পৃষ্ঠা 1 থেকে 45 ফলাফল
Two novel highly basic type 1 (single chain) ribosome-inactivating proteins (RIPs) with N-glycosidase activity have been found in elderberries (the fruits of Sambucus nigra L.). Mass spectrometry of these RIPs, which we named nigritins f1 and f2, gave Mr values of 24095 and 23 565, respectively.
A second NeuAc(alpha2,6)Gal/GalNAc binding type 2 ribosome-inactivating protein (RIP), called SNAI' has been isolated from elderberry (Sambucus nigra) bark. SNAI' is a minor bark protein which closely resembles the previously described major Neu5Ac(alpha2,6)Gal/GalNAc binding type 2 RIP called SNAI
The major protein of elderberry (Sambucus nigra L.) fruits is a lectin, called Sambucus nigra agglutinin IVf or SNAIVf. This lectin is composed of subunits that strongly resemble the B chain of the type 2 ribosome-inactivating protein (RIP), called SNAVf, present in the same tissue. To corroborate
One of the predominant proteins in the bark of elderberry (Sambucus nigra) has been identified as a novel type 2 ribosome-inactivating protein that exhibits a normal RNA N-glycosidase activity, but is devoid of carbohydrate binding activity. Sequence analysis of the corresponding cDNA clones
Nigrin b, a lectin isolated from the bark of elderberry (Sambucus nigra L.), has structure and enzymatic activity similar to that of ricin and other type 2 ribosome inactivating proteins (RIPs), and yet is much less toxic to cells and animals. In an attempt to explain this difference, we studied (1)
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)
A novel, strongly basic, two-chain ribosome-inactivating protein (RIP) with an apparent Mr of 64000 by SDS-PAGE and 63469 by mass spectrometry analysis, that we have named basic nigrin b, has been found in the bark of elder (Sambucus nigra L.). The new protein does not agglutinate red blood cells,
A new N-glycosidase ribosome-inactivating protein (RIP) belonging to the novel family of the nontoxic type 2 RIPs from Sambucaceae has been isolated from rhizomes of dwarf elder (Sambucus ebulus L.) and named ebulin r. Dwarf elder rhizomes also contain a novel monomeric N-Ac-galactosamine-binding
Two monomeric lectins, SSA-b-3 and SSA-b-4, were purified from the bark tissue of Japanese elderberry, Sambucus sieboldiana. SDS-PAGE of the purified lectins showed the presence of single bands of 35 and 33 kDa for SSA-b-3 and SSA-b-4, respectively, irrespective of the presence of reducing agent. MS
In recent years, different classes of proteins have been reported to promote toxic effects when ingested. Type-2 ribosome-inactivating proteins (RIPs) are a group of chimeric proteins built up of an A-chain with RNA N-glycosidase activity and a B-chain with lectin activity. These proteins are
A type II ribosome-inactivating protein (RIP) was isolated from the bark tissue of Japanese elderberry (Sambucus sieboldiana) and named sieboldin-b. Sieboldin-b is a heterodimeric protein consisting of 27- and 33-kDa subunits and showed strong ribosome-inactivating activity in vitro but did not show
Although the type-2 ribosome-inactivating proteins (SNA-I, SNA-V, SNLRP) from elderberry (Sambucus nigra L.) are all devoid of rRNA N-glycosylase activity towards plant ribosomes, some of them clearly show polynucleotide-adenosine glycosylase activity towards tobacco mosaic virus RNA. This
Sambucus nigra agglutinin I (SNA-I) is a type 2 ribosome-inactivating protein. Site-directed mutagenesis was used to mimic the conversion of the highly active B-chain of fruit-specific SNA (SNA-If) into the completely inactive B-chain of the closely related and naturally occurring loss-of-activity
Fruits of elderberry (Sambucus nigra) express small quantities of a type-2 ribosome-inactivating protein with an exclusive specificity towards the NeuAc(alpha2,6)Gal/GalNAc disaccharide and a unique molecular structure typified by the occurrence of a disulfide bridge between the B-chains of two
Analysis of affinity-purified preparations of the fetuin-binding proteins from elderberry bark and fruits revealed besides the previously reported Neu5Ac(alpha-2,6)Gal/GalNAc-specific type 2 ribosome-inactivating proteins (RIP) the occurrence of single chain proteins of 22 kDa, which according to