Effects of gamma-irradiation and air annealing on Yb-doped Y3Al5O12 single crystal

The effects of gamma-irradiation on the air-annealed 10 at.% Yb:Y3Al5O12 (YAG) and air annealing on the gamma-irradiated 10at.% Yb:YAG have been studied by the difference absorption spectra before and after treatment. The gamma-irradiation and air annealing led to opposite changes of the absorption properties of the Yb:YAG crystal. After air annealing, the gamma-irradiation induced centers were totally removed and the concentration of Fe3+ and Yb3+ were lightly increased. For the first time, the gamma-irradiation induced valence changes between Yb3+ and Yb2+ ions in Yb:YAG crystals have been observed. (C) 2007 Elsevier B.V. All rights reserved.

The separation of beta-BBO phase in alpha-BBO crystal by the irradiation of femtosecond laser

We observed and described some phenomena, which were that when a alpha-BBO crystal was irradiated by a focused femtosecond laser beam, the temperature effect happened in a minute area of focus, then the induced beta-BBO phase was separated within the minute area in the alpha-BBO crystal. (C) 2007 Elsevier B.V. All rights reserved.

Influences of CO2 laser irradiation on the structure and photoluminescence of zinc oxide thin films

CO2 laser irradiation experiments on ZnO thin films are reported. The structural, optical, luminescent and vibrational properties of the samples were investigated by X-ray diffraction (XRD), transmittance, photoluminescence (PL) and Raman measurements. XRD results show that the crystalline of the irradiated films was improved. The (002) peaks of irradiated ZnO films shift to. higher 20 angles due to the stress relaxation in the case of laser beam irradiation. From optical transmittance spectra, all films exhibit high transmittance in the visible range, the optical band edge of irradiated films showed a redshift compared with that of as-grown films. Compared with the as-grown films, the photoluminescence emission (in particular the relative intensities of visible emissions) intensities of irradiated samples enhanced. In the Raman scattering spectral both the A I. and E modes exhibited slight Raman blueshift. (c) 2005 Elsevier B.V. All rights reserved.

Damage on HfO2/SiO2 high-reflecting coatings under single and multiple Nd:YAG laser pulse irradiation

The single- and multi-shot damage behaviors of HfO2/SiO2 high-reflecting (HR) coatings under Nd:YAG laser exposure were investigated. Fundamental aspects of multi-shot laser damage, such as the instability due to pulse-to-pulse accumulation of absorption defect and structural defect effect, and the mechanism of laser induced defect generation, are considered. It was found in multi-shot damage, the main factors influencing laser-induced damage threshold (LIDT) are accumulation of irreversible changes of structural defects and thermal stress that induced by thermal density fluctuations.

Identification and cloning of a trypsin inhibitor from skin secretions of Chinese red-belly toad Bombina maxima

A novel trypsin inhibitor was identified and purified from skin secretions of Chinese red-belly toad Bombina maxima. The partial N-terminal 29 amino acid residues of the peptide, named BMTI, were determined by automated Edman degradation. This allowed the cloning of a full-length cDNA encoding BMTI from a cDNA library prepared from the toad skin. The deduced complete amino acid sequence of BMTI indicates that mature BMTI is composed of 60 amino acids. A FASTA search in the databanks revealed that BMTI exhibits 81.7% sequence identity with BSTI, a trypsin/thrombin inhibitor from European toad Bombina bombina skin secretions. Sequence differences between BMTI and BSTI were due to 11 substitutions at positions 2, 9, 25, 27, 36-37, 39, 41-42, 50 and 56. BMTI potently inhibited trypsin with a K-i value of 0.06 muM, similar to that of BSTI. However, unlike BSTI, which also inhibited thrombin with a K-i value of 1 muM, no inhibitory effect of BMTI on thrombin was observed under the assay conditions. (C) 2002 Elsevier Science Inc. All rights reserved.

Purification and characterization of an irreversible serine protease inhibitor from skin secretions of Bufo andrewsi

Amphibian skin secretions contain many bioactive compounds. In the present work, an irreversible serine protease inhibitor, termed baserpin, was purified for the first time from the skin secretions of toad Bufo andrewsi by Successive ion-exchange and gelfiltration chromatography. Baserpin is a single chain glycoprotein, with an apparent molecular weight of about 60 kDa in SDS-PAGE. Baserpin is an irreversible inhibitor and effectively inhibits the catalytic activity of trypsin, chymotrypsin and elastase. SDS-stable baserpin-trypsin complex could be seen in SDS-PAGE indicates that it possibly belongs to the serpin superfamily. According to the association rates determined, baserpin is a potent inhibitor of bovine trypsin (4.6 X 10(6) M-1 S-1), bovine chymotrypsin (8.9 X 10(6) M-1 s(-1)) and porcine elastase (6.8 X 10(6) M-1 s(-1)), whereas it shows no inhibitory effect on thrombin. The N-terminal sequence of baserpin is HTQYPDILIAKPXDK, which shows no similarity with other known serine protease inhibitors. (c) 2005 Elsevier Ltd. All rights reserved.

Frog albumin is expressed in skin and characterized as a novel potent trypsin inhibitor

A novel potent trypsin inhibitor was purified and characterized from frog Bombina maxima skin. A full-length cDNA encoding the protein was obtained from a cDNA library constructed from the skin. Sequence analysis established that the protein actually comprises three conserved albumin domains. B. maxima serum albumin was subsequently purified, and its coding cDNA was further obtained by PCR-based cloning from the frog liver. Only two amino acid variations were found in the albumin sequences from the skin and the serum. However, the skin protein is distinct from the serum protein by binding of a haem b (0.95 mol/mol protein). Different from bovine serum albumin, B. maxima albumin potently inhibited trypsin. It bound tightly with trypsin in a 1: 1 molar ratio. The equilibrium dissociation constants (K-D) obtained for the skin and the serum proteins were 1.92 x 10(-9) M and 1.55 x 10(-9) M, respectively. B. maxima albumin formed a noncovalent complex with trypsin through an exposed loop formed by a disulfide bond (Cys(53)-Cys(62)), which comprises the scissile bond Arg(58)(P-1)-His(59)(P-1'). No inhibitory effects on thrombin, chymotrypsin, elastase, and subtilisin were observed under the assay conditions. Immunohistochemical study showed that B. maxima albumin is widely distributed around the membranes of epithelial layer cells and within the stratum spongiosum of dermis in the skin, suggesting that it plays important roles in skin physiological functions, such as water economy, metabolite exchange, and osmoregulation.

A small trypsin inhibitor from the frog of Odorrana grahami

A novel peptide inhibitor (OGTI) of serine protease with a molecular weight of 1949.8, was purified from the skin secretion of the frog, Odorrana grahami. Of the tested serine proteases, OGTI only inhibited the hydrolysis activity of trypsin on synthetic chromogenic substrate. This precursor deduced from the cDNA sequence is composed of 70 amino acid residues. The mature OGTI contains 17 amino acid residues including a six-residue loop disulfided by two half-cysteines (AVNIPFKVHFRCKAAFC). In addition to its unique six-residue loop, the overall structure and precursor of OGTI are different from those of other serine protease inhibitors. It is also one of the smallest serine protease inhibitors ever found. (C) 2008 Elsevier Masson SAS. All rights reserved.

A serine proteinase inhibitor from frog eggs with bacteriostatic activity

By Sephadex G-50 gel filtration, Resource Q anionic exchange and C4 reversed phase liquid high performance liquid chromatography, a proteinase inhibitor protein (Ranaserpin) was identified and purified from the eggs of the odour frog, Rana grahami. The protein displayed a single band adjacent to the molecular weight marker of 14.4 kDa analyzed by SDS-PAGE. The inhibitor protein homogeneity and its molecular weight were confirmed again by MALDI-TOF mass spectrometry analysis. The MALDI-TOF mass spectrum analysis gave this inhibitor protein an m/z of 14422.26 that was matched well with the result from SDS-PAGE. This protein is a serine proteinase inhibitor targeting multiple proteinases including trypsin, elastase, and subtilisin. Ranaserpin inhibited the proteolytic activities of trypsin, elastase, and subtilisin. It has an inhibitory constant (K-i) of 6.2 x 10(-8) M, 2.7 x 10(-7) M and 2.2 x 10(-8) M for trypsin, elastase, and subtilisin, respectively. This serine proteinase inhibitor exhibited bacteriostatic effect on Gram-positive bacteria Bacillus subtilis (ATCC 6633). It was suggested that ranaserpin might act as a defensive role in resistance to invasion of pests or pathogens. This is the first report of serine proteinase inhibitor and its direct defensive role from amphibian eggs. (C) 2007 Elsevier Inc. All rights reserved.