魚介類トロポミオシンの構造安定性に関する研究

University of Tokyo (東京大学) 博士(農学) The amino acid sequences of tropomyosins (TMs) have been determined for many species: Atlantic salmon Salmo salar (Heeley et al., 1995), bluefin tuna Tunnus tuna (Huang et al., 2004; Ochiai et al., 2010), kuruma prawn Marsupenaeus japonicas (Motoyama et al., 2007),...

Full description

Bibliographic Details
Main Authors: Ozawa, Hideo, 11557
Language:English
Published: 2012
Subjects:
487
Mak
Online Access:https://repository.dl.itc.u-tokyo.ac.jp/record/5550/files/39-097064.pdf
id ftunivtokyo:oai:repository.dl.itc.u-tokyo.ac.jp:00005550
record_format openpolar
spelling ftunivtokyo:oai:repository.dl.itc.u-tokyo.ac.jp:00005550 2023-05-15T15:32:52+02:00 魚介類トロポミオシンの構造安定性に関する研究 Studies on the structural stability of tropomyosins from fish and marine invertebrates Ozawa, Hideo 11557 2012-03-22 application/pdf https://repository.dl.itc.u-tokyo.ac.jp/record/5550/files/39-097064.pdf eng eng 甲第28073号 https://repository.dl.itc.u-tokyo.ac.jp/record/5550/files/39-097064.pdf 487 2012 ftunivtokyo 2022-12-23T04:46:54Z University of Tokyo (東京大学) 博士(農学) The amino acid sequences of tropomyosins (TMs) have been determined for many species: Atlantic salmon Salmo salar (Heeley et al., 1995), bluefin tuna Tunnus tuna (Huang et al., 2004; Ochiai et al., 2010), kuruma prawn Marsupenaeus japonicas (Motoyama et al., 2007), mussel Mytilus edulis galloprovincialis (Iwasaki et al., 1997), rabbit Oryctolagus cuniculus (Stone and Smillie, 1978; Mak et al., 1979), tokobushi abalone Haliotis diversicolor (Chu et al., 2000), torafugu Takifugu rubripes (Ikeda et al., 2003), white croaker Pennahia argentata (Ochiai et al., 2001), walleye pollack Theragra chalcogramma (Ochiai et al., 2003), Yesso scallop Mizuhopecten yessoensis (Hasegawa, 2001), and zebrafish Danio rerio (Ohara et al., 1989). Invertebrate TMs are known as allergens and show higher viscosity than fish TMs, but the basic characteristics, in view of the comparative biochemistry, have not been studied so much. Elucidation of the relationship between amino acid sequence and stability would contribute to ascertain above interesting invertebrate TM properties. But the stability of invertebrate TM has been rarely measured (Inoue et al., 2004). The stability of TMs from fish (Huang and Ochiai, 2005) was estimated by differential scanning calorimetry (DSC) and it has been shown that fish TM, as rabbit TM (Potekhin and Privalov 1982), contains a few unfolding units. Thus, it would be adequate to measure the thermal stability of peptides or fragments. In Chapter 1, the stability of invertebrate TMs was investigated. TMs from the tail muscle of kuruma prawn, mantle muscle of Japanese common squid Todarodes pacificus, foot muscle of tokobushi abalone, and striated and smooth adductor muscles of Yesso scallop were purified and these stabilities were determined by circular dichroism (CD) spectrometry and DSC. The white croaker TM was used as control. In addition, three mRNAs encoding the smooth muscle TMs of the scallop have been sequenced (Hasegawa, 2001) and the major component was ... Other/Unknown Material Atlantic salmon Salmo salar Theragra chalcogramma The University of Tokyo: UT Repository Mak ENVELOPE(162.381,162.381,56.401,56.401)
institution Open Polar
collection The University of Tokyo: UT Repository
op_collection_id ftunivtokyo
language English
topic 487
spellingShingle 487
Ozawa, Hideo
11557
魚介類トロポミオシンの構造安定性に関する研究
topic_facet 487
description University of Tokyo (東京大学) 博士(農学) The amino acid sequences of tropomyosins (TMs) have been determined for many species: Atlantic salmon Salmo salar (Heeley et al., 1995), bluefin tuna Tunnus tuna (Huang et al., 2004; Ochiai et al., 2010), kuruma prawn Marsupenaeus japonicas (Motoyama et al., 2007), mussel Mytilus edulis galloprovincialis (Iwasaki et al., 1997), rabbit Oryctolagus cuniculus (Stone and Smillie, 1978; Mak et al., 1979), tokobushi abalone Haliotis diversicolor (Chu et al., 2000), torafugu Takifugu rubripes (Ikeda et al., 2003), white croaker Pennahia argentata (Ochiai et al., 2001), walleye pollack Theragra chalcogramma (Ochiai et al., 2003), Yesso scallop Mizuhopecten yessoensis (Hasegawa, 2001), and zebrafish Danio rerio (Ohara et al., 1989). Invertebrate TMs are known as allergens and show higher viscosity than fish TMs, but the basic characteristics, in view of the comparative biochemistry, have not been studied so much. Elucidation of the relationship between amino acid sequence and stability would contribute to ascertain above interesting invertebrate TM properties. But the stability of invertebrate TM has been rarely measured (Inoue et al., 2004). The stability of TMs from fish (Huang and Ochiai, 2005) was estimated by differential scanning calorimetry (DSC) and it has been shown that fish TM, as rabbit TM (Potekhin and Privalov 1982), contains a few unfolding units. Thus, it would be adequate to measure the thermal stability of peptides or fragments. In Chapter 1, the stability of invertebrate TMs was investigated. TMs from the tail muscle of kuruma prawn, mantle muscle of Japanese common squid Todarodes pacificus, foot muscle of tokobushi abalone, and striated and smooth adductor muscles of Yesso scallop were purified and these stabilities were determined by circular dichroism (CD) spectrometry and DSC. The white croaker TM was used as control. In addition, three mRNAs encoding the smooth muscle TMs of the scallop have been sequenced (Hasegawa, 2001) and the major component was ...
author Ozawa, Hideo
11557
author_facet Ozawa, Hideo
11557
author_sort Ozawa, Hideo
title 魚介類トロポミオシンの構造安定性に関する研究
title_short 魚介類トロポミオシンの構造安定性に関する研究
title_full 魚介類トロポミオシンの構造安定性に関する研究
title_fullStr 魚介類トロポミオシンの構造安定性に関する研究
title_full_unstemmed 魚介類トロポミオシンの構造安定性に関する研究
title_sort 魚介類トロポミオシンの構造安定性に関する研究
publishDate 2012
url https://repository.dl.itc.u-tokyo.ac.jp/record/5550/files/39-097064.pdf
long_lat ENVELOPE(162.381,162.381,56.401,56.401)
geographic Mak
geographic_facet Mak
genre Atlantic salmon
Salmo salar
Theragra chalcogramma
genre_facet Atlantic salmon
Salmo salar
Theragra chalcogramma
op_relation 甲第28073号
https://repository.dl.itc.u-tokyo.ac.jp/record/5550/files/39-097064.pdf
_version_ 1766363354758119424