Isolation of pure LpB from human serum.

Zechner, Rudolf; Moser, Renate; Kostner, Gerhard M.

doi:10.1016/s0022-2275(20)38807-6

Cited by 22 publications

(5 citation statements)

References 14 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In the first set of experiments we studied the influence of purified LCAT, derived from pig and human plasma, on pig HDL, human HDL-3, pig LDL-1, pig LDL-2, human LDL, and Lp(a). Since apoC proteins are known to modulate the LCAT activity (Soutar et al, 1975;Albers et al, 1979), in some cases human LDL were depleted from apoC polypeptides by incubation with phospholipid-poor lipofundin (Zechner et al, 1986) prior to incubation with LCAT. Removal of apoC from pig LDL by incubation with lipofundin was also tried but was incomplete.…”

Section: Resultsmentioning

confidence: 99%

“…Since the LDL fractions from pig and human plasma still contained small amounts of apoA-I, apoC, and apoE, in some cases pig and human LDL fractions were incubated with IgG fractions prepared from antisera against pig or human apoA-I (Knipping et al, 1975;Kostner & Alaupovic, 1972) and from antiserum against apoE (Kostner, 1982). ApoC polypeptides of human LDL were removed by incubation of 2 mL of 4% human LDL with equal volumes of phospholipid-poor lipofundin (10%) (Braun Melsungen AG) for 1 h at 37 °C (Zechner et al, 1986). After treatment with IgG or lipofundin all LDL fractions were again spun in the TFT-41 rotor under the same conditions as above.…”

Section: Methodsmentioning

confidence: 99%

See 1 more Smart Citation

Studies on the substrate specificity of human and pig lecithin:cholesterol acyltransferase: role of low-density lipoproteins

Knipping¹,

Birchbauer²,

Steyrer³

et al. 1986

Biochemistry

View full text Add to dashboard Cite

The substrate properties of low-density lipoprotein (LDL) fractions from human and pig plasma and of lipoprotein a [Lp(a)] upon incubation with either pig or human lecithin:cholesterol acyltransferase (LCAT, EC 2.3.1.43) were investigated and compared with those of pig high-density lipoproteins (HDL) or human HDL-3. The cholesterol esterification using purified native pig LDL-1, human LDL, or Lp(a) as a substrate was approximately 36-42% that of pig HDL or human HDL-3, while cholesteryl ester formation with pig LDL-2 was 41-47%. No significant difference was found in the substrate activity between pig HDL and human HDL-3, and between human LDL and Lp(a), respectively. After depletion of pig LDL-1, pig LDL-2, and human LDL from apolipoprotein A-I (apoA-I), cholesteryl ester formation decreased to about 22-28% of the value found with pig HDL. Depletion of human LDL from apolipoprotein E (apoE) did not result in significantly different esterification rates in comparison to native LDL. Total removal of non-apoB proteins from human LDL resulted in esterification rates of approximately 10-15% that of HDL. Readdition of apoA-I to all these LDL fractions produced solely in apoA-I-depleted LDL fractions an increase of cholesteryl ester formation, whereas in those LDL fractions that were additionally depleted from apoE and/or from apoC polypeptides, a further decrease in the esterification rate occurred.(ABSTRACT TRUNCATED AT 250 WORDS)

show abstract

Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Studies on the substrate specificity of human and pig lecithin:cholesterol acyltransferase: role of low-density lipoproteins

Knipping¹,

Birchbauer²,

Steyrer³

et al. 1986

Biochemistry

View full text Add to dashboard Cite

show abstract

“…Transfer was done at 150 V and 0.4 A for 1.5 h with cooling at 4 'C. Afterwards antigens were identified with a doubleantibody technique involving monospecific antiserum against /J2-G-I prepared in our own laboratory as described previously [17] and IgG coupled to horseradish peroxidase (Bio-Trade) with 4-chloro-1-naphthol (Sigma) as substrate [18]. Tryptic peptide mapping Tryptic peptide mapping was performed by the method of Cleveland et al [19].…”

Section: Immunoblottingmentioning

confidence: 99%

Characterization of isoelectric subspecies of asialo-β2-glycoprotein I

Gries

Nimpf

Wurm

et al. 1989

Biochemical Journal

Self Cite

View full text Add to dashboard Cite

Isoelectric focusing of purified beta 2-glycoprotein I (beta 2-G-I) revealed five major bands with isoelectric points (pI) between 5.1 and 6.1. Neuraminidase treatment decreased the number of bands to two (pI 8.0 and 8.2). The two asialo subfractions of beta 2-G-I were purified by cation-exchange column chromatography. The more basic isoform II was found to have a higher content of lysine. Western-blot analysis of different plasma samples confirmed the heterogeneity of beta 2-G-I in plasma. Plasma treated with neuraminidase showed two bands irrespective of the number of isoforms as well as of the concentration in native plasma. This led us to the conclusion that human plasma beta 2-G-I consists of two isoproteins that are sialylated to different extents.

show abstract

“…A variety of assays exist to determine or purify cholesterol subfractions. New modifications have recently been described and evaluated: HDL (337)(338)(339)(340)(341)(342)(343)(344), VLDL (341), LDL (341,345,346), Lp(X) (347). There are three major methods to quantitate concentrations of apolipoproteins (303,304,348,349): chromatography, isoelectric focusing and immunoassays.…”

Section: Analytes Of Clinical Interestmentioning

confidence: 99%