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Katayama, Kazunori,Fuchu, Hidetaka,Sugiyama, Masaaki,Kawahara, Satoshi,Yamauchi, Kiyoshi,Kawamura, Yukio,Muguruma, Michio Asian Australasian Association of Animal Productio 2003 Animal Bioscience Vol.16 No.9
In order to clarify one of the biological functions of pork, we investigated whether a peptic hydrolysate of denatured porcine crude myosin showed inhibitory activity against angiotensin I-converting enzyme (ACE), which contributed to hypertension. Our results indicated that this hydrolysate showed relatively strong activity, and we therefore attempted to separate the involved peptides, which were considered to be active substances. To isolate these active peptides, the hydrolysate was separated using a solidphase separation, gel filtration high-performance liquid chromatography (HPLC), and two kinds of reverse phase HPLC. In each stage of separation, many fractions were detected, almost all of which showed ACE inhibitory activity. Thus, we suggested that the activity of the hydrolysate as a whole was a result of the activities of the many individual peptides. Six peaks were distinguished, with yields from 34 to 596 ppm of original crude myosin. In addition to the six peaks, many other active fractions were found throughout the separation steps, strongly suggesting that whole porcine crude myosin itself had ACE inhibitory activity. Moreover, pork as food was considered to function as an ACE inhibitory material in vivo, because pork proteins consist primarily of crude myosin, which included almost all the myofibrillar structural proteins.
Isolation and characterization of acid-soluble bluefin tuna (Thunnus orientalis) skin collagen
Tanaka, Teruyoshi,Takahashi, Kenji,Tsubaki, Kazufumi,Hirata, Maika,Yamamoto, Keiko,Biswas, Amal,Moriyama, Tatsuya,Kawamura, Yukio The Korean Society of Fisheries and Aquatic Scienc 2018 Fisheries and Aquatic Sciences Vol.21 No.4
In this study, we isolated and characterized the acid-soluble skin collagen of Pacific bluefin tuna (PBT, Thunnus orientalis). The PBT skin collagen was composed of two ${\alpha}$ chains (${\alpha}1$ and ${\alpha}2$) and one ${\beta}$ chain. The denaturation temperature of PBT collagen was low although it was rich in proline and hydroxyproline. The primary structure of PBT skin collagen was almost identical to that of calf and salmon skin collagen; however, it differed with respect to the epitope recognition of the antibody against salmon type I collagen. These results suggest that the primary structure of skin collagen was highly conserved among animal species, although partial sequences that included the epitope structure differed among collagens.
Isolation and characterization of acidsoluble bluefin tuna (Thunnus orientalis) skin collagen
Teruyoshi Tanaka,Kenji Takahashi,Kazufumi Tsubaki,Maika Hirata,Keiko Yamamoto,Amal Biswas,Tatsuya Moriyama,Yukio Kawamura 한국수산과학회 2018 Fisheries and Aquatic Sciences Vol.21 No.2
In this study, we isolated and characterized the acid-soluble skin collagen of Pacific bluefin tuna (PBT, Thunnus orientalis). The PBT skin collagen was composed of two α chains (α1 and α2) and one β chain. The denaturation temperature of PBT collagen was low although it was rich in proline and hydroxyproline. The primary structure of PBT skin collagen was almost identical to that of calf and salmon skin collagen; however, it differed with respect to the epitope recognition of the antibody against salmon type I collagen. These results suggest that the primary structure of skin collagen was highly conserved among animal species, although partial sequences that included the epitope structure differed among collagens.