[Validation Study of Analytical Method for Determination of Amnesic Shellfish Poison in Bivalves].

Amnesic shellfish poison (ASP) is regarded as one of the shellfish poison groups in the EU, though it is not subject to regulation in Japan. We have developed an analytical method of ASP based on the report by Hatfield et al. and other methods.

Intra-surgical vs. radiographic bone level assessments in measuring peri-implant bone loss.

Objective: To evaluate the accuracy between the intra-surgical and the peri-apical radiographic measurements of bone loss at implant with peri-implantitis.

Materials And Methods: A total of 46 Brånemark implants in 24 patients with diagnosis of peri-implantitis were included in the study. The amount of peri-implant bone loss occurred at those implants was measured during peri-implant surgery and compared to the radiographic bone loss measured by three independent examiners.

Efficacy and safety of a therapeutic apparatus using hydrogen peroxide photolysis to treat dental and periodontal infectious diseases.

The present study aimed to evaluate the acute locally injurious property of our most current hydroxyl radical generation system by hydrogen peroxide (HO) photolysis. This system, which releases 3% HO with a 405-nm laser, was developed in our laboratory for the treatment of dental and periodontal infectious diseases. First, the hydroxyl radical yield generated by HO photolysis was examined by applying an electron spin resonance-spin trapping technique.

[Electrophoretic Analysis of Abnormal Data on Serum Protein Electrophoresis].

We recently demonstrated glycation of monoclonal IgA and the presence of IgA-albumin complexes, but the significance of the complexes was not clear. We describe a non-diabetic patient with IgA type M-protein whose serum fructosamine and glycoalbumin levels were elevated. On electrophoresis of the serum protein of the patient, the albumin band shifted to the cathode side.

An immunoglobulin A1 that inhibits lactate dehydrogenase activity, with reversal of inhibition by addition of NADH.

We discovered a patient with low serum lactate dehydrogenase (LD) activity and an abnormal LD isozyme pattern. We analyzed the patient's LD inhibitor using electrophoresis, affinity chromatography, and immunochemical technologies. The LD activity of the patient's serum was inhibited more strongly at 4 degrees C than at 37 degrees C.

Identification of complexes of gelatinase A and tissue inhibitor of metalloproteinase-2 in human follicular fluid.

Ovulation involves considerable tissue remodeling in normal ovarian function. These processes are expected to involve matrix metalloproteinases (MMP). Follicular rupture is caused by the degradation of the basement membrane between the thecal and granulose layers, as well as disruption of the extracellular matrix (ECM) at the site of rupture.

[Characterization of anti-DNA antibody on IgG3-kappa type M-protein in a patient with rheumatoid arthritis].

A 66 year-old male patient with rheumatoid arthritis, was admitted due to bronchial pneumonia. Anti-nuclear antibody and anti-DNA antibody were both detected in the patient's serum and many LE-like cells were found in the pleural effusion. In addition, M-proteins(IgG-kappa type, IgM-kappa type) were detected in both serum and pleural effusion by immunofixation electrophoresis.

Complexes of gelatinases and tissue inhibitor of metalloproteinases in human seminal plasma.

Previously reported data have indicated the existence of two kinds of matrix metalloproteinases (MMP-2 and MMP-9) in human seminal plasma (Shimokawa et al, 2002). Here we report the existence of complexes of gelatinases and tissue inhibitor of metalloproteinase-1 (TIMP-1) and TIMP-2 in human seminal plasma. After the seminal plasma supernatant was separated on a gel-filtration column chromatography of GCL-2000-sf-cellulofine.

Matrix metalloproteinase (MMP)-2 and MMP-9 activities in human seminal plasma.

We report on the existence of two kinds of matrix metalloproteinases (MMPs), MMP-2 and MMP-9, in human seminal plasma. Partial purification of the proteinases was achieved by two steps, consisting of chromatography on a gel-filtration column and then on a gelatin affinity column. Proteinase activities in the chromatography extracts were shown to hydrolyse a fluorescent substrate specific to MMPs (Dnp-Pro-Leu-Gly-Leu-Trp-Ala-D-Arg-NH2).