cerebrospinal fluid (CSF) protein values when assayed in the Du Pont aca. Conversely, our modified turbidimetric method, in which trichloroacetic acid (TCA) plus a sample blank containing dilute hydrochloric acid is used in place of TCA, exhibits little or no interference from methotrexate. This was verified by assaying solutions that contained a constant amount of protein (approximately 430 mg/L) and various amounts of methotrexate (0.0-2.3 x 10(-4) mol/L) by both the Du Pont aca and the manual turbidimetric method. As expected, the aca results showed increasing protein values with increasing methotrexate, whereas the manual method gave results approximating the expected protein value irrespective of the methotrexate concentration.

Cerebrospinal Fluid Proteins↗