PURIFICATION AND PROPERTIES OF SERINE HYDROXYMETHYLTRANSFERASE FROM NICOTIANA RUSTICA L.

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概要

• 論文の詳細を見る

• Serine hydroxymethyltransferase was partially purified from Nicotiana rustica roots. The pH optimum for the enzyme is 4.0. A requirement for pyridoxal phosphate and a divalent cation was shown, and the enzyme was inhibited by sulfhydryl reagents and the reaction is folic acid-dependent.

• 日本植物生理学会の論文

著者

• Sisler Edward

  Department Of Biochemistry North Carolina State University

• PRATHER CHARLES

  Department of Biochemistry, North Carolina State University

• Prather Charles

  Department Of Biochemistry North Carolina State University:(present)spruance Research Laboratories E

関連論文

• EFFECT OF TEMPERATURE AND MOISTURE ON THE INACTIVATION OF O-DIPHENOL OXIDASE
• PURIFICATION AND PROPERTIES OF SERINE HYDROXYMETHYLTRANSFERASE FROM NICOTIANA RUSTICA L.

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