Ultracytochemical localization and characterization of membrane-bound ATPases in lateral buds from intact and decapitated plants of an aquatic fern,Marsilea drummondii A. Br.

PROTOPLASMA ◽  
1985 ◽  
Vol 127 (3) ◽  
pp. 180-191 ◽  
Author(s):  
L. Sossountzov ◽  
Y. Habricot
Keyword(s):  
Aquatic Fern ◽  
Lateral Buds ◽  
Membrane Bound

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.

Characterization of soluble vs membrane-bound human placental 5′-nucleotidase

1990 ◽  
Vol 172 (3) ◽  
pp. 1371-1377 ◽  
Author(s):  
Mary R. Klemens ◽  
William R. Sherman ◽  
Nels J. Holmberg ◽  
Julie M. Ruedi ◽  
Martin G. Low ◽  
...  
Keyword(s):  
Membrane Bound

scholarly journals Structural characterization of membrane-bound human immunodeficiency virus-1 Gag matrix with neutron reflectometry

2017 ◽  
Vol 12 (2) ◽  
pp. 02D408 ◽  
Author(s):  
Rebecca Eells ◽  
Marilia Barros ◽  
Kerry M. Scott ◽  
Ioannis Karageorgos ◽  
Frank Heinrich ◽  
...  
Keyword(s):  
Human Immunodeficiency Virus ◽  
Structural Characterization ◽  
Neutron Reflectometry ◽  
Immunodeficiency Virus ◽  
Membrane Bound ◽  
Human Immunodeficiency Virus 1

Detection and Characterization of Membrane-Bound Selenoproteins in the Kidney of the Rat

2002 ◽  
Vol 973 (1) ◽  
pp. 289-292 ◽  
Author(s):  
A. KYRIAKOPOULOS ◽  
H. BERTELSMANN ◽  
A. GRAEBERT ◽  
B. HOPPE ◽  
M. KÜHBACHER ◽  
...  
Keyword(s):  
Membrane Bound

scholarly journals Molecular characterization of structural genes coding for a membrane bound hydrogenase in Methylococcus capsulatus (Bath)

2001 ◽  
Vol 205 (2) ◽  
pp. 203-207 ◽  
Author(s):  
R. Csáki ◽  
T. Hanczár ◽  
L. Bodrossy ◽  
J.C. Murrell ◽  
K.L. Kovács
Keyword(s):  
Molecular Characterization ◽  
Methylococcus Capsulatus ◽  
Structural Genes ◽  
Membrane Bound
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