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Journal of Biochemistry Advance Access published online on October 30, 2007
Journal of Biochemistry, doi:10.1093/jb/mvm199
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© 2007 The Japanese Biochemical Society

Identification and characterization of cathepsin D in a highly purified sialidase from starfish A.pectinifera

Ramaswamy Kannappan1, Youichi Satoh1, Naoko Iriyama1, Masayuki Ando1, Michiko Takagi Sawada2, Nobuaki Takahashi3, Kimio Furuhata4 and Yutaka Uda1,*

1Department of Health Chemistry, Faculty of Pharmaceutical Science, Niigata University of Pharmacy and Applied Life Sciences, Niigata 956-8603, Japan; and 2Evaluation Department, National Institute of Advanced Industrial Science and Technology, Tsukuba, Ibaraki 305-8568, Japan; and 3Marine Biomedical Institute, Sapporo Medical University, School of Medicine, Risirifuji, Hokkaodo 097-0101, Japan; 4Scohool of Pharmaceutical Sciences, Kitasato University, Minato-ku, Tokyo 108-8641, Japan

*Address for correspondence: Dr. Yutaka Uda, Department of Health Chemistry, Faculty of Pharmaceutical Science, Niigata University of Pharmacy and Applied Life Sciences, 265-1, Higashijima, Akiha, Niigata 956-8603, Japan, Phone: +81-250-25-5270, E-mail: uda{at}nupals.ac.jp

Received June 16, 2007; Accepted October 10, 2007


  Abstract

A sialidase [EC 3.2.1.1 [EC] 8] from the ovary of starfish Asterina pectinifera was isolated and highly purified by preparative PAGE. The SDS-PAGE separation of the purified enzyme revealed two natures of protein bands, upper (50 kDa) and a lower (47 kDa). To identify the protein, N-terminal amino acid sequence of the upper band was done. The sequence matched with the N-terminal amino acid sequence of human lysosomal mature cathepsin D and cathepsin D activity was also found in all the preparation steps. Protease inhibitor pepstatin A inhibited the proteolysis activity of cathepsin D against a synthetic substrate. The two enzymes sialidase and cathepsin D were separated from each other by using High performance gel filtration chromatography. The Western blot analysis and iso-electric focusing showed the co-purified cathepsin D is a 50 kDa protein with a PI value of 4.2.

Key Words: Asterina pectinifera, cathepsin D, enzymatic properties, sialidase, ovary of starfish


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