N-Terminal Amino Acid Sequence of Persimmon Fruit [beta]-Galactosidase | Zendy

InnKyu Kang | Zendy; Sang-Jin Suh | Zendy; K.C. Gross | Zendy; J.K. Byun | Zendy

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N-Terminal Amino Acid Sequence of Persimmon Fruit [beta]-Galactosidase

Author(s) -

InnKyu Kang,

Sang-Jin Suh,

K.C. Gross,

J.K. Byun

Publication year - 1994

Publication title -

plant physiology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 3.554

H-Index - 312

eISSN - 1532-2548

pISSN - 0032-0889

DOI - 10.1104/pp.105.3.975

Subject(s) - electroelution , size exclusion chromatography , sephadex , molecular mass , chromatography , chemistry , amino acid , polyacrylamide gel electrophoresis , gel electrophoresis , sodium dodecyl sulfate , biochemistry , enzyme , peptide sequence , yield (engineering) , gene , materials science , metallurgy

beta-Galactosidase (EC 3.2.1.23) from persimmon fruit was purified 114-fold with a 15% yield using Sephadex G-100 gel filtration, CM-Sephadex ion exchange, and Sephacryl S-200 gel filtration chromatography, with subsequent electroelution from nondenaturing polyacrylamide gel electrophoresis (PAGE) gels. The estimated molecular mass of the native beta-galactosidase by Sephacryl S-200 was 118 kD. After sodium dodecyl sulfate-PAGE of the enzyme electroeluted from native gels, two subunits with estimated molecular masses of 34 and 44 kD were observed, suggesting that the native enzyme was an aggregate of several subunits. Amino acid composition and N-terminal amino acid sequences of the two major subunits were different.

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