Antimicrobial peptides and proteins are being studied with increasing interest because of their broad range antimicrobial activity. Among plant antimicrobial proteins, the wheat seed polypeptides, puroindoline a and puroindoline b, are particularly interesting because of their established antibacterial activity. In this paper we describe different strategies used to clone His tagged and GST tagged puroindolines obtaining 1.5 mg recombinant protein from 1 l culture. The antimicrobial activity of recombinant and native puroindolines was comparable.
Cloning and expression of two plant proteins: similar antimicrobial activity of native and recombinant form / Capparelli, Rosanna; Palumbo, D; Iannaccone, Marco; Ventimiglia, I; DI SALLE, E; Capuano, F; Salvatore, Paola; Amoroso, Mg. - In: BIOTECHNOLOGY LETTERS. - ISSN 0141-5492. - 28(13):(2006), pp. 943-949. [10.1007/s10529-006-9031-9]
Cloning and expression of two plant proteins: similar antimicrobial activity of native and recombinant form.
CAPPARELLI, ROSANNA;IANNACCONE, MARCO;SALVATORE, PAOLA;
2006
Abstract
Antimicrobial peptides and proteins are being studied with increasing interest because of their broad range antimicrobial activity. Among plant antimicrobial proteins, the wheat seed polypeptides, puroindoline a and puroindoline b, are particularly interesting because of their established antibacterial activity. In this paper we describe different strategies used to clone His tagged and GST tagged puroindolines obtaining 1.5 mg recombinant protein from 1 l culture. The antimicrobial activity of recombinant and native puroindolines was comparable.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
