Comparison of agar gel electrophoresis and isoelectric focusing in multiple sclerosis and subacute sclerosing panencephalitis

Abstract Partially purified hemoglobin A2 has been examined for the existence of glycosylated components by isoelectric focusing and by acid agar gel electrophoresis. Bands analogous to the glycohemoglobin derivatives of hemoglobin A, hemoglobin-A1.a.b.c, were readily detected. Evidence that these minor bands are in fact glycohemoglobins was obtained by showing that 14C-glucose bound to hemoglobin A2 moved with these minor bands. The amounts of glycohemoglobin derivatives of hemoglobin A2 were increased in the blood of diabetic patients.

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Glycosylated hemoglobin A2 components

Blood ◽

10.1182/blood.v56.3.571.bloodjournal563571 ◽

1980 ◽

Vol 56 (3) ◽

pp. 571-572

Author(s):

C Tegos ◽

E Beutler

Keyword(s):

Isoelectric Focusing ◽

Gel Electrophoresis ◽

Glycosylated Hemoglobin ◽

Diabetic Patients ◽

Agar Gel ◽

Hemoglobin A ◽

Hemoglobin A1 ◽

Agar Gel Electrophoresis ◽

Derivatives Of ◽

Hemoglobin A2

Partially purified hemoglobin A2 has been examined for the existence of glycosylated components by isoelectric focusing and by acid agar gel electrophoresis. Bands analogous to the glycohemoglobin derivatives of hemoglobin A, hemoglobin-A1.a.b.c, were readily detected. Evidence that these minor bands are in fact glycohemoglobins was obtained by showing that 14C-glucose bound to hemoglobin A2 moved with these minor bands. The amounts of glycohemoglobin derivatives of hemoglobin A2 were increased in the blood of diabetic patients.

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HbA1 determination by agar gel electrophoresis after elimination of labile HbA1: a comparison with ion-exchange chromatography

Scandinavian Journal of Clinical and Laboratory Investigation ◽

10.3109/00365518209168046 ◽

1982 ◽

Vol 42 (1) ◽

pp. 27-33 ◽

Cited By ~ 11

Author(s):

Knut Dahl-Jørgensen ◽

Anne Elise Larsen

Keyword(s):

Ion Exchange ◽

Gel Electrophoresis ◽

Ion Exchange Chromatography ◽

Exchange Chromatography ◽

Agar Gel ◽

Agar Gel Electrophoresis

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Purification of Human Urokinase and its Topographical Localisation in Renal Parenchyma

10.1055/s-0039-1689144 ◽

1975 ◽

Author(s):

K. Andrassy ◽

E. Ritz ◽

U. Bleyl ◽

R. Egbring

Keyword(s):

Molecular Weight ◽

Isoelectric Focusing ◽

Gel Electrophoresis ◽

Serum Proteins ◽

Renal Tissue ◽

Clot Lysis ◽

Agar Gel ◽

High Molecular Weight Complex ◽

Zone Electrophoresis ◽

Human Serum Proteins

Urokinase Leo was separated by agar zone electrophoresis into an anodic and cathodic fraction. The cathodic fraction, isolated from agar gel by ultracentrifugation, showed two precipitation bands with rabbit Urokinase antibodies. Band I displayed main Urokinase activity, in band II Urokinase was present in a high molecular weight complex with human serum proteins (albumin, a2-macroglobulin, a2HS glycoprotein); with affinity chromatography further separation of Urokinase isoenzymes from serum proteins was possible. The isoelectric point of these two Urokinase isoenzymes were pH 6.8 and pH 8.7 respectively in preliminary results with isoelectric focusing. Purification steps were controlled by disc gel electrophoresis and immunological techniques (Ouchterlony technique, Immunoelectrophoresis, clot lysis test with Urokinase antibodies).Topographic localisation of Urokinase in renal tissue, investigated with antibodies against Urokinase isoenzymes, revealed Urokinase activity both in the iuxtamedullary region (V. arcuatae, V. interlobulares, less V. recta) and in calyceal epithelia of the renal pelvis.

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