Isolation and characterization of the membrane-bound cytochrome c-554 from the thermophilic green photosynthetic bacterium Chloroflexus aurantiacus

1990 ◽  
Vol 23 (1) ◽  
pp. 29-38 ◽  
Author(s):  
John C. Freeman ◽  
Robert E. Blankenship
Keyword(s):  
Cytochrome C ◽  
Photosynthetic Bacterium ◽  
Chloroflexus Aurantiacus ◽  
Isolation And Characterization ◽  
Membrane Bound

scholarly journals Isolation and characterization of the cDNAs encoding two isoforms of subunit CIX of bovine cytochrome c oxidase.

1990 ◽  
Vol 265 (5) ◽  
pp. 2677-2681
Author(s):  
R Lightowlers ◽  
G Ewart ◽  
R Aggeler ◽  
Y Z Zhang ◽  
L Calavetta ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Isolation And Characterization

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 Isolation and Characterization of a Purple Non-Sulfur Photosynthetic Bacterium Rhodopseudomonas faecalis Strain A from Swine Sewage Wastewater

2016 ◽  
Vol 21 (1) ◽  
pp. 29-36 ◽  
Author(s):  
HONGYI WEI ◽  
SUGURU OKUNISHI ◽  
TAKESHI YOSHIKAWA ◽  
YUTO KAMEI ◽  
HIROTO MAEDA
Keyword(s):  
Photosynthetic Bacterium ◽  
Isolation And Characterization

scholarly journals Isolation and Characterization of Membrane-Bound Arylamidases from Human Placenta and Kidney

1980 ◽  
Vol 104 (1) ◽  
pp. 155-165 ◽  
Author(s):  
Kunio HIWADA ◽  
Taketoshi ITO ◽  
Masako YOKOYAMA ◽  
Tatsuo KOKUBU
Keyword(s):  
Human Placenta ◽  
Isolation And Characterization ◽  
Membrane Bound
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