No abstract

Gold-deposited optical fiber sensors with film thicknesses from 30 to 60 nm were prepared, and the responses to a wide range of a refractivity (1.33 -1.54 refractive index (RI) units) were investigated both experimentally and theoretically. The response curve of the sensor has two minima in the refractivity range from 1.33 to 1.44 and at 1.462 RI units. The former minimum is due to surface plasmon resonance (SPR) in the thin gold film, and shifts to a lower refractivity as the film becomes thicker. The response curves of the sensors with film thicknesses of 45 and 60 nm agreed well with those calculated from SPR theoretical equations. Morphology observations of the surfaces of deposited gold films on glass by atomic force microscopy (AFM) and a variation in resistance of the films with various thicknesses show the structure of the gold films. We concluded that the thin deposited gold films have many defects, and that the core of the golddeposited optical fiber leaks light through the defects to the sample solution with the same refractivity (1.462 RI units) as that of the core.

No abstract

Anti-ferritin autoantibodies are found in many animals. Human ferritin-binding proteins (FBPs) were partially purified from human serum by ion-exchange chromatography and immobilized metal affinity chromatography with Zn 2+ . Crude FBPs were immunocoprecipitated with canine liver ferritin followed by the addition of anti-ferritin antibodies. Immunoglobulins in the immunocoprecipitate were detected with antibodies specific for human IgG, IgM or IgA heavy chains, and immunoglobulins IgG, IgM and IgA to bind to expressed recombinant human H and L chain homopolymers were also found. A portion of human serum proteins bound to zinc ions immobilized on beads were released upon the addition of canine liver ferritin, and the released protein was identified as IgM antibody. Additionally, the released proteins recognized peptide sequence (DPHLCDF) commonly found in amino acid sequences of mammalian ferritin H and L subunits. These results suggest that human serum contains anti-ferritin autoantibodies (IgG, IgM and IgA) which bind zinc ions and preferentially bind ferritin over both the H and L subunits, and that a portion of, but not all, the IgM antibodies bound to ferritin with higher affinity than to zinc ions and may recognize the common sequence found in mammalian ferritin H and L subunits.

2013J o u r n a l o f I n f o r m a t i o n P r o c e s s i n g a n d M a n a g e m e n t JOHO KANRI