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2.
Zhonghua Bing Li Xue Za Zhi ; 49(9): 946-948, 2020 Sep 08.
Article in Chinese | MEDLINE | ID: mdl-32892566
3.
Biol Chem ; 377(12): 825-31, 1996 Dec.
Article in English | MEDLINE | ID: mdl-8997493

ABSTRACT

Porrectin, a new type II ribosome-inactivating protein (RIP), was purified from the seeds of the camphor tree (Cinnamomum porrectum) by affinity chromatography on acid-treated Sepharose 4B. Porrectin is a glycoprotein (M(r)64,500, sugar content 2.5%) consisting of an A-chain (M(r)30,500) and a B-chain (M(r)33,500) linked by the disulfide bond. The terminal sugar of glycan in porrectin B-chain is determined to be mannose. By non-denaturing polyacrylamide gel electrophoresis, porrectin displayed three isoforms that have different pl values with the same molecular weight. Porrectin is a potent inhibitor of eukaryotic protein synthesis in the rabbit reticulocyte lysate system. The molecular mechanism of action of porrectin on rat liver ribosomes is demonstrated to be specific for RNA N-glycosidase. The cleavage site is the adenosine at position 4324 (rat liver 28S rRNA) embedded in the highly conserved ricin/alpha-sarcin ('R/S') domain.


Subject(s)
N-Glycosyl Hydrolases/metabolism , Plant Proteins/isolation & purification , Protein Synthesis Inhibitors/isolation & purification , Ribosomes/drug effects , Seeds/chemistry , Algal Proteins , Animals , Carbohydrates/chemistry , Hemagglutination/drug effects , Liver/drug effects , Molecular Weight , N-Glycosyl Hydrolases/chemistry , N-Glycosyl Hydrolases/isolation & purification , N-Glycosyl Hydrolases/pharmacology , Plant Proteins/chemistry , Plant Proteins/pharmacology , Protein Synthesis Inhibitors/chemistry , Protein Synthesis Inhibitors/pharmacology , Proteins , Rabbits , Rats , Ribosome Inactivating Proteins , Ribosome Inactivating Proteins, Type 2 , Trees
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