Adenine Phosphoribosyltransferase in Plant Tissues: Some Effects of Kinetin on Enzymic Activity | Zendy

P. B. Nicholls | Zendy; Andrew W. Murray | Zendy

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Adenine Phosphoribosyltransferase in Plant Tissues: Some Effects of Kinetin on Enzymic Activity

Author(s) -

P. B. Nicholls,

Andrew W. Murray

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.43.4.645

Subject(s) - adenine phosphoribosyltransferase , callus , kinetin , phosphoribosyltransferase , biochemistry , enzyme , glycine , chemistry , hordeum vulgare , enzyme assay , pyrophosphate , biology , botany , hypoxanthine guanine phosphoribosyltransferase , poaceae , tissue culture , purine , in vitro , gene , amino acid , mutant

Adenine phosphoribosyltransferase activity was measured in extracts of soybean (Glycine max var. Acme) callus and of senescing barley leaves (Hordeum distichon c.v. Prior). The enzyme from soybean callus had Michaelis constants for adenine and 5-phosphoribosyl pyrophosphate of 1.5 and 7.5 mum respectively and was inhibited by AMP and stimulated by ATP. The presence of kinetin was found to considerably increase the activity of adenine phosphoribosyltransferase in extracts of soybean callus and senescing barley leaves.

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