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Isolation and Properties of Glucose-1-phosphatase from Mycelia ofPholiota nameko
Author(s) -
Toshio Joh,
Junshi Yazaki,
Kayo Suzuki,
Toshiro HAYAKAWA
Publication year - 1998
Publication title -
bioscience biotechnology and biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.509
H-Index - 116
eISSN - 1347-6947
pISSN - 0916-8451
DOI - 10.1271/bbb.62.2251
Subject(s) - mycelium , acid phosphatase , biochemistry , chemistry , molybdate , enzyme , sodium molybdate , phosphatase , biology , botany , organic chemistry
An acid phosphatase with a very high substrate specificity for glucose-1-phosphate was isolated for the first time from mycelia of Pholiota nameko. The molecular weight of the enzyme was estimated to be 31,000 on gel filtration and 35,000 on SDS-PAGE. The activity was inhibited by Cu2+, Hg2+, molybdate, and tartaric acid. The sequence of N-terminal 20 amino acid residues was analyzed.

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