-transparent.png){kind=logo}
Lysosomal beta-mannosidase was purified almost 10,000-fold from human placenta. The final preparation showed several protein bands on polyacrylamide gel electrophoresis. Its molecular mass was estimated to be 110 kDa, the optimal pH was 4.5, the Km was 0.56 mM, and the isoelectric point was 4.7. The enzyme was found to bind completely to Con A-Sepharose, and the pI was not changed after neuraminidase treatment. These results indicate that the purified enzyme represents a lysosomal form which contains high mannose type oligosaccharide chains and only a few sialic acids, if any.
Related Publications
Y Iwasaki, and
A Tsuji, and
K Omura, and
Y Suzuki
December 1983,
Hoppe-Seyler's Zeitschrift fur physiologische Chemie,
Y Iwasaki, and
A Tsuji, and
K Omura, and
Y Suzuki
December 1988,
Indian journal of biochemistry & biophysics,
Y Iwasaki, and
A Tsuji, and
K Omura, and
Y Suzuki
January 1993,
The Biochemical journal,
Y Iwasaki, and
A Tsuji, and
K Omura, and
Y Suzuki
November 1988,
Journal of biochemistry,
Y Iwasaki, and
A Tsuji, and
K Omura, and
Y Suzuki
January 1987,
Steroids,
Y Iwasaki, and
A Tsuji, and
K Omura, and
Y Suzuki
August 1966,
Archives of biochemistry and biophysics,
Y Iwasaki, and
A Tsuji, and
K Omura, and
Y Suzuki
March 1996,
Biochimica et biophysica acta,
Y Iwasaki, and
A Tsuji, and
K Omura, and
Y Suzuki
February 1978,
Biochemistry,
Y Iwasaki, and
A Tsuji, and
K Omura, and
Y Suzuki
June 1983,
Proceedings of the National Academy of Sciences of the United States of America,
Y Iwasaki, and
A Tsuji, and
K Omura, and
Y Suzuki
May 2001,
Molecular genetics and metabolism,
