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J. Biochem, 1983, Vol. 94, No. 1 115-122
© 1983 Japanese Biochemical Society

research-article

Enzymatic Activity of Avian Egg-White Lysozymes1

Tamo FUKAMIZO*,2, Takao TORIKATA**, Toshiro NAGAYAMA*, Takeya MINEMATSU* and Katsuya HAYASHI*

*Department of Agricultural Chemistry, Kyushu University Higashi-ku, Fukuoka, Fukuoka 812
**Faculty of Agriculture, Kyushu Tokai University Choyo-mura, Aso, Kumamoto 869-14

2 To whom correspondence should be addressed.

The experimental time-courses of eight avian lysozymes, seven hen-type lysozymes and one goose-type lysozyme, were measured with a substrate of chitopentaose (GlcNAc)5 at pH 5.0 and 50°C. Chitooligosaccharides in the reaction mixture were analyzed by high-performance gel-filtration. From the experimental time-courses, the overall reaction rates represented by the disappearance of the initial substrate and the values of reaction parameters were estimated by computer analysis. With taking hen lysozyme as the reference, the values of reaction parameters estimated were correlated to the replaced amino acid residue in the binding site of the lysozyme, and the roles of some amino acid residues in the binding site were discussed.

1 This study was supported by a Grant-in-Aid for Scientific Research from the Ministry of Education, Science and Culture of Japan.


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H. Hirakawa, A. Ochi, Y. Kawahara, S. Kawamura, T. Torikata, and S. Kuhara
Catalytic Reaction Mechanism of Goose Egg-white Lysozyme by Molecular Modelling of Enzyme-Substrate Complex
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[Abstract] [Full Text] [PDF]


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