Display Settings:

Items per page
We are sorry, but NCBI web applications do not support your browser and may not function properly. More information

Results: 6

1.
Fig 5

Fig 5. From: Phytophthora infestans Cholinephosphotransferase with Substrate Specificity for Very-Long-Chain Polyunsaturated Fatty Acids.

Kinetic analysis of PiCPT1. Data are means ± SE from three biological replicates. The kinetic constants were estimated from a Michaelis-Menten plot using the averages of triplicate measurements with GraphPad Prism 6 software.

Yan Chen, et al. Appl Environ Microbiol. 2013 March;79(5):1573-1579.
2.
Fig 4

Fig 4. From: Phytophthora infestans Cholinephosphotransferase with Substrate Specificity for Very-Long-Chain Polyunsaturated Fatty Acids.

Substrate specificity of PiCPT1 for different DAGs. Values are means ± standard errors (SE) from three biological replicates. Seven DAGs (di16:0, di16:1, di18:0, di18:1, di18:2, 18:0/20:4, and 18:0/22:6) were used in in vitro CPT assays.

Yan Chen, et al. Appl Environ Microbiol. 2013 March;79(5):1573-1579.
3.
Fig 1

Fig 1. From: Phytophthora infestans Cholinephosphotransferase with Substrate Specificity for Very-Long-Chain Polyunsaturated Fatty Acids.

Alignment of putative PiCPTs, PiEPT from P. infestans, and ScCPT1 and cEPT1 from S. cerevisiae. The GenBank accession numbers of the protein sequences are as follows: ScCPT1, AAA63571; ScEPT1, AAA63572; PiCPT1, XM_002900684; PiCPT2, XM_002997893; PiEPT, XM_002907680. The conserved CDP-alcohol phosphotransferase motif is underlined. Regions of the protein sequences that are highly conserved among the sequences are shown by black boxes.

Yan Chen, et al. Appl Environ Microbiol. 2013 March;79(5):1573-1579.
4.
Fig 2

Fig 2. From: Phytophthora infestans Cholinephosphotransferase with Substrate Specificity for Very-Long-Chain Polyunsaturated Fatty Acids.

Kyte-Doolittle hydropathy plots of PiCPT1. Protscale was used to determine the hydrophobic profile of the polypeptide based on Kyte-Doolittle parameters (47). Window size was set at 19. Peaks greater than 1.5 indicate the presence of hydrophobic domains. The conserved CDP-alcohol phosphotransferase motif is located in the hydrophilic region (*), close to the second hydrophobic domain.

Yan Chen, et al. Appl Environ Microbiol. 2013 March;79(5):1573-1579.
5.
Fig 6

Fig 6. From: Phytophthora infestans Cholinephosphotransferase with Substrate Specificity for Very-Long-Chain Polyunsaturated Fatty Acids.

Transcript levels of PiCPT1 in P. infestans cultured in the presence of exogenous fatty acids. Values are the means for three replicates ± SE. cDNA from the biomass not fed with any fatty acid was used as a negative control. Values followed by a different letter (a, b, c, or d) are significantly different according to a Duncan hypothetical test (P < 0.01).

Yan Chen, et al. Appl Environ Microbiol. 2013 March;79(5):1573-1579.
6.
Fig 3

Fig 3. From: Phytophthora infestans Cholinephosphotransferase with Substrate Specificity for Very-Long-Chain Polyunsaturated Fatty Acids.

TLC plates showing the radioactive lipids in the CPT and EPT assays. Substrates used in this experiment were di18:1 DAG and [14C]CDP-choline or [14C]CDP-ethanolamine. Lipids were separated in TLC plates with chloroform-methanol-water (65:25:4, vol/vol/vol/). Lanes: control, DBY747-ΔCPTEPT with empty vector (negative control); PiCPT1, DBY747-ΔCPTEPT with PiCPT1; ScCPT1, DBY747-ΔCPTEPT with ScCPT1 (positive control in the CPT assay); ScEPT1, DBY747-ΔCPTEPT with ScEPT1 (positive control in the EPT assay). The 200-μl reaction mixture contained 600 μM 1,2-dioleoyl-sn-glycerol (di18:1 DAG) and 4.05 μM [14C]CDP-choline or [14C]CDP-ethanolamine with 50 μg of microsomal proteins. The reaction mixture was incubated at 23°C for 15 min. The original picture was generated by the program Win-Scan 2D105. The picture was then manipulated from standard color to gray scale using Corel Paint Shop Pro X.

Yan Chen, et al. Appl Environ Microbiol. 2013 March;79(5):1573-1579.

Display Settings:

Items per page

Supplemental Content

Recent activity

Your browsing activity is empty.

Activity recording is turned off.

Turn recording back on

See more...
Write to the Help Desk