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Nakagawa, Toshiko,Suzuki, Kazuo,Haga, Akira,Hayakawa, Naoya Journal of International Conference on Electrical 2013 Journal of international Conference on Electrical Vol.2 No.4
The authors study a novel type of elevator emergency stop device which enables to soften impact force at an emergency halt. A new structure of emergency stop devices has been already proposed by our laboratory and also its characteristics has been already proposed by our laboratory and also its characteristics has been shown by digital simulations[1]. In order to confirm the actual effects of our proposed emergency stop device, we have made up a simulator having the same characteristics as the conventional emergency stop device to accomplish the experiments from now on. In this paper, this process is introduced.
Kazuhisa, Nakayama,Toshio, Watanabe,Tsutomu, Nakagawa,Kim, Won Sin,Masami, Nagahama,Masahiro, Hosaka,Kiyotaka, Hatsuzawa,Kiyomi, Kondoh-Hashiba,Kazuo, Murakami 圓光大學校 基礎自然科學硏究所 1993 基礎科學硏究誌 Vol.12 No.2
Many peptide hormones and neuropeptides are produced from larger, inactive precursors though endoproteolysis at sites usually marked by paired basic residues (primarily Lys-Arg and Arg-Arg), or occasionally by a monobasic residue (primarily Arg). Based upon data concerning processing of prorenin and its mutants around the native Lys-Arg cleavage site expressed in mouse pituitary AtT-20 cells, we present the following sequence rules that govern mono-arginyl cleavages: (a) a basic residue at the fourth (position-4) or the sixth(position-6) residue upstream of the cleavage site is required, (b) at position - 4, Arg ; more favorable than Lys, and (c) at position I, a hydrophobic aliphatic residue is not suitable. These rules are compatible with those proposed by comparison of precursor sequences around mono-arginyl cleavage sites. We also provide evidence that precursor cleavages at mono-arginly and dibasic sites can be catalyzed by the same Kex2-like processing endoprotease, PC1/PC3.
Kazuhisa Nakayama,Kim, Won-Sin,Seiji Torii,Masahiro Hosaka,Tsutomu Nakagawa,Jo Ikemizu,Tadashi Baba,Kazuo Murakami 원광대학교기초자연과학연구소 1992 基礎科學硏究誌 Vol.11 No.3
We used the polymerase chain reaction to identify a mouse testis cDNA that represented another member of a growing class of mammalian endoproteases involved in the processing of precursor proteins. This cDNA encoded a 655-residue protein, designated PC4, containing a bacterial subtilisin-like catalytic domain closely related to those of the recently characterized precursor-processing endoproteases, furin, PC1/PC3, PC2, and Kex2. Within this domain, the amino acid sequence of PC4 was 70, 58, 55, and 45% identical with those of mouse furin, mouse PC1/PC3, mouse PC2, and yeast Kex2, respectively. Northern blot analysis indicated that the PC4 mRNA was detectable only in the testes after the 20th day of postnatal development. Moreover, this message was mainly expressed in the round spermatids. These data suggest that PC4 represents a prime candidate for a precursor-processing endoprotease in the testicular germ cells and that its gene expression is regulated during spermatogenesis.