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    STUDIA BIOLOGIA - Issue no. 1 / 2007  
         
  Article:   PARTIAL BIOCHEMICAL CHARACTERIZATION OF STORAGE PROTEIN FROM ALEURONE CELLS OF BARLEY (HORDEUM VULGARE L.).

Authors:  HORIA L. BANCIU, FLORINA OLARU, VERENA HENGST, MANUELA BANCIU, IOAN PETRESCU, AURORA MOCANU, CORNELIU TARBA, TRAIANOS YUPSANIS, MARIA TOMOAIA-COTIŞEL. 		 
       
         
  Abstract:  The present paper focuses on the characterization of 7S globulin regarding its biochemical and biophysical properties. 7S globulin was extracted by the purification of aleurone cells of barley (Yupsanis et al., 1990). This protein belongs to the storage protein class with important roles in providing the amino acids during germination of plants. 7S globulin from barley aleurone was found to be positively-charged since the measurement of zeta potential revealed a value of +17 mV. Spectrofluorimetric measurements using the anionic probe ANS (anilino-naphtalene sulfonate) showed that the positive amino acids are probably located mainly on the external surface of protein. 7S globulin is chemically stable up to 6 M urea and consists of 4 different subunits with molecular weights of 65, 37, 25 and 20 kDa. Due to its chemical and physical properties this protein may be of interest for nanobiotechnology of surface coatings (glass, mica, silicone etc).  
         
     
         
         
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