Phospholipid composition of dystrophic chicken erythrocyte plasmalemmae II. Characterization of a unique lipid from dystrophic erythrocyte membranes as ethanolamine plasmalogen

1984 ◽  
Vol 778 (1) ◽  
pp. 121-128 ◽  
Author(s):  
Mark Kester ◽  
C.A. Privitera
Keyword(s):  
Phospholipid Composition ◽  
Erythrocyte Membranes ◽  
Chicken Erythrocyte ◽  
Ethanolamine Plasmalogen ◽  
Dystrophic Chicken

Characterization of phospholipid composition of pig plasma and erythrocyte membranes

2008 ◽  
Vol 32 (S1) ◽  
pp. 115-118 ◽  
Author(s):  
G. Bruschetta ◽  
D. Alberghina ◽  
G. Nastasi ◽  
E. Rotondo ◽  
A. M. Ferlazzo
Keyword(s):  
Phospholipid Composition ◽  
Erythrocyte Membranes

scholarly journals Isolation and characterization of a membrane protein from rat erythrocytes which inhibits lysis by the membrane attack complex of rat complement

1992 ◽  
Vol 284 (1) ◽  
pp. 169-176 ◽  
Author(s):  
T R Hughes ◽  
S J Piddlesden ◽  
J D Williams ◽  
R A Harrison ◽  
B P Morgan
Keyword(s):  
Affinity Purification ◽  
Membrane Attack Complex ◽  
Erythrocyte Membranes ◽  
Dependent Manner ◽  
Inhibitory Protein ◽  
Rat Erythrocytes ◽  
Butanol Extract ◽  
Isolation And Characterization ◽  
Membrane Bound

The membrane attack complex (MAC) of complement in humans is regulated by several membrane-bound proteins; however, no such proteins have so far been described in other species. Here we report the isolation and characterization of a rat erythrocyte membrane glycoprotein of molecular mass 21 kDa which inserts into cell membranes and is a potent inhibitor of the rat MAC. This protein, here called rat inhibitory protein (RIP), was first partially purified by column chromatography from a butanol extract of rat erythrocyte membranes. Monoclonal antibodies (Mabs) were raised against RIP and used for its affinity purification. Affinity-purified RIP was shown to inhibit in a dose-dependent manner the cobra venom factor (CVF)-mediated ‘reactive’ lysis of guinea pig erythrocytes by rat complement. Conversely, the anti-RIP MAbs 6D1 and TH9 were shown to markedly enhance the CVF-mediated lysis of rat erythrocytes by rat complement. RIP acted late in the assembly of the MAC (at or after the C5b-8 stage) and was releasable from the membranes of rat erythrocytes by phosphatidylinositol-specific phospholipase C. These features, together with its size, deglycosylation pattern and N-terminal amino acid sequence, lead us to conclude that RIP is the rat homologue of the human MAC-inhibitory protein CD59 antigen.

scholarly journals Membrane glycopeptides from old and young human erythrocytes (Short Communication)

1974 ◽  
Vol 140 (3) ◽  
pp. 557-560 ◽  
Author(s):  
Cesare Balduini ◽  
Carlo Luigi Balduini ◽  
Edoardo Ascari
Keyword(s):  
Sialic Acid ◽  
Erythrocyte Membrane ◽  
Human Erythrocyte ◽  
Short Communication ◽  
Chemical Characterization ◽  
Erythrocyte Membranes ◽  
Main Peak ◽  
Human Erythrocyte Membranes ◽  
Papain Digestion

Glycopeptides were extracted by papain digestion from old and young human erythrocyte membranes and fractionated on DEAE-Sephadex A-25. Chemical characterization of the unfractionated samples and of the main peak eluted from the column indicates that glycoproteins of the erythrocyte membrane undergo significant decreases in sialic acid and galactosamine content with aging.

Characterization of the fusogenic properties of Sendai virus: kinetics of fusion with erythrocyte membranes

Biochemistry ◽  
1985 ◽  
Vol 24 (18) ◽  
pp. 4739-4745 ◽  
Author(s):  
Dick Hoekstra ◽  
Karin Klappe ◽  
Tiny De Boer ◽  
Jan Wilschut
Keyword(s):  
Sendai Virus ◽  
Erythrocyte Membranes ◽  
Kinetics Of

scholarly journals Isolation and partial characterization of high-density lipoprotein HDL1 from rat plasma by gradient centrifugation

1979 ◽  
Vol 183 (1) ◽  
pp. 83-90 ◽  
Author(s):  
L T Lusk ◽  
L F Walker ◽  
L H DuBien ◽  
G S Getz
Keyword(s):  
Gradient Centrifugation ◽  
Low Density Lipoprotein ◽  
Phospholipid Composition ◽  
Density Lipoprotein ◽  
Gel Permeation Chromatography ◽  
Rat Plasma ◽  
Density Range ◽  
Gel Permeation ◽  
Triacylglycerol Content

The lipoproteins isolated from rat plasma by flotation in the density range 1.019-1.063 g/ml were further characterized. Using rate zonal ultracentrifugation, we isolated two lipoproteins in almost equal proportions from this density range. Similar isolations may be accomplished with density gradients in a swinging-bucket rotor. On isopycnic-density-gradient ultracentrifugation one component banded at rho = 1.031 g/ml and the other at rho = 1.054 g/ml. More that 98% of the apoprotein of the lighter component was B protein, and hence this particle is LD (low-density) lipoprotein. Of the apoproteins of the rho = 1.054 g/ml particles, designated lipoprotein HDL1, over 60% was arginine-rich peptide, and the remainder was A-I, A-IV and C peptides. The molecular weight of these lipoproteins determined by agarose column chromatography was 2.36 × 10(6) for LD lipoprotein and 1.30 × 10(6) for lipoprotein HDL1. On electron microscopy the radius of LD lipoprotein was 14.0 nm and that of lipoprotein HDL1 was 10.0 nm, in contrast with molecular radii of 10.4 nm and 8.4 nm respectively determined from the gel-permeation-chromatography data. The lipid and phospholipid composition of both particles was determined. Lipoprotein HDL1 was notable for both the concentration of its esterified cholesterol, which was similar to that of LD lipoprotein, and the low triacylglycerol content, resembling that of HD lipoprotein. The possible origin of lipoprotein HDL1 is discussed.

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