Isolation of thermostable phosphatase from the hyperthermophilic archaeon Thermococcus pacificus by immobilized metal affinity chromatography | Zendy

Bannikova Galina E. | Zendy; Varlamov Valery P. | Zendy; Miroshnichenko Margarita L. | Zendy; BonchOsmolovskaya Elizaveta A. | Zendy

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Isolation of thermostable phosphatase from the hyperthermophilic archaeon Thermococcus pacificus by immobilized metal affinity chromatography

Author(s) -

Bannikova Galina E.,

Varlamov Valery P.,

Miroshnichenko Margarita L.,

BonchOsmolovskaya Elizaveta A.

Publication year - 1998

Publication title -

iubmb life

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.132

H-Index - 113

eISSN - 1521-6551

pISSN - 1521-6543

DOI - 10.1080/15216549800201372

Subject(s) - size exclusion chromatography , affinity chromatography , chemistry , agarose , enzyme , phosphatase , pyrococcus furiosus , biochemistry , chromatography , gel permeation chromatography , protein subunit , archaea , organic chemistry , gene , polymer

Phosphatase was isolated from cells of the hyperthermophilic marine archaeon Thermococcus pacificus by a procedure including chromatography on Butyl‐Fractogel TSK‐650 and Ni2+‐iminodiacetic‐agarose. Enzyme activity is maximal at 90°C, and the enzyme half‐life time at this temperature is 1 h. The pH optimum of phosphatase activity is 6.0. Electrophoresis under denaturating conditions yielded a subunit molecular weight of 45 kDa. On gel‐filtration on Sephacryl S‐300 HR three peak corresponding to 295, 85 and 45 kDa were observed, suggesting that the enzyme is a homohexamer.

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