Characterization of gangliosides of porcine erythrocyte membranes: Occurrence of ganglioside GD3 as major ganglioside

Lipids ◽  
1985 ◽  
Vol 20 (9) ◽  
pp. 588-593 ◽  
Author(s):  
Yasuo Suzuki ◽  
Naoto Suzuki ◽  
Hiroyasu Michi ◽  
Makoto Matsumoto
Keyword(s):  
Erythrocyte Membranes ◽  
Ganglioside Gd3 ◽  
Major Ganglioside ◽  
Porcine Erythrocyte

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

Erratum to “Ganglioside characterization of a cell line displaying motor neuron-like phenotype: GM2 as a possible major ganglioside in motor neurons”

1995 ◽  
Vol 134 (1-2) ◽  
pp. 219-220
Author(s):  
Akiko Matsumoto ◽  
Hiide Yoshino ◽  
Nobuhiro Yuki ◽  
Yukichi Hara ◽  
Neil R. Cashman ◽  
...  
Keyword(s):  
Motor Neuron ◽  
Cell Line ◽  
Motor Neurons ◽  
A Cell ◽  
Major Ganglioside
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