Purification and Characterization of Lysozyme from Ayu Skin Mucus.

Itami, Toshiaki; Takehara, Atsushi; Nagano, Yoshinobu; Suetsuna, K.; Mitsutani, Atsushi; Takesue, Kaoru; Takahashi, Yuichiro

doi:10.2331/suisan.58.1937

Cited by 19 publications

(8 citation statements)

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“…Even though not as substantial as in the case of the rainbow trout, some other fi sh lysozymes such as the c-type lysozymes from ayu fi sh, coho salmon eggs and Japanese fl ounder, and the g-type lysozymes from yellow croaker, orange-spotted grouper and Japanese fl ounder, were reported to have antibacterial activity against Gram-negative bacteria as well (Itami et al 1992;Yousif et al 1994;Hikima et al 2001;Minagawa et al 2001;Zheng et al 2007). Remarkably, the activity of these fi sh lysozymes inversely correlated with the virulence of the target bacteria for that particular species (Saurabh and Sahoo 2008).…”

Section: Antibacterial Activity Of Lysozymesmentioning

confidence: 95%

“…During the past decades, lysozyme activity has been widely reported in fi sh tissues including the head kidney, which is a leukocyte-rich key organ in immunity, and in the gill, skin, gastrointestinal tract and eggs, where the risk of bacterial invasion is high (Saurabh and Sahoo 2008). Moreover, several c-and g-type fi sh lysozymes have been reported to kill both Gram-positive and Gram-negative bacteria (Grinde 1989;Itami et al 1992;Yousif et al 1994;Hikima et al 2001;Minagawa et al 2001;Zheng et al 2007; cfr section 3.4), thus highlighting their capacities as antibacterial proteins even more than those from other animals.…”

Section: (Iii) Fishmentioning

confidence: 98%

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Lysozymes in the animal kingdom

2010

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Lysozymes (EC 3.2.1.17) are hydrolytic enzymes, characterized by their ability to cleave the beta-(1,4)-glycosidic bond between N-acetylmuramic acid and N-acetylglucosamine in peptidoglycan, the major bacterial cell wall polymer. In the animal kingdom, three major distinct lysozyme types have been identified--the c-type (chicken or conventional type), the g-type (goose-type) and the i-type (invertebrate type) lysozyme. Examination of the phylogenetic distribution of these lysozymes reveals that c-type lysozymes are predominantly present in the phylum of the Chordata and in different classes of the Arthropoda. Moreover, g-type lysozymes (or at least their corresponding genes) are found in members of the Chordata, as well as in some bivalve mollusks belonging to the invertebrates. In general, the latter animals are known to produce i-type lysozymes. Although the homology in primary structure for representatives of these three lysozyme types is limited, their three-dimensional structures show striking similarities. Nevertheless, some variation exists in their catalytic mechanisms and the genomic organization of their genes. Regarding their biological role, the widely recognized function of lysozymes is their contribution to antibacterial defence but, additionally, some lysozymes (belonging to different types) are known to function as digestive enzymes.

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Section: Antibacterial Activity Of Lysozymesmentioning

confidence: 95%

Section: (Iii) Fishmentioning

confidence: 98%

Lysozymes in the animal kingdom

2010

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“…The enzyme has been purified from the serum of plaice, Pleuronectes platessa (Fletcher and White 1976), the skin mucus of carp, Cyprinus carpio ) and ayu, Plecoglossus altivelis (Itami et al 1992), the kidney of rainbow trout, Oncorhynchus mykiss (Grinde et al 1988), the eggs of coho salmon, 0. kisutch (Yousif et al 1991), and partially from the liver of tilapia, Oreochromis mossambicus (Sankaran and Gurnani 1972). These lysozymes have a low molecular mass, ranging from 14kDa to 18kDa (Fletcher and White 1973;Grinde et al 1988;Yousif et al 1991;Itami et al 1992).…”

Section: Introductionmentioning

confidence: 99%

“…These lysozymes have a low molecular mass, ranging from 14kDa to 18kDa (Fletcher and White 1973;Grinde et al 1988;Yousif et al 1991;Itami et al 1992).…”

Section: Introductionmentioning

confidence: 99%

Lysozyme in the ovary of tilapia (Oreochromis mossambicus): its purification and some biological properties

Takemura

Takano

1995

Fish Physiol Biochem

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Lysozyme was purified from the ovary of tilapia, Oreochromis mossambicus, with two steps, chitin coated-cellulose and Sephadex G-100, and its biological properties were investigated. Purified lysozyme had a molecular mass of 15kDa on SDS-PAGE under reducing condition. Analyses with antibody (a-EL) against the purified lysozyme revealed that serum and egg extract reacted with a-EL and the precipitin lines fused completely. The enzyme activities in serum and egg extract were inhibited by adding serially diluted a-EL. Therefore, egg extract and serum lysozyme was immunologically identical. Immunohistochemically, lysozyme was observed in the ooplasm of the oocytes laden with yolk but not in the follicle layers, egg envelope or immature oocytes (the peri-nucleolus stage). In addition, the enzyme activity in the large oocytes was higher than that in the small ones. These results suggest that lysozyme detected in the oocytes is derived from extra-ovarian tissue and transfers from the maternal circulation. Lysozyme activity in the serum of female tilapia increased with oocyte development, suggesting that the change in the enzyme level may be partially related to the reproductive events (especially vitellogenesis) of the female fish.

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“…The elevated activities of AST and ALT presumably indicate damage to the liver, but other organs like the kidney and gills may also be damaged (Hochachka and Mommsen, 1995;Bernet et al, 2001). The lysozyme enzyme, a polypeptide with a molecular weight of 14-18 kDa, is one of the key components of non-specific immune system of the fish (Itami et al, 1992;Yousif et al, 1991). Lysozyme is an anti-bacterial agent secreted by white blood cells (mainly by neutrophils, monocytes and macrophages) and leukocyte-rich tissues such as kidney, spleen, skin mucus, gills and digestive tract (Ghafoori et al, 2014).…”

Section: Introductionmentioning

confidence: 98%