CDPcholine:1,2-diacylglycerol cholinephosphotransferase from rat liver microsomes. I. Solubilization and characterization of the partially purified enzyme and the possible existence of an endogenous inhibitor

Lipids ◽  
1993 ◽  
Vol 28 (2) ◽  
pp. 89-96 ◽  
Author(s):  
Kozo Ishidate ◽  
Ritsuko Matsuo ◽  
Yasuo Nakazawa
Keyword(s):  
Rat Liver ◽  
Liver Microsomes ◽  
Rat Liver Microsomes ◽  
Endogenous Inhibitor

scholarly journals In Vitro Characterization of Borneol Metabolites by GC--MS Upon Incubation with Rat Liver Microsomes

2008 ◽  
Vol 46 (5) ◽  
pp. 419-423 ◽  
Author(s):  
R. Zhang ◽  
C.-h. Liu ◽  
T.-l. Huang ◽  
N.-s. Wang ◽  
S.-q. Mi
Keyword(s):  
Rat Liver ◽  
Liver Microsomes ◽  
Rat Liver Microsomes ◽  
In Vitro Characterization

scholarly journals Characterization of solubilized insulin receptors from rat liver microsomes. Existence of two receptor species with different binding properties

1986 ◽  
Vol 154 (2) ◽  
pp. 281-287 ◽  
Author(s):  
Rudiger KOCH ◽  
Arno DEGER ◽  
Hans-Martin JACK ◽  
Karl-Norbert KLOTZ ◽  
Dieter SCHENZLE ◽  
...  
Keyword(s):  
Rat Liver ◽  
Liver Microsomes ◽  
Insulin Receptors ◽  
Rat Liver Microsomes ◽  
Binding Properties

Separation and Characterization of Carboxyl-linked Glucuronides of Bile Acids in Incubation Mixture of Rat Liver Microsomes

Steroids ◽  
1998 ◽  
Vol 63 (4) ◽  
pp. 186-192 ◽  
Author(s):  
Junichi Goto ◽  
Naoaki Murao ◽  
Chifumi Nakada ◽  
Takashi Motoyama ◽  
Junji Oohashi ◽  
...  
Keyword(s):  
Bile Acids ◽  
Rat Liver ◽  
Liver Microsomes ◽  
Incubation Mixture ◽  
Rat Liver Microsomes

scholarly journals Functional reconstitution into liposomes and characterization of the carnitine transporter from rat liver microsomes

2006 ◽  
Vol 1758 (1) ◽  
pp. 124-131 ◽  
Author(s):  
Annamaria Tonazzi ◽  
Michele Galluccio ◽  
Francesca Oppedisano ◽  
Cesare Indiveri
Keyword(s):  
Rat Liver ◽  
Liver Microsomes ◽  
Rat Liver Microsomes ◽  
Carnitine Transporter

scholarly journals Characterization of the interaction between p100, a novel G-protein-related protein, and rat liver endosomes

1991 ◽  
Vol 280 (1) ◽  
pp. 171-178 ◽  
Author(s):  
L M Traub ◽  
E Shai ◽  
R Sagi-Eisenberg
Keyword(s):  
Rat Liver ◽  
Liver Microsomes ◽  
Rat Liver Microsomes ◽  
Trypsin Treatment ◽  
Putative Receptor ◽  
Microsomal Membranes ◽  
Direct Binding ◽  
Triton X ◽  
Binding Sequence

p100 is a recently identified 100 kDa protein which shares a putative receptor-binding sequence with the signal transducing G-proteins Gt and Gi. In liver, p100 immunoreactivity is distributed between the cytosolic and the microsomal fractions [Traub, Evans & Sagi-Eisenberg (1990) Biochem. J. 272, 453-458; Udrisar & Rodbell (1990) Proc. Natl. Acad. Sci. U.S.A. 87, 6321-6325]. More specifically, we have localized the membrane-associated form of p100 to an endosomal subfraction of rat liver microsomes. In this study we have investigated the nature of the interaction between p100 and microsomal membranes. p100 was located on the cytoplasmic surface of the microsomal vesicles, and could be released by treatment with 0.5 M-NaCl or 0.5 M-Tris/HCl, pH 7.0. However, p100 was not released by non-ionic detergents, such as Triton X-100. Binding of p100 to the membrane was reversible, as both membrane-released and cytosolic p100 could re-bind stripped (Tris-washed) microsomes. Soluble p100 could not, however, bind to untreated microsomes. Binding to stripped microsomes approached saturation and was inhibited by up to 60% by either heat treatment or mild trypsin treatment of the vesicles. This implies that the interaction between p100 and the microsomal vesicles involves the direct binding of p100 to vesicular proteins. This binding was regulated by both adenine and guanine nucleotides. As p100 contains a region similar to the C-terminal decapeptide of alpha i, (the alpha-subunit of Gi) and has a localization that is restricted to an endosomal subfraction, we propose that cytosolic p100 may bind to cytoplasmically exposed domains of internalized receptors. Thus, like the adaptins, p100 may be involved in the process of sorting and receptor trafficking through the endosomal compartment of the cells.

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