Brief Instructions for the Preparation of Gels and for the Electrophoretic Procedure

2011 ◽  
Keyword(s):  
Electrophoretic Procedure

scholarly journals Direct comparison of performance characteristics of two immunoassays for bone isoform of alkaline phosphatase in serum

1997 ◽  
Vol 43 (11) ◽  
pp. 2052-2057 ◽  
Author(s):  
Christopher P Price ◽  
Thomas P Milligan ◽  
Claude Darte
Keyword(s):  
Alkaline Phosphatase ◽  
Reference Range ◽  
Cross Reactivity ◽  
Performance Characteristics ◽  
Paget Disease ◽  
Specific Assay ◽  
Comparison Of Results ◽  
Immunometric Assay ◽  
Detailed Evaluation ◽  
Electrophoretic Procedure

Abstract A clinical need exists for a sensitive and specific assay for the quantitation of the bone isoform of alkaline phosphatase in serum. The majority of methods do not meet this requirement; however, the recent development of immunoassays for this isoform may provide a solution. In a detailed evaluation of two immunoassays, we found a degree of imprecision that enables the discrimination of changes within the reference range. The cross-reactivity of the liver isoform was found to be between 7.1% and 12.7% when two different methods of assessment were used. The comparison of results with an electrophoretic procedure showed that the immunocapture method recovered less of the bone isoform in samples from children than in samples from patients with Paget disease; no such difference was found with the immunometric method. This suggests that the immunocapture antibody may discriminate between different bone isoforms in children whereas the immunometric assay does not.

A Rapid Electrophoretic Method for the Determination of the Isoenzymes of Serum Lactate Dehydrogenase

1966 ◽  
Vol 12 (5) ◽  
pp. 308-313 ◽  
Author(s):  
Albert W Opher ◽  
Charles S Collier ◽  
Joseph M Miller
Keyword(s):  
Enzyme Activity ◽  
Lactate Dehydrogenase ◽  
Quantitative Determination ◽  
Serum Lactate ◽  
Serum Lactate Dehydrogenase ◽  
Electrophoretic Method ◽  
The Individual ◽  
Electrophoretic Procedure ◽  
Purple Formazan

Abstract A convenient electrophoretic procedure for the separation and quantitation of lactate dehydrogenase (LDH) isoenzymes is described. The system uses polyacetate Sepraphore III strips.* The areas of activity are shown by incubation with an LDH substrate combined with tetra-nitro-blue-tetrazolium. The reduction of the latter to the purple formazan is quantitatively related to the enzyme activity. Quantitative determination of the individual colored areas is performed by densitometry.

IDENTIFICATION OF CULTIVARS OF FORAGE LEGUME (Desmodium ovalifolium GUILL ET PERR.) BY THEIR ELECTROPHORETIC PATTERNS

1987 ◽  
Vol 67 (3) ◽  
pp. 713-717 ◽  
Author(s):  
A. HUSSAIN ◽  
W. BUSHUK ◽  
H. RAMIREZ ◽  
W. ROCA
Keyword(s):  
Gel Electrophoresis ◽  
Cultivar Identification ◽  
Polyacrylamide Gel Electrophoresis ◽  
Seed Proteins ◽  
Polyacrylamide Gel ◽  
Forage Legume ◽  
Desmodium Ovalifolium ◽  
Electrophoretic Patterns ◽  
Electrophoretic Procedure

An electrophoretic procedure was developed for discriminating cultivars of Desmodium ovalifolium on the basis of patterns of partially purified seed proteins. Electrophoresis was done on uniform 15% polycrylamide gels in basic (8.9) pH. The method produced satisfactory discrimination of eight cultivars used in its initial evaluation.Key words: Forage legume, Desmodium ovalifolium Guill et Perr., cultivar identification, polyacrylamide gel electrophoresis

Improved procedure for measuring gamma-glutamyltransferase isoenzymes in serum.

1988 ◽  
Vol 34 (2) ◽  
pp. 419-422 ◽  
Author(s):  
L Sacchetti ◽  
G Castaldo ◽  
G Fortunato ◽  
F Salvatore
Keyword(s):  
Scattered Light ◽  
Density Lipoprotein ◽  
Normal Subjects ◽  
Total Activity ◽  
Coumarin Derivative ◽  
Very Low Density Lipoproteins ◽  
Gamma Glutamyltransferase ◽  
Analytical Imprecision ◽  
Hepatobiliary Diseases ◽  
Electrophoretic Procedure

Abstract In this electrophoretic procedure for measuring isoenzymes of gamma-glutamyltransferase, patterns obtained are highly reproducible and the analytical imprecision (CV) ranges from 1.10% to 6.17%. A cellulose acetate support is used, at 220 V for 40 min. Sharply resolved isoenzyme bands were made visible by fluorescence scattered light, formed by use of a coumarin derivative as donor substrate. Two bands were observed for sera from normal subjects; four bands were variably present in sera from patients with different hepatobiliary diseases. Detection of the latter was satisfactory, down to a total activity in serum of 8-10 U/L. Three of the pathological bands were associated with low- and (or) very-low-density lipoproteins, whereas a major fraction of one of the normal bands in cirrhotic sera precipitated with high-density lipoprotein. The bands in normal sera, and one of the abnormal bands, did not.

scholarly journals Quantitative Abnormalities of Aα Chain Molecular Weight in the Fibrinogen of Cirrhotic Patients

1977 ◽  
Author(s):  
Mark Weinstein ◽  
Daniel Deykin
Keyword(s):  
Molecular Weight ◽  
Plasma Proteins ◽  
Normal Subjects ◽  
Small Samples ◽  
Two Stage ◽  
Large Pore ◽  
Total Range ◽  
Cirrhotic Patients ◽  
Electrophoretic Procedure ◽  
Molecular Weight Heterogeneity

A novel two-stage SDS gel electrophoretic procedure was devised to examine the molecular weight heterogeneity of fibrinogen in small samples of whole plasma from 12 normal and 7 cirrhotic individuals. Fibrinogen was first separated from other plasma proteins on a large pore gel, cut out of the gel, reduced, and separated into its component Aα, Bβ, and γ chains on a second gel. Two major mol wt species—fibrinogen I and II—were observed on the first gel. The ~ 25000 mol wt difference between these two forms reflected a decrease primarily in the size of one of the fibrinogen II Aα chains. In both normals and cirrhotic patients fibrinogen II comprised 30% of the total (range 20–35%). Fibrinogen I and II each contained two major high mol wt Aα chains—Aα/1 and a smaller Aα/2—that differ by 3000 mol wt. In normal fibrinogen I, Aα/2 comprised 33% of the total Aα chains (range 27–41%). In contrast the fibrinogen I of 6 out of the 7 patients had a lower per cent of Aα/2 (range 10–25%). Similar quantitative differences were seen in the decreased fraction of Aα/2 in the fibrinogen II of cirrhotic patients compared to normals. No correlation was found between per cent fibrinogen II and per cent Aα/2 in either normal subjects or cirrhotics. These results suggest that at least two independent processes are responsible for the observed levels of Aα chain heterogeneity in normals and cirrhotics and that one of these processes yields a lower than normal fraction of Aa/2 chains in the fibrinogen of cirrhotic individuals.

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