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glycosidase/holunder
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Seite 1 von 35 Ergebnisse
Impact of bacterial vaginosis, as assessed by nugent criteria and hormonal status on glycosidases and lectin binding in cervicovaginal lavage samples.
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The objective of this study was to evaluate the impact of hormonal status and bacterial vaginosis (BV) on the glycosidases present and glycosylation changes as assessed by lectin binding to cervicovaginal lavage constituents. Frozen cervicovaginal lavage samples from a completed study examining the
Analysis of recombinant Duffy protein-linked N-glycans using lectins and glycosidases.
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Duffy antigen is a glycosylated blood group protein acting as a malarial and chemokine receptor. Using glycosylation mutants we have previously demonstrated, that all three potential glycosylation sites of the Duffy antigen are occupied by N-linked oligosaccharide chains. In this study, wild-type
Ribosome-inactivating lectins with polynucleotide:adenosine glycosidase activity.
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Lectins from Aegopodium podagraria (APA), Bryonia dioica (BDA), Galanthus nivalis (GNA), Iris hybrid (IRA) and Sambucus nigra (SNAI), and a new lectin-related protein from Sambucus nigra (SNLRP) were studied to ascertain whether they had the properties of ribosome-inactivating proteins (RIP). IRA
Substrate specificities of glycosidases from Aspergillus species pectinase preparations on elderberry anthocyanins.
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Attractive color is one of the most important sensory characteristics of fruit and berry products, and elderberry juice is widely used as natural colorant. When pectinase preparations were used in the production of elderberry juice for clarification, a concomitant decrease of anthocyanins and thus a
The major Kurloff cell glycoproteins: lectin affinities, glycosidase susceptibilities and relationship with the sialylated acid phosphatases of the Kurloff body.
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Urea-soluble fractions from purified Kurloff cells (KC) were analysed by affinoblotting. Lectin reactivities were quasi-exclusively confined to the 30-35 kDa major glycoproteins (mGPs) (responsible for the PAS positivity of the Kurloff body) with strong affinities for Canavalia ensiformis lectin,
Ebulitins: a new family of type 1 ribosome-inactivating proteins (rRNA N-glycosidases) from leaves of Sambucus ebulus L. that coexist with the type 2 ribosome-inactivating protein ebulin 1.
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A new family of single chain (type 1) ribosome-inactivating proteins (RIPs), that we have named ebulitins, have been found in mature leaves of Sambucus ebulus L., a caprifoliaceae plant also known to contain a non-toxic two chain (type 2) RIP named ebulin I in its leaves. Ebulitins are basic
Constitutive and inducible type 1 ribosome-inactivating proteins (RIPs) in elderberry (Sambucus nigra L.).
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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.
Isolation and molecular cloning of a novel type 2 ribosome-inactivating protein with an inactive B chain from elderberry (Sambucus nigra) bark.
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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
Purification and partial characterization of a novel lectin from elder (Sambucus nigra L.) fruit.
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A previously unknown haemagglutinin, named Sambucus nigra agglutinin-III (SNA-III), has been purified from the fruit of the elder (Sambucus nigra). Whereas elder bark agglutinin I (SNA-I) is highly specific for terminal alpha 2,6-linked sialic acid residues, SNA-III displays a high affinity for
Site specific N-glycan profiling of NeuAc(α2-6)-Gal/GalNAc-binding bark Sambucus nigra agglutinin using LC-MSn revealed differential glycosylation.
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The bark of Sambucus nigra contains a complex mixture of glycoproteins that are characterized as chimeric lectins known as type II ribosome inactivating proteins and holo lectins. These type II ribosome inactivating proteins possess RNA N-glycosidase activity in subunit A and lectin activity
Isolation and partial characterization of nigrin b, a non-toxic novel type 2 ribosome-inactivating protein from the bark of Sambucus nigra L.
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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)
Characterization of a new non-toxic two-chain ribosome-inactivating protein and a structurally-related lectin from rhizomes of dwarf elder (Sambucus ebulus L.).
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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
Entomotoxic action of Sambucus nigra agglutinin I in Acyrthosiphon pisum aphids and Spodoptera exigua caterpillars through caspase-3-like-dependent apoptosis.
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In this project, the toxicity and mechanism of action of the ricin-B-related lectin SNA-I from elderberry (Sambucus nigra) in the pea aphid (Acyrthosiphon pisum) and the beet armyworm (Spodoptera exigua), two important pest insects in agriculture, were studied. SNA-I is a chimeric lectin belonging
Carbohydrate-binding activity of the type-2 ribosome-inactivating protein SNA-I from elderberry (Sambucus nigra) is a determining factor for its insecticidal activity.
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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
Characterization of human arylsulfatase A glycans.
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Despite numerous studies on arylsulfatase A, the structure of the glycans present in each of its two subunits has not been determined. This is important because the carbohydrate component of human arylsulfatase A synthesized in tumor tissues and transformed cells has been shown to undergo apparent
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