Watt-level single-frequency tapered amplifier laser using a narrowband interference filter.

We demonstrate a tunable external cavity tapered amplifier laser (ECTAL) using a narrowband interference filter as the wavelength discriminator. The laser is tunable over a wavelength range from 1006 to 1031 nm with an output power of ∼1 W. The amplified stimulated emission of the laser system is suppressed to better than 32 dB. The laser is applied to study the saturation spectroscopy on the R(39) 57-0 line of iodine molecule, which, to our best knowledge, is the first measurement of this line close to the dissociation limit. The linewidth of the a1 component is ∼2 MHz at the iodine vapor pressure of ∼11 Pa, and the pressure-broadening coefficient is ∼156 kHz/Pa. This laser system is also used for the injection seeding of a 1030 nm disk laser to perform hyperfine spectroscopy of muonic hydrogen. To reach a satisfactory condition for disk laser use, the ECTAL is successfully stabilized to the iodine Doppler-free spectroscopy of the P(26) 43-0 line near 515 nm, with continuous locking over 48 h.

Functional importance of apolipoprotein A5 185G in the activation of lipoprotein lipase.

BACKGROUND: Apolipoprotein A5 (APOA5) over-expression enhances lipolysis of triglyceride (TG) through stimulation of lipoprotein lipase (LPL) activity; however, an APOA5 G185C variant was found associated with hypertriglyceridemia. The aim of this study was, therefore, to explore the importance of APOA5 185GG in the activation of LPL. METHODS: A fragment containing mature human APOA5 cDNA was obtained by RT-PCR and subcloned into pET-15b vector. Site-directed mutagenesis was performed to generate 19 variants. Recombinant human APOA5 wild type and variants were produced in Escherichia coli, and then activation of LPL was measured. RESULTS: Activity of APOA5 variants on LPL-mediated 1,2-dimyristoyl-sn-glycero-3-phosphocholine hydrolysis was reduced by 17 to 74% in comparison to wild type APOA5 (P<0.0001). All variants also showed reduced activation (P<0.0001) of LPL-mediated hydrolysis of very low-density lipoprotein (VLDL); activation abilities of APOA5 variants ranged from 31 to 81% of wild-type APOA5. CONCLUSIONS: APOA5 residue 185G is very important in LPL-mediated VLDL hydrolysis, and any mutation at this residue will decrease LPL activation and concomitant TG modulation.