[Renal cell carcinoma in a horseshoe kidney with abdominal aortic aneurysm: a case report].

We herein report a case of renal cell carcinoma in a horseshoe kidney with an abdominal aortic aneurysm in a 69-year-old man. Radiological examinations showed a left renal tumor, horseshoe kidney and abdominal aortic aneurysm. We performed a left radical nephrectomy with the division of the isthmus and artificial graft through an abdominal transperitoneal approach. Histological findings revealed clear cell type renal cell carcinoma without invasion of the capsule or renal pelvis. Only 31 cases of renal cell carcinoma in a horseshoe kidney have been reported in Japan, and our case is the 32nd. No case with abdominal aortic aneurysm has been reported previously. We assume that abdominal aortic aneurysm was associated with renal cell carcinoma by chance in the horseshoe kidney in this case. The arterial and venous supplies vary from case to case. We emphasize that arteriography and venography are very important preoperative procedures.

Purification and characterization of a novel metal-containing nonheme bromoperoxidase from Pseudomonas putida.

A novel bromoperoxidase was purified to homogeneity from the bacterium Pseudomonas putida IF-3 strain, which produces the antibiotic pyrrolnitrin. The enzyme had a molecular mass of 68,000 and was composed of two identical subunits (33,000). It was specific for I- and Br- and inactive toward Cl- and F- in the monochlorodimedone assay system. The optimum pH of the enzyme was around 4.2 and it rapidly lost its activity below 3.5, but it was stable over of range pH of 4 to 11. The purified enzyme was activated several fold by incubation with only cobalt ions, and did not contain an organic prosthetic group such as heme, flavin and cobalamin. Analyses of prosthetic metal compounds in the enzyme using plasma atomic emission spectroscopy (ICP-AES) combined with mass-spectroscopy (MS) and trace metal determination by high performance liquid chromatography (HPLC)-spectrometry, revealed that the enzyme contained 0.35 +/- 0.1 mol of cobalt ions, 1.0 +/- 0.2 mol of nickel ions, 0.8 +/- 0.2 mol of zinc ions and 2.0 +/- 0.2 mol of ferric iron per mol of enzyme, assuming the molecular weight of 68,000. There was no trace of vanadium in the enzyme, unlike in some nonheme haloperoxidases. Thus the bromoperoxidase of P. putida is a novel nonheme metal-containing bromoperoxidase.

Efficient transformation of pseudomonas strains with pNI vectors by electroporation.

The optimum conditions for electro-transformation of some Pseudomonas strains including P. putida, P. fluorescens, and P. flavida, were defined using the pNI105 vector, resulting in 100-10,000 fold increases in transformation efficiency compared with conventional chemical transformation with MgCl2. The growth phase of the cultured cells and the field strength were important in obtaining high transformation efficiency. Under optimal conditions, 3.2 x 10(7) transformants per 1 microgram DNA were obtained using a combination of pNI105 and P. fluorescens IAM12022. This value is the highest ever obtained for a Pseudomonas species. In addition, the procedures were applicable to the effective transformation of fluorescent Pseudomonas strains with pNI vectors.

Oxidation of aniline to nitrobenzene by nonheme bromoperoxidase.

Nonheme bromoperoxidase found in Pseudomonas putida catalyzed the bromination of aniline with hydrogen peroxide and bromide ions to give o- and p-bromoanilines. However, in the absence of bromide ions, it oxidized aniline via azobenzene and azoxybenzene finally into nitrobenzene. This is the first report of the biological oxidation of an arylamine to the corresponding nitrocompound at the enzyme level. In addition, nitrobenzene was not formed by a nonheme bromoperoxidase from Corallina pilulifera (marine alga), implying that the alga enzyme has a different reaction mechanism.