Reproducibility of IntraLASIK Flap Thickness Measured with Optical Coherence Tomography

PURPOSE: To investigate the relationship among optical coherence tomography (OCT), ultrasound pachymetry, and Orbscan in central corneal thickness measurement and to evaluate the reproducibility of flap thickness using an IntraLase femtosecond laser. METHODS: Central corneal thickness was measured by OCT, ultrasound pachymetry, and Orbscan in 59 eyes of 30 patients before LASIK. After IntraLASIK, the corneal flap thickness measured using OCT was compared with the intended corneal flap thickness. RESULTS: Central corneal thickness measured by OCT was thinner than that measured by other instruments preoperatively, but there was no significant difference among these methods (p>0.01), and corneal thickness values obtained by ultrasound pachymetry and Orbscan correlated well with those obtained by OCT (r ranged from 0.804 to 0.889, p0.01). CONCLUSIONS: OCT is a relatively accurate instrument for measuring corneal thickness and can easily measure the corneal flap thickness after LASIK. Compared with the results of a previous study, the mean measured flap thickness in this study was more reproducible with the IntraLase femtosecond laser.

Cysteine carboxyl O-methylation of human placental 23 kDa protein

C-Terminal carboxyl methylation of a human placental 23 kDa protein catalyzed by membrane-associated methyltransferase has been investigated. The 23 kDa protein substrate methylated was partially purified by DEAE-Sephacel, hydroxyapatite and Sephadex G-100 gel filtration chromatographies. The substrate protein was eluted on Sephadex G-100 gel filtration chromatography as a protein of about 29 kDa. In the absence of Mg2+, the methylation was stimulated by guanine nucleotides (GTP, GDP and GTPgammaS), but in the presence of Mg2+, only GTPgammaS stimulated the methylation which was similar to the effect on the G25K/rhoGDI complex. AFC, an inhibitor of C-terminal carboxyl methylation, inhibited the methylation of human placental 23 kDa protein. These results suggests that the substrate is a small G protein different from the G25K and is methylated on C-terminal isoprenylated cysteine residue. This was also confirmed by vapor phase analysis. The methylated substrate protein was redistributed to membrane after in vitro methylation, suggesting that the methylation of this protein is important for the redistribution of the 23 kDa small G protein for its putative role in intracellular signaling.