Kyoto University · Biochemistry, Genetics and Molecular Biology
Professor Kenji Sato's research lab specializes in food biochemistry and muscle physiology, with a primary focus on the structural and functional properties of collagen in fish and other animal tissues. His work explores collagen solubility, its role in muscle texture and swimming mechanics, and the biochemical changes during postmortem storage, particularly in relation to connective tissue degradation. The lab also investigates protein cross-linking and analytical methods for detecting bioactive compounds in food proteins.
Figures are computed from collected data and may differ slightly.
The contents of acid-soluble and insoluble collagens in the ordinary muscle of twenty-two species of fishes was determined. In addition, the contribution of muscle collagen to the swimm-ing movement of fish and to the texture of the sliced raw meat was examined. The total collagen content varied with species in the ranges from 0.34 to 2.19% of wet tissue and from 1.6 to 12.4% of crude protein. The solubility of muscle collagen of fishes was generally much higner than that reported for muscle col
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTType V collagen in trout (Salmo gairdneri) muscle and its solubility change during chilled storage of muscleKenji Sato, Chiho Ohashi, Kozo Ohtsuki, and Makoto KawabataCite this: J. Agric. Food Chem. 1991, 39, 7, 1222–1225Publication Date (Print):July 1, 1991Publication History Published online1 May 2002Published inissue 1 July 1991https://pubs.acs.org/doi/10.1021/jf00007a005https://doi.org/10.1021/jf00007a005research-articleACS PublicationsRequest reus
Type V collagen became solubilized in softened sardine muscle after 1 day of chilled storage with the concomitant weakening of pericellular connective tissue induced by disintegration of thin collagen fibrils. However, no significant changes were observed in the structure of interstitial connective tissue or biochemical properties of type I collagen. Z disk in myofibrils showed structural changes, but no significant loss of longitudinal continuity of myofibrils was observed even at the deteriora
Results indicated that compared with isolates from conventional dairy farms, E. coli isolates from organic dairy herds have significantly lower prevalences of resistance to 7 antimicrobials; however, prevalence of resistance was not significantly different for 10 other antimicrobials. Resistance was more common for isolates from calves than for isolates from adult dairy cows.
Although methacholine (MCh) and a Ca2+ ionophore A23187 do not enhance the tissue adenosine 3',5'-cyclic monophosphate (cAMP) level by themselves, they markedly potentiate isoproterenol (ISO)-induced tissue cAMP accumulation in isolated simian eccrine sweat glands in a dose-dependent manner. The agonist concentration producing 50% of the maximal response of such a potentiated cAMP accumulation was 2.1 X 10(-7) M for MCh, 2.5 X 10(-7) M for ISO, and 2.9 X 10(-6) M for A23187. Unlike cAMP accumula
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTImproved method for identification and determination of .epsilon.-(.gamma.-glutamyl)lysine cross-link in protein using proteolytic digestion and derivatization with phenyl isothiocyanate followed by high-performance liquid chromatography separationKenji. Sato, Yasuyuki. Tsukamasa, Chiharu. Imai, Kozo. Ohtsuki, Yutaka. Shimizu, and Makoto. KawabataCite this: J. Agric. Food Chem. 1992, 40, 5, 806–810Publication Date (Print):May 1, 1992Publication History
Many cells and soluble factors are involved in the wound healing process, which can be divided into inflammatory, proliferative, and remodeling phases. Fibroblasts play a crucial role in wound healing, especially during the proliferative phase, and show heterogeneity depending on lineage, tissue distribution, and extent of differentiation. Fibroblasts from tissue stem cells rather than from healthy tissues infiltrate wounds and proliferate. Some fibroblasts in the wound healing site express the
Attempts were made to isolate native acid-soluble collagen from fish muscle by removing selectively non-collagenous proteins with a dilute NaOH solution. The preliminary extraction with 0.01 and 0.05N NaOH did not remove satisfactorily non-collagenous proteins from carp muscle, whereas the preliminary extraction with 0.5 and 1.0N NaOH modified the polypeptide chains of collagen, thus increasing the solubility of collagen. On the other hand, the preliminary extraction with 0.1N NaOH was found to
The muscle of carp was fractionated into water-soluble, alkali-soluble (0.1N NaOH), acid-soluble (0.5M acetic acid), hot water-soluble (extraction with water at 120°C for 1h), and residual fractions. The analyses of amino acid and SDS-polyacrylamide gel electrophoresis showed that collagen in the muscle was quantitatively recovered only in the acid-soluble and hot water-soluble fractions and non-collagenous proteins were absent in these fractions. On the basis of the colori-metric determination
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