Influence of oleic acid on serum lipoprotein-X in vitro.

1977 ◽  
Vol 23 (12) ◽  
pp. 2302-2305 ◽  
Author(s):  
T J Muckle ◽  
J A Edwards ◽  
P Auckland
Keyword(s):  
Oleic Acid ◽  
Electrophoretic Mobility ◽  
Gel Electrophoresis ◽  
Serum Lipoprotein ◽  
Specific Antiserum ◽  
Agar Gel ◽  
Precipitation Technique ◽  
Agar Gel Electrophoresis

Abstract Lipoprotein-X is no longer detectable in serum by either the agar gel-electrophoresis/polyanion precipitation technique or immunoelectrophoresis with specific antiserum after in vitro addition of oleic acid. Evidence is presented which indicates that this ostensible loss is due not to its destruction, but rather to altered electrophoretic mobility. The findings suggest an explanation for the well known post-heparin "disappearance" of lipoprotein-X, and indicate that caution may be needed in the interpretation of such lipoprotein-X testing of sera from subjects with increased concentrations of lysolipids in their blood.

Acceleration of hemoglobin C crystallization by hemoglobin S

Blood ◽  
1989 ◽  
Vol 74 (5) ◽  
pp. 1823-1825
Author(s):  
MJ Lin ◽  
RL Nagel ◽  
RE Hirsch
Keyword(s):  
Gel Electrophoresis ◽  
Phosphate Buffer ◽  
Potassium Phosphate ◽  
Potassium Phosphate Buffer ◽  
Time Intervals ◽  
Agar Gel ◽  
Hemoglobin C ◽  
Agar Gel Electrophoresis ◽  
Over Time

We previously reported that circulating hemoglobin (Hb) CC erythrocytes contain oxygenated HbC crystals with little or no HbF and that HbF inhibits in vitro crystallization of HbC. We now report that HbS accelerates in vitro crystallization of HbC. Crystals were formed in 1.8 mol/L potassium phosphate buffer, pH 7.4, at 30 degrees C and were counted in several time intervals with a hematocytometer. The hemoglobin composition of Millipore-isolated crystals and supernatant were also analyzed. Under the conditions selected, 100% HbS formed needle-shaped crystals only after two hours. Pure HbC does not form crystals within 15 minutes, whereas a ratio of 10% HbS:90% HbC forms 1,100 crystals/mm3, 20% HbS:80% HbC forms 370 crystals/mm3, and 30% HbS:70% HbC forms 5 crystals/mm3. Crystals formed in the presence of HbS are tetragonal, as are pure HbC crystals. As compared with 100% HbC, HbA or albumin mixed with HbC showed a decreased number of crystals as a result of dilution. Analysis of the Hb content of isolated crystals by citrate agar gel electrophoresis showed that HbS was rapidly incorporated into the crystal in the same ratio over time. These results demonstrate that HbS accelerates crystallization of HbC with respect to the rates of crystallization of any of these two Hbs separately, through a mechanism that involves cocrystallization. These results may be significant in understanding SC disease.

scholarly journals Acceleration of hemoglobin C crystallization by hemoglobin S

Blood ◽  
1989 ◽  
Vol 74 (5) ◽  
pp. 1823-1825 ◽  
Author(s):  
MJ Lin ◽  
RL Nagel ◽  
RE Hirsch
Keyword(s):  
Gel Electrophoresis ◽  
Phosphate Buffer ◽  
Potassium Phosphate ◽  
Potassium Phosphate Buffer ◽  
Time Intervals ◽  
Agar Gel ◽  
Hemoglobin C ◽  
Agar Gel Electrophoresis ◽  
Over Time

Abstract We previously reported that circulating hemoglobin (Hb) CC erythrocytes contain oxygenated HbC crystals with little or no HbF and that HbF inhibits in vitro crystallization of HbC. We now report that HbS accelerates in vitro crystallization of HbC. Crystals were formed in 1.8 mol/L potassium phosphate buffer, pH 7.4, at 30 degrees C and were counted in several time intervals with a hematocytometer. The hemoglobin composition of Millipore-isolated crystals and supernatant were also analyzed. Under the conditions selected, 100% HbS formed needle-shaped crystals only after two hours. Pure HbC does not form crystals within 15 minutes, whereas a ratio of 10% HbS:90% HbC forms 1,100 crystals/mm3, 20% HbS:80% HbC forms 370 crystals/mm3, and 30% HbS:70% HbC forms 5 crystals/mm3. Crystals formed in the presence of HbS are tetragonal, as are pure HbC crystals. As compared with 100% HbC, HbA or albumin mixed with HbC showed a decreased number of crystals as a result of dilution. Analysis of the Hb content of isolated crystals by citrate agar gel electrophoresis showed that HbS was rapidly incorporated into the crystal in the same ratio over time. These results demonstrate that HbS accelerates crystallization of HbC with respect to the rates of crystallization of any of these two Hbs separately, through a mechanism that involves cocrystallization. These results may be significant in understanding SC disease.

POLYETHYLENE GLYCOL ON AGAR-GEL ELECTROPHORESIS

The Lancet ◽  
1974 ◽  
Vol 304 (7892) ◽  
pp. 1321-1322
Author(s):  
W.H. Taylor ◽  
D.J. Etherington
Keyword(s):  
Polyethylene Glycol ◽  
Gel Electrophoresis ◽  
Agar Gel ◽  
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.

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