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Electrophoretic study of lipo protein fractions isolated by preparative ultra centrifugation

, : Electrophoretic study of lipo protein fractions isolated by preparative ultra centrifugation. Giornale della Arteriosclerosi 4(2): 103-114

A new methodology for the electrophoretic study of lipoprotein classes, as prepared by ultracentrifugation, is described. Sera from 61 normal and hyperlipidemic subjects were examined. Very low density lipoproteins (VLDL) change their electrophoretic mobility on cellulose acetate after isolation. LDL and high density lipoproteins after isolation migrate with the same mobility as in the total serum. Two abnormal bands are also detectable in many normolipidemic and hyperlipidemic subjects: they probably correspond to the late (slow) pre-.beta. and sinking pre-.beta. lipoprotein.

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Related references

Martin R.A.; D.L.I.lesia F.A., 1980: Rapid preparative scale isolation and quantitation of lipo protein fractions by density gradient ultra centrifugation. Clinical Chemistry 26(7): 1025

Foreman, J.R.; Karlin, J.B.; Edelstein, C.; Juhn, D.J.; Rubenstein, A.H.; Scanu, A.M., 1977: Fractionation of human serum lipo proteins by single spin gradient ultra centrifugation quantification of apo lipo protein b and apo lipo protein a i and lipid components. A sensitive and reproducible method was developed for separation of the major serum lipoproteins from 1 ml or less of human serum by isopycnic density gradient ultracentrifugation. The serum, applied to a step gradient (total volume 12.8 ml), was...

Shono T., 1982: Properties of high density lipo protein 2 and high density lipo protein 3 in normal subjects hyper lipidemics and hepatic disorders isolated by zonal ultra centrifugation. Two major subfractions of high density lipoprotein, HDL2 and HDL3 were isolated by a single zonal ultracentrifugation and subsequently analyzed for chemical composition, apoprotein content and molecular characteristics. Subjects analyzed were 4 no...

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Hallinan F.M.; Rose M.; Eagleton M.; Tempany E., 1986: Electrophoretic characterization of human parotid saliva protein fractions isolated by preparative isoelectric focusing. Human parotid saliva proteins fractionated by preparative isoelectric focusing into 3 main fractions have been characterised electrophoretically and immunochemically. The anodic proteins constitute a polymorphic family of collagenase and trypsin s...

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