Biochemical characterization of cowpea seed proteins (Contributo in volume (capitolo o saggio))

Type
Label
  • Biochemical characterization of cowpea seed proteins (Contributo in volume (capitolo o saggio)) (literal)
Anno
  • 1989-01-01T00:00:00+01:00 (literal)
Alternative label
  • Pedalino M.; Paino D'urzo M.; Costa A.; Grillo S.; Rao R. (1989)
    Biochemical characterization of cowpea seed proteins
    in Cowpea Genetic Resources, 1989
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Pedalino M.; Paino D'urzo M.; Costa A.; Grillo S.; Rao R. (literal)
Pagina inizio
  • 81 (literal)
Pagina fine
  • 89 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#titoloVolume
  • Cowpea Genetic Resources (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#pagineTotali
  • 9 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Istituto di Genetica Vegetale (literal)
Titolo
  • Biochemical characterization of cowpea seed proteins (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#isbn
  • 978-131-053-7 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autoriVolume
  • N.Q. NG; L.M. Monti (literal)
Abstract
  • Total seed proteins and the albumin and globulin fractions were analysed in 35 accessions using various electrophoretic techniques. Two major pattern types for total proteins were observed; 8 accessions possessed 23- and 32-kDa globulin subunits (type A) while the remaining 27 accessions lacked them (type B). The seed albumin fraction proved heterogeneous; the accessions differed in number, molecular weight and relative intensity of polypeptides belonging to the 63- and 95-kDa major subunits. Two major globulins, CP1 and CP2, were observed in all accessions. CP1 consisted of the 49-, 58- and 63-kDa major subunits, while CP2 was more complex, also having the 49- and 58-kDa subunits as well as the 23- and 32-kDa units of protein pattern type A accessions. The 3 major subunits were heterogeneous and consisted of similar multiple charge forms in the pH range 4.6-5.1. Three globulin subunits, with molecular weight 94,5, 87 and 40 kD, were found to be composed of disulfide-linked subunits. Since the 87 kD subunit consists oh both acidic (63 kD) and basic (22 kD) disukfide-bonded polypeptides, it could be considered a legumin-like component. (literal)
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