• Journal of Welding and Joining
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• v.13 no.2
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• pp.12-24
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• 1995

Recently, more researches have been actively performed for the assessment of material degradation and residual-life of elevated temperature plant components, as some of domestic fossil power plants become older than 30 years. In this paper, results of on_site residual life assessment are reported for main steam pipes of Youngwol power station #2 which have operated since 1965. For critical weld locations such as butt welds branch welds, Y_sections and a T-section, replication technique and hardness measurement technique were employed for life_assessment. When cracks were detected by conventional NDT tests, crack growth life was calculated using a computer code. On the other hand, for matrix of pipes, residual life was quantitatively estimated by an analytic method and material degradation was estimated qualitatively using diameter measurement data and grain-boundary etching method. Also, direction in further improvement of on-site life assessment techniques are proposed.

• International Journal of Industrial Entomology and Biomaterials
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• v.11 no.1
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• pp.37-42
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• 2005

We cloned the $\beta$-tubulin genes from the wild type strain and two benomyl-resistant mutants of Metahizium anisopliae and determined their nucleotide sequences. A $\beta$-tubulin encoding 448-residue protein from wild type M. anisopliae shows strong homology to other $\beta$-tubulins. The coding region is interrupted by four introns. Comparisons of intron position between the M. anisopliae gene and other fungal $\beta$-tubulin genes show considerable positional conservation. The mutations responsible for benomyl resistance were determined in two spontaneous mutants, 8-18 and 8­19. One mutant 8-18 substituted glutamate for aspar­agine at position 33 and lysine for glutamine at position 134. The other mutant 8-19 showed alterations at three positions of $\beta$-tubulin arginine for tryptophan at position 21, lysine for asparagine at position 33, and phenylalanine for leucine at position 240. These data suggest that regions of $\beta$-tubulin containing amino acids 21, 33,134, and 240 interact to form the binding site of benomyl.