This study showed that compared with transmalleolar drilling, retrograde drilling for osteochondral lesions of the talar dome can improve the arthroscopic assessment of the lesions.

The DNA fragment (3.3 kb) containing the erythromycin resistance determinant was cloned from Escherichia coli Tf481A and sequenced. Deletion and complementation analyses indicated that the expression of high-level resistance to erythromycin requires two genes, mphA and mrx, which encode macrolide 2-phosphotransferase I and an unidentified hydrophobic protein, respectively.We previously reported a new resistance phenotype with resistance to high levels of erythromycin (EM) in clinical isolate Tf481A of Escherichia coli (12). This resistance was caused by inactivation of macrolide antibiotics by macrolide 2Ј-phosphotransferase I [MPH(2Ј)I]. MPH(2Ј)I is an inducible intracellular enzyme and it inactivates macrolides with a 14-membered ring more strongly than those with a 16-membered ring (13).In this report, we describe the cloning and nucleotide sequencing of the Em r determinant. Furthermore, two genes that are required for the expression of high-level resistance to EM are identified.No transfer of the Em r determinant of E. coli Tf481A to another strain was observed by conjugation (13). By using E. coli Tf481A into which the conjugative plasmid RP1 was introduced (4), the Em r determinant was transferred to other E. coli strains by the broth mating method. Restriction analysis of plasmid RP1-EM481 in a transconjugant showed that a 21.9-kb DNA fragment had been inserted into the PstI-D fragment of RP1 (3).From RP1-EM481, we cloned the Em r determinant and obtained pTZ3509 and pTZ3519 by inserting the 4.1-kb PstI fragment and the 3.3-kb BamHI-PstI fragment into the cloning sites of pUC119 (19), respectively, (the fragments were in opposite orientations). Both plasmids conferred high-level resistance to EM and the production of MPH(2Ј)I. By digestion of pTZ3519 and pTZ3509 with exonuclease III (5), deletion derivatives of various sizes were constructed. The nucleotide sequence of the 3.3-kb BamHI-PstI fragment was determined by the dideoxy-chain termination method (15) with Bca BEST DNA polymerase (17). The full sequence of 3,267 bp is presented in Fig. 1 (Fig. 2).To determine the locations of the genes that conferred highlevel resistance to EM, we investigated the activity of MPH (2Ј)I (13) and the MIC of EM (7) for E. coli strains carrying the various deletion derivatives (Fig. 2). These results indicated that the mphA gene for MPH(2Ј)I was located in the region from nucleotide 1630 (breakpoint of ⌬436) to 2884 (breakpoint of ⌬51). ORF2 and ORF3 were located in this region in opposite orientations. The MIC (200 g/ml) for the strain carrying ⌬115 with a deletion from the 5Ј end to nucleotide 510 was much lower than the original MIC of Ͼ3,200 g/ml, despite the fact that ⌬115 contained mphA. The data suggested that some other gene was necessary for the expression of highlevel resistance to EM. A complementation analysis was performed to determine the region that encoded this gene, temporarily designated mrx. The EcoRI-HindIII fragment of ⌬436 containing mphA was subcloned into pBR322 (now called pBR⌬436), whereas th...

We have demonstrated a personal identification system that is based on near-infrared finger vein patterns. Finger vein patterns of 678 volunteers are acquired by transmitting near-infrared light through a finger and capturing the image with a CCD camera. These vein patterns are enhanced by a background-reduction filter. The similarity between two patterns is then quantified by use of the normalized maximum of the cross correlation of the two images after correction of the tilt angle. The enhanced finger vein pattern enabled 678 persons to be successfully identified.

The resistance mechanism of Escherichia coli BM2506 to macrolides was found to be due to inactivation. Inactivated oleandomycin was identified as oleandomycin 2'-phosphate by thin-layer chromatography. A new type of macrolide-phosphorylating enzyme, macrolide 2'-phosphotransferase type II (MPH(2')II), was detected, purified 95-fold and its enzymological properties investigated. MPH(2')II was a constitutive intracellular enzyme which showed high levels of activity with both 14-member-ring and 16-member-ring macrolides. The optimum pH for the inactivation of oleandomycin was 8.2 and the optimum temperature of the reaction was 40 degrees C. Enzyme activity was lost by heat treatment at 60 degrees C for 1 min. The isoelectric point and M(r) of the enzyme were 5.3 and 48,000, respectively. Purine nucleotides, such as ITP, GTP and ATP, were effective as cofactors in the inactivation of macrolides. An inhibitory effect of iodine, EDTA, or divalent cations on MPH(2')II activity was observed.

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