cDNAs encoding spinach stromal and thylakoid‐bound ascorbate peroxidase, differing in the presence or absence of their 3′‐coding regions

FEBS Letters

Takeda, Toru¹  Yoshimura, Kazuya¹  Sakai, Kosuke¹  Ishikawa, Takahiro¹  Shigeoka, Shigeru¹ 

[1] Department of Food and Nutrition, Faculty of Agriculture, Kinki University, 3327-204 Nakamachi, Nara 631, Japan

关键词: Ascorbate peroxidase;    Isozyme;    cDNA cloning;    Chloroplast;    Expression;    Spinach (Spinacia oleracea);    AsA;    ascorbate;    AsAP;    ascorbate peroxidase;    CCP;    cytochrome c peroxidase;    GP;    guaiacol peroxidase;    mAb;    monoclonal antibody;    cAsAP;    cytosolic ascorbate peroxidase;    sAsAP;    stromal ascorbate peroxidase;    tAsAP;    thylakoid-bound ascorbate peroxidase;   

DOI  :  10.1016/0014-5793(96)00332-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Two cDNA clones encoding stromal (SAP28) and thylakoid-bound (SAP22) ascorbate peroxidase were isolated from a spinach cDNA library constructed by greening cotyledons. The SAP22 and SAP28 contained an open reading frame encoding mature protein of 295 and 345 amino acids with calculated molecular mass of 32 239 Da and 37 710 Da, respectively, preceded by the common transit peptides of 70 amino acid residues. Interestingly, the N-terminal 364 amino acids of SAP22 were 100% identical with SAP28 except for one C-terminal amino acid residue (Asp-365), and the C-terminal of SAP22, which is the putative transmembrane segment, was 50 amino acids longer than that of SAP28.

【 授权许可】

Unknown