scholarly journals Glycosylated hemoglobin A2 components

Blood ◽  
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

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.

scholarly journals Glycosylated hemoglobin A2 components

Blood ◽  
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.

Quantitiative determination of glycosylated hemoglobin A1 by agar gel electrophoresis.

1980 ◽  
Vol 26 (11) ◽  
pp. 1598-1602 ◽  
Author(s):  
L Menard ◽  
M E Dempsey ◽  
L A Blankstein ◽  
H Aleyassine ◽  
M Wacks ◽  
...  
Keyword(s):  
Gel Electrophoresis ◽  
Glycosylated Hemoglobin ◽  
Agar Gel ◽  
Hemoglobin A1 ◽  
Agar Gel Electrophoresis

scholarly journals Hemoglobin Hope: A Beta Chain Variant

Blood ◽  
1965 ◽  
Vol 25 (5) ◽  
pp. 830-838 ◽  
Author(s):  
VIRGINIA MINNICH ◽  
ROBERT J. HILL ◽  
PHILIP D. KHURI ◽  
MARY E. ANDERSON
Keyword(s):  
Blood Cells ◽  
Gel Electrophoresis ◽  
Starch Gel Electrophoresis ◽  
Beta Chain ◽  
Agar Gel ◽  
Hemoglobin A ◽  
Abnormal Hemoglobin ◽  
Starch Gel ◽  
Agar Gel Electrophoresis ◽  
Chain Variant

Abstract A new hemoglobin, hemoglobin Hope, with a beta chain abnormality has been found in three generations of a St. Louis Negro family. The abnormal hemoglobin in the heterozygous state caused neither clinical stigmata nor abnormality in the red blood cells. Hemoglobin Hope was detected by agar gel electrophoresis at pH 6.2, but could not be differentiated from hemoglobin A by starch block electrophoresis at pH 8.6. Also, it could not be separated from hemoglobin A by paper, or starch gel electrophoresis employing a range of buffers from pH 6.2 to 8.6. Amino acid analysis showed that aspartic acid was substituted for glycine at position 136 of the beta chain. Hemoglobin Hope may be formulated as α2Aβ2136 gly-asp.

Purification of Human Urokinase and its Topographical Localisation in Renal Parenchyma

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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