Isolation and partial characterization of nigrin b, a non-toxic novel type 2 ribosome-inactivating protein from the bark of Sambucus nigra L.
The bark of Sambucus nigra L. contains a non-toxic novel type 2 ribosome-inactivating protein that we named nigrin b. In vitro, nigrin b strongly inhibited mammalian protein synthesis but did not affect plant nor bacterial protein synthesis. The protein (M(r) 58,000) contains two subunits, A (M(r) 26,000) and B (M(r) 32,000); linked by disulphide bridge(s). Nigrin b was found to be an rRNA N-glycosidase of the rRNA of intact mammalian ribosomes and shares a very good N-terminal amino-acid sequence homology with the anti-HIV-1 proteins TAP 29 and trichosanthin.
Girbés
T
T
Departamento de Bioquimíca y Biología Molecular, Facultad de Ciencias, Universidad de Valladolid, Spain.
Citores
L
L
Ferreras
J M
JM
Rojo
M A
MA
Iglesias
R
R
Muñoz
R
R
Arias
F J
FJ
Calonge
M
M
García
J R
JR
Méndez
E
E
D000595:Amino Acid Sequence; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D006386:Hemagglutination Tests; D008969:Molecular Sequence Data; D009699:N-Glycosyl Hydrolases / Q000737:chemistry / Q000302:isolation & purification* / Q000494:pharmacology; D010940:Plant Proteins / Q000302:isolation & purification* / Q000494:pharmacology; D012335:RNA, Ribosomal / Q000378:metabolism; D011817:Rabbits; D051381:Rats; D054788:Ribosome Inactivating Proteins; D054790:Ribosome Inactivating Proteins, Type 2; D012270:Ribosomes / Q000187:drug effects*; D017386:Sequence Homology, Amino Acid; D014197:Trees / Q000737:chemistry*
D010940:Plant Proteins; D012335:RNA, Ribosomal; D054790:Ribosome Inactivating Proteins, Type 2; D009699:N-Glycosyl Hydrolases; D054788:Ribosome Inactivating Proteins