ATP Sulfurylase Activity in the Soybean [Glycine max (L.) Merr.] | Zendy

Clifford A. Adams | Zendy; Robert E. Johnson | Zendy

AI Assistant Blog Pricing

Home ZAIA Blog

Open Access

ATP Sulfurylase Activity in the Soybean [Glycine max (L.) Merr.]

Author(s) -

Clifford A. Adams,

Robert E. Johnson

Publication year - 1968

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.43.12.2041

Subject(s) - inorganic pyrophosphatase , molybdate , pyrophosphatase , chemistry , glycine , enzyme , biochemistry , enzyme assay , magnesium , chromatography , pyrophosphate , inorganic chemistry , organic chemistry , amino acid

ATP sulfurylase activity was assayed in soybean leaf extracts. A simple, rapid assay system using molybdate as an analogue of sulfate was developed. The assay was coupled to inorganic pyrophosphatase. The high pyrophosphatase level in soybean leaf extracts obviated the necessity of adding this enzyme to the assay system. ATP sulfurylase has a pH maximum above 7.5, uses molybdate and ATP as substrates, and requires magnesium ions for activity.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.

Having issues? You can contact us here

Accelerating Research