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J. Biochem, 1988, Vol. 103, No. 5 872-877
© 1988 Japanese Biochemical Society

research-article

A Comparative Study on 40S Ribosomal Proteins of Artemia salina and Rat Liver: Micro Analysis of Amino Acid Composition by High-Performance Liquid Chromatography1

Sumiko Odani2, Naoya Kenmochi3 and Kikuo Ogata4

Department of Biochemistry, Niigata University School of Medicine Niigata, Niigata 951

3To whom correspondence should be addressed at: Faculties of Comparative Medicine & Animal Experimentation, Niigata University School of Medicine, Niigata, Niigata 951.

The amino acid compositions of 24 proteins of 40S ribosomal subunits of Artemia salina cysts were determined and compared with those of rat liver. The basic proteins of A. salina 40S ribosomes were separated by two-dimensional polyacrylamide gel electrophoresis and extracted with 70% formic acid. Samples were freed from contaminants by gel-filtration through a high-performance liquid chromatography column. Amino acid compositions were determined for individual proteins by pre-column derivatization with N, N-dimethylaminoazobenzenesulfonyl chloride followed by reverse phase high-performance liquid chromatography. The similarity of amino acid compositions between A. salina and rat liver 40S ribosomal proteins was evaluated by the method of Cornish-Bowden (Cornish-Bowden, A. (1980) Anal. Biochem. 105, 233–238), and possible relationships between A. salina and rat were detected for 16 protein species (S2, S3, S4, S6, S7, S8, S15a, S16, S17, and S18, strongly related and S14, S15, S20, S23, S24, and S26, weakly related), indicating a conservative nature of eukaryotic ribosomal proteins.

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

2Present address: Faculty of Education, Niigata University, Niigata, Niigata 950-21.

4 Present address: Institute for Gene Expression, Dobashi Kyoritsu Hospital, Matuyama, Ehime 790.


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