Methods PatientsSix cases of PAD were enrolled, all male patients: 5 cases of TAO, and 1 of ASO. All the patients had a history of intermittent claudication, rest pain, non-healing ischemic ulcers, or all three, and were not candidates for surgical revascularisation. None of the patients had responded to conventional medical therapy for at least 8 weeks. Exclusion criteria were: diabetes mellitus with proliferative retinopathy; malignant disease; recent onset (within 3 month) of myocardial infarction or brain infarction; uncontrolled myocardial ischemia; persistent severe heart failure (ejection fraction <30%); hematological disease; current serious infectious disease; aged older than 80 years; and diseases with life expectancy of less than 1 year. We

These results show that microscopic lymphatic vessel-isolated vein anastomosis is a minimally invasive operation, with good long-term effects, making it the treatment of choice for intractable secondary lymphedema of the lower extremities refractory to physiotherapy.

Two cases of necrotizing myelopathy were autopsied; one was complicated with lung carcinoma and the other with chronic type adult T cell leukemia (ATL leukemia). To our knowledge, they were the first cases of their type in Japan. In both cases, necrosis of the spinal cord was observed in the gray and white matter along most of its extent. Marked changes were found in the lumbar segment. The patients were not treated with intravenous cancer chemotherapy or irradiation. Immunohistochemical and electron microscopic examination revealed an extremely strong infection of herpes simplex virus (HSV) type 2. However, HSV type 1 and cytomegalovirus antigens were not detected.

A case of rapidly progressing ascending myelitis was necropsied. Necrosis was present throughout the whole length of the spinal cord and involved both the grey and white matter randomly. The perivascular lymphocytic infiltration in the spinal cord in the present case was more pronounced than that in the previously reported two cases of necrotizing myelopathy associated with malignancy. Using immunoperoxidase staining the presence of herpes simplex virus type 2 (HSV 2) antigen was demonstrated. Electron microscopic examinations revealed large numbers of HSV particles in the spinal cord. HSV 2 may be a common aetiological agent of necrotizing myelopathy and myelitis in Okinawa, an HSV 2 endemic area. In the present case, the necrosis was mainly found in the spinal cord but was also observed, to a very limited extent, in the brain.

The increased serum level of α-fetoprotein (AFP) in a case of renal cell carcinoma, a rare condition of AFP production by mesoderm-derived cells, was evaluated for its lectin reactivity by affinity electrophoresis, followed by the antibody-affinity transfer to nitrocellulose membranes for visualization of separated AFP bands. The AFP of this case was characterized by relative increases of concanavalin A-nonreactive AFP-C1 (60.4%), erythroagglutinating phytohemagglutinin-reactive AFP-P4 (37.8%) and AFP-P5 (46.3%) and Allomyrina dichotoma lectin-nonreactive AFP-A1s (66.7%), and by the total absence of lentil lectin-reactive components, AFP-L2 and AFP-L3. Thus, the lectin-reactive pattern of AFP markedly deviated not only from that of cord serum, but also from those of other malignancies and of fetal kidney cells in culture.

Although further follow-up study is necessary, these results point to the functional and clinical usefulness of femoral valvuloplasty performed simultaneously with varicose vein surgery in patients with moderate to severe deep venous reflux. The venous filling index obtained with air plethysmography is an excellent predictor of the clinical severity of the disease and of postoperative clinical results.

No abstract

a-L-Iduronidase was purified about 100000-fold from pig liver by employing column chromatography on cellulose phosphate (P1 1), concanavalin A-Sepharose 4B, heparin-Sepharose 4B, Toyopearl HW-55, Sephadex G-100 and chelating Sepharose 6B charged with cupric ions. The molecular mass of the purified enzyme was estimated to be 70 kDa by Sephadex G-100 column chromatography. The purified enzyme gave a single band on disc polyacrylamide gel electrophoresis without using sodium dodecyl sulfate. However, two separate components of 70 kDa and 62 kDa appeared when it was analyzed by SDS/polyacrylamide gel electrophoresis. These 70-kDa and 62-kDa components were confirmed as a-L-iduronidase immunochemically. The isoelectric points of these enzymes were both 9.1 as measured by isoelectric focusing in a polyacrylamide gel containing ampholine and sucrose. The optimal pH and K,,, values were 3.0 -3.5 and 65 pM 4-methylumbelliferyl-a-~-iduronide, respectively. The purified enzyme was stable in the pH range 3.5 -6.0 under conditions with or without 0.5 M NaCI. However, in the presence of 0.5 M NaCl, it was unstable at pH 3.0. Moreover, it was conversely stabilized at pH 7.0 in the presence of 0.5 M NaCI. Immunohistochemically, the enzyme was found in the Kupffer cells and was abundant on their lysosomal membranes. In liver cells, however, the immunohistochemical reaction was weak.a-L-Iduronidase(a-L-iduronide iduronohydrolase) is known to be one of the lysosomal enzymes which is engaged in the degradation of dermatan sulfate, heparan sulfate and heparin [I]. This enzyme is required for the cleavage of iduronic acid residues; the degradation of such polymers is blocked in Hurler's disease and its milder variant, Scheie's disease [2 -41. Many attempts have been made to purify this enzyme, in connection with Hurler's disease and correction of the defect in Hurler fibroblasts [5]. Purified enzyme has so far been obtained from tissues of several human organs, such as the kidney, liver and lung. However, the reported molecular mass of the enzymes varied from 60 kDa to 80 kDa. The enzyme molecular mass in the kidney was 60 kDa [2], that in the liver 65 kDa [4] and that in the lung 80 kDa and 68 kDa [3]. Such molecular heterogeneity, tissue specificity and the cellular distribution of this enzyme attracted our attention. Clearly, to investigate these problems in detail, further purification of the enzyme and a reliable antibody against it are needed. In the present study, we established a method for the purification of this enzyme and obtained some useful information concerning the properties of the enzyme including its immunohistochemical localization in pig liver. MATERIALS AND METHODS ReagentsSephacryl S-200, Sephadex G-100, Sepharose 4B and chelating Sepharose 6B were obtained from Pharmacia FineCorrespondence to T .