An alpha slow-moving high-density-lipoprotein subfraction in serum of a patient with radiation enteritis and peritoneal carcinosis.

1989 ◽  
Vol 35 (4) ◽  
pp. 674-678
Author(s):  
J Peynet ◽  
A Legrand ◽  
B Messing ◽  
F Thuillier ◽  
F Rousselet

Abstract An alpha slow-moving high-density-lipoprotein (HDL) subfraction was seen in a patient presenting with radiation enteritis and peritoneal carcinosis, who was given long-term cyclic parenteral nutrition. This subfraction, observed in addition to normal HDL, was precipitated with low-density lipoproteins (LDL) and very-low-density lipoproteins (VLDL) by sodium phosphotungstate-magnesium chloride. The patient's serum lipoproteins were analyzed after fractionation by density gradient ultracentrifugation. The alpha slow-moving HDL floated in the ultracentrifugation subfractions with densities ranging from 1.028 to 1.084 kg/L, and their main apolipoproteins included apolipoprotein E in addition to apolipoprotein A-I. These HDL were larger than HDL2. The pathogenesis of this unusual HDL subfraction is hypothesized.

1978 ◽  
Vol 24 (1) ◽  
pp. 161-165 ◽  
Author(s):  
R J Liedtke ◽  
B Busby ◽  
J D Batjer

Abstract The enzymatic cholesterol method used with the Du Pont aca has been modified to provide a reliable measurement of high-density lipoprotein cholesterol in serum after heparin/Mn2+ precipitation of the low- and very-low-density lipoproteins. Interference by Mn2+, equivalent to about 90 mg of cholesterol per liter, is decreased to less than 40 mg of cholesterol per liter by the presence of ethylenediaminetetraacetate (8 mmol/liter) in the diluent; the residual effect of Mn2+ is compensated by calibrating the aca with standards containing Mn2+ and heparin. With an 80-microliter sample, the sensitivity is 236 muA/mg per liter and linearity ranges from 50 to 1500 mg/liter. Average analytical recovery of cholesterol added to the high-density lipoprotein fraction was 103%. Diluted fractions give the expected results. Between-run reproducibility (CV) is 1.3 and 1.6% at 463 and 554 mg/liter. Correlation with the Lipid Research Clinics' procedure (25 samples) gave a regression line of y(aca) = 1.039x- 15, and a correlation coefficient of 0.997.


1980 ◽  
Vol 26 (9) ◽  
pp. 1275-1277 ◽  
Author(s):  
Y Yamaguchi

Abstract I describe a method for measuring high-density lipoprotein phospholipids. Magnesium chloride and dextran sulfate are used to precipitate all low-density and very-low-density lipoproteins. The supernate contains only high-density lipoproteins, the phospholipid concentration of which is determined by an enzymic method. The precision of the method (CV) is 2.35% (10 repeated assays), and the mean value for HDL-phospholipids was 1006 (SD 248) mg/L for 30 apparently healthy subjects. I used electrophoresis and enzymic color development to confirm the presence of HDL-phospholipids. Results are compared with those obtained by an ultracentrifugation method.


1979 ◽  
Vol 25 (7) ◽  
pp. 1309-1313 ◽  
Author(s):  
C Mayfield ◽  
G R Warnick ◽  
J J Albers

Abstract Commercial heparin preparations (18 lots) from seven manufacturers were compared in the heparin-Mn2+ procedure for high-density-lipoprotein cholesterol quantitation. With normotriglyceridemic samples, 16 heparin lots, isolated from porcine intestinal mucosa, gave mean values for supernatant cholesterol that did not differ statistically; all were within 7 mg/L. Two heparin preparations from bovine lung gave results that were slightly (16 mg/L, average) but significantly (p less than 0.005) lower. With hypertriglyceridemic samples, we observed greater variation in supernatant cholesterol among the heparin preparations, which was ascribable to variable sedimentation by centrifugation of very-low-density and low-density lipoproteins precipitated by heparin-Mn2+ treatment. If the precipitated lipoproteins were completely removed by an ultrafiltration procedure, we saw no significant difference among the heparin preparations for results with hypertriglyceridemic samples.


Author(s):  
Catherine J Briggs ◽  
Deborah Anderson ◽  
P Johnson ◽  
T Deegan

Treatment of fresh sera with polyethylene glycol 6000 at a final concentration of 100 g/l produced selective precipitation of low-density lipoproteins with only traces of contamination with high-density lipoproteins, as determined by electroimmunoassay using antisera to human α1-lipoprotein and human β-lipoprotein. Supernatants collected for high-density lipoprotein-cholesterol estimation were free from low-density lipoproteins. Precipitates sedimented readily from specimens with high triglyceride contents, and secondary precipitation during enzymatic cholesterol determinations was absent. Values obtained by this method correlated well with those obtained by precipitation of low-density lipoproteins with heparin and manganous ions at concentrations optimal for discrete separation of lipoprotein classes (r = 0·975; P<0·001).


Author(s):  
P Johnson ◽  
R A Muirhead ◽  
T Deegan

By use of an electroimmunoassay, concentrations of A-apoproteins were estimated in serum and in corresponding apoprotein fractions isolated by ultracentrifugation. These values were compared with high-density lipoprotein concentrations determined by analytical ultracentrifugation. Concentrations of A-apoproteins estimated in serum were considerably higher than in isolated high-density lipoprotein fractions. These discrepancies could not be accounted for entirely by material losses into other fractions during ultracentrifugal fractionation. No comparable differences in apoprotein-B concentrations were observed during the ultracentrifugal separation of low-density lipoprotein. Concentrations of A-apoproteins estimated in the residual serum after precipitation of low-density lipoproteins by heparin and manganous ions were also lower than in the corresponding whole sera. The discrepancies persisted after treatment of serum and isolated fractions with tetramethylurea, urea (9 mol/l), and by heating at 52°C for 3 hours. It is considered that separation by ultracentrifugation induces subtle alterations in the surface structure of the lipoprotein species which give rise to changes in immunoreactivity.


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