PMID- 24196668
OWN - NLM
STAT- PubMed-not-MEDLINE
DCOM- 20131108
LR  - 20211021
IS  - 0032-0935 (Print)
IS  - 0032-0935 (Linking)
VI  - 181
IP  - 1
DP  - 1990 Apr
TI  - Purification and characterization of ten new rice NaCl-soluble proteins: 
      identification of four protein-synthesis inhibitors and two 
      immunoglobulin-binding proteins.
PG  - 1-9
LID - 10.1007/BF00202318 [doi]
AB  - Ten new proteins from rice (Oryza saliva L. cv. Bahia) including four 
      protein-synthesis inhibitors and two immunoglobulin E (IgE)-binding proteins have 
      been isolated and characterized. These proteins as well as one previously known 
      component, alpha-globulin, were purified from a 0.5 M NaCl extract of rice endosperm 
      by a new, apparently non-denaturing, isolation procedure developed for rice 
      proteins. The method is based on extractions of this complex protein mixture with 
      a diluted volatile salt solution and an aqueous solution of ethanol. This 
      preliminary step results in an improvement in the separation of these proteins, 
      thus facilitating their subsequent purification by reversed-phased 
      high-performance liquid chromatography. These new proteins have similar relative 
      molecular masses (Mrs) from 11000 to 17000. The purity of the proteins was 
      analyzed by micro two-dimensional gel electrophoresis. Four of these components 
      were found to be in-vitro protein-synthesis inhibitors in a cell-free system from 
      rat brain. The NH2-terminal amino-acid sequences of these four inhibitors were 
      determined from 12 to 26 cycles after direct blotting of the separated proteins 
      from electrophoresis gels. Three of these proteins with Mrs between 16000 and 
      17000 showed a high degree of homology ranging from 57% to 75% but seem to be 
      unrelated to the fourth inhibitor. In addition, the alpha-globulin and one of the new 
      low-molecular-weight proteins of Mr 12500 seemed to show allergenic properties 
      since they bound IgE antibodies from the sera of hypersensitive patients. Boths 
      proteins have blocked NH2-terminal amino acids.
FAU - Limas, G G
AU  - Limas GG
AD  - Servicio de Endocrinologia, Hospital "Ramon y Cajal", E-28034, Madrid, Spain.
FAU - Salinas, M
AU  - Salinas M
FAU - Moneo, I
AU  - Moneo I
FAU - Fischer, S
AU  - Fischer S
FAU - Wittmann-Liebold, B
AU  - Wittmann-Liebold B
FAU - Mendez, E
AU  - Mendez E
LA  - eng
PT  - Journal Article
PL  - Germany
TA  - Planta
JT  - Planta
JID - 1250576
EDAT- 1990/04/01 00:00
MHDA- 1990/04/01 00:01
CRDT- 2013/11/08 06:00
PHST- 1989/04/04 00:00 [received]
PHST- 1989/09/06 00:00 [accepted]
PHST- 2013/11/08 06:00 [entrez]
PHST- 1990/04/01 00:00 [pubmed]
PHST- 1990/04/01 00:01 [medline]
AID - 10.1007/BF00202318 [doi]
PST - ppublish
SO  - Planta. 1990 Apr;181(1):1-9. doi: 10.1007/BF00202318.