Isolation and characterization of a reserve protein from the seeds of Opuntia ficus-indica (Cactaceae).
We describe here the isolation and characterization of a major albumin from the seeds of Opuntia ficus-indica (Cactaceae). This protein has a molecular mass of 6.5 kDa and was isolated by a combination of gel filtration chromatography and reverse-phase HPLC. The amino acid composition of this protein was determined and it was shown to have similarities with the amino acid composition of several proteins from the 2S albumin storage protein family. The N-terminal amino acid sequence of this protein is Asp-Pro-Tyr-Trp-Glu-Gln-Arg.
Uchoa
A F
AF
Departamento de Bioquímica e Biologia Molecular, Universidade Federal do Ceará, Fortaleza, CE, Brasil.
Souza
P A
PA
Zarate
R M
RM
Gomes-Filho
E
E
Campos
F A
FA
D000418:Albumins / Q000737:chemistry / Q000302:isolation & purification; D000596:Amino Acids / Q000032:analysis / Q000737:chemistry; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D011506:Proteins / Q000737:chemistry* / Q000302:isolation & purification*; D012639:Seeds / Q000737:chemistry*
D000418:Albumins; D000596:Amino Acids; D011506:Proteins