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J. Biochem, 1988, Vol. 103, No. 6 986-991
© 1988 Japanese Biochemical Society

research-article

Structures of Sugar Chains of a p-Nitrophenyl Acetate-Hydrolyzing Esterase from the Microsomes of Rat Liver1

Shunji Natsuka, Faculty of Pharmaceutical Science*, Masaru Himeno**, Sumihiro Hase*,2, Harunobu Ito**, Tadashi Ueda, Faculty of Pharmaceutical Science**, Keitaro Kato, Faculty of Pharmaceutical Science** and Tokuji Ikenaka*

* Department of Chemistry, Osaka University College of Science Toyonaka, Osaka 560
** Kyushu University Higashi-ku, Fukuoka, Fukuoka 812

2To whom correspondence should be addressed.

The structures of sugar chains of a p-nitrophenyl acetate-hydrolyzing esterase from the microsomes of rat liver were established. The enzyme contained mannose and glucosamine as sugar components. Asparagine-linked sugar chains of the esterase were liberated by hydrazinolysis. After N-acetylation of the hydrazinolysate, the reducing ends of the sugar chains were coupled with 2-aminopyridine. Fluorescent pyridylamino (PA-) derivatives of sugar chains thus obtained were purified by gel filtration and reversed-phase HPLC. Eleven PA-sugar chains were obtained. The structures of the PA-sugar chains were first identified by HPLC using two series of separation systems by which 11 PA-oligomannose-type sugar chains with known structures could be separated. Further elucidation of the structures of each PA-sugar chain was performed by exoglycosidase digestions and partial acetolysis. The structures of two of the PA-sugar chains were further confirmed by 500 MHz 1H-NMR spectroscopy.

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


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