scholarly journals Identification by Mutagenesis of a Conserved Glutamate (Glu487) Residue Important for Catalytic Activity in Rat Liver Carnitine Palmitoyltransferase II

2002 ◽  
Vol 277 (44) ◽  
pp. 42219-42223 ◽  
Author(s):  
Guolu Zheng ◽  
Jia Dai ◽  
Gebre Woldegiorgis
Keyword(s):  
Catalytic Activity ◽  
Rat Liver ◽  
Carnitine Palmitoyltransferase ◽  
Carnitine Palmitoyltransferase Ii

scholarly journals Over-expression and characterization of active recombinant rat liver carnitine palmitoyltransferase II using baculovirus

1995 ◽  
Vol 309 (2) ◽  
pp. 689-693 ◽  
Author(s):  
T M Johnson ◽  
W R Mann ◽  
C J Dragland ◽  
R C Anderson ◽  
G M Nemecek ◽  
...  
Keyword(s):  
Rat Liver ◽  
Large Scale ◽  
Insect Cells ◽  
Specific Activity ◽  
Recombinant Baculovirus ◽  
Cell System ◽  
Carnitine Palmitoyltransferase ◽  
Sds Page ◽  
Infected Insect ◽  
Carnitine Palmitoyltransferase Ii

The cDNA encoding rat liver carnitine palmitoyltransferase II (CPT-II) was heterologously expressed using a recombinant baculovirus/insect cell system. Unlike Escherichia coli, the baculovirus-infected insect cells expressed mostly soluble active recombinant CPT-II (rCPT-II). CPT activity from crude lysates of recombinant baculovirus-infected insect cells was maximal between 50 and 72 h post-infection, with a peak specific activity of 100-200 times that found in the mock- or wild-type-infected control lysates. Milligram quantities (up to 1.8 mg/l of culture) of active rCPT-II were chromatographically purified from large-scale cultures of insect cells infected with the recombinant baculovirus. The rCPT-II was found to be: (1) similar in size to the native rat liver enzyme (approximately 70 kDa) as judged by SDS/PAGE; (2) immunoreactive with a polyclonal serum raised against rat liver CPT-II; and (3) not glycosylated. Kinetic analysis of soluble rCPT-II revealed Km values for carnitine and palmitoyl-CoA of 950 +/- 27 microM and 34 +/- 5.6 microM respectively.

Eritadenines - Novel type of potent inhibitors of S-adenosyl-L-homocysteine hydrolase

1982 ◽  
Vol 47 (1) ◽  
pp. 167-172 ◽  
Author(s):  
Ivan Votruba ◽  
Antonín Holý
Keyword(s):  
Catalytic Activity ◽  
Rat Liver ◽  
Hydrolytic Reaction

Rat liver SAH-hydrolase is strongly inhibited by four stereoisomeric 4-(adenin-9-yl)-2,3-dihydroxybutyric acids (eritadenines). D-Eritadenine, which is the most effective of the four, inactivates the catalytic activity of SAH-hydrolase at IC50 = 1.2 .10-8 mol l-1 in the hydrolytic reaction. The enzyme is irreversibly inhibited (τ/2 = 1.6 min). The inactivation activity decreases in the order D-erythro(2R, 3R) L-erythro(2S, 3S) threo(2S, 3R) threo(2R, 3S) configuration.

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