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Seite 1 von 27 Ergebnisse
Albumin and Ricinus communis agglutinin decrease endothelial permeability via interactions with matrix.
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We studied the effects of albumin and the lectin Ricinus communis agglutinin (RCA) on hydraulic conductivity (Lp) of bovine pulmonary microvascular endothelial cell monolayers (BPMVEC) because of the evidence that albumin and RCA can interfere with transendothelial albumin permeability
Temporal and spatial expression of 2S albumin in castor (Ricinus communis L.).
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We studied the temporal and spatial expression of the 2S albumin in castor (Ricinus communis L.) during seed development, germination, post-germination, and plant development. Quantitative polymerase chain reaction analysis showed that the 2S albumin transcript accumulated to a maximum level at the
An allergenic 2S storage protein from Ricinus communis seeds which is a part of the 2S albumin precursor predicted by c-DNA data.
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1. A 1.9S albumin having allergenic activity and denoted Ric c III was isolated from an alcohol extract of defatted Ricinus communis seeds, CB-1A, as a homogeneous protein by ion-exchange chromatography on SP-Sephadex, gel filtration on Sephadex G-75 and preparative polyacrylamide gel
Amino acid sequence of a new 2S albumin from Ricinus communis which is part of a 29-kDa precursor protein.
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The isolation and sequence determination of a new 2S albumin storage protein from Ricinus communis seeds denoted 2S ASP-Ib are described. The fragment approach using selective enzymatic cleavage, Edman degradation, and mass spectrometry was used to demonstrate that the 11-kDa heterodimer protein
In silico structural characteristics and α-amylase inhibitory properties of Ric c 1 and Ric c 3, allergenic 2S albumins from Ricinus communis seeds.
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The major Ricinus communis allergens are the 2S albumins, Ric c 1 and Ric c 3. These proteins contain a trypsin/α-amylase inhibitor family domain, suggesting that they have a role in insect resistance. In this study, we verified that Ric c 1 and Ric c 3 inhibited the α-amylase activity of
Ric c 1 and Ric c 3, the allergenic 2S albumin storage proteins of Ricinus communis: complete primary structures and phylogenetic relationships.
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The 2S albumin storage protein of Ricinus communis consists of the two heterodimeric proteins Ric c 1 and Ric c 3 each of which is composed of a small and a large subunit linked together by disulphide bridges. The complete primary structures of both heterodimeric proteins were determined by
The Ricinus communis 2S albumin precursor: a single preproprotein may be processed into two different heterodimeric storage proteins.
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The Ricinus communis (castor bean) 2S albumin is a heterodimer of glutamine-rich, disulphide-linked 4 and 7 kDa polypeptide. A cDNA library was constructed using mRNA from maturing castor bean endosperm as template. Clones containing sequences complementary to albumin mRNA were isolated by
Transport of ricin and 2S albumin precursors to the storage vacuoles of Ricinus communis endosperm involves the Golgi and VSR-like receptors.
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We have studied the transport of proricin and pro2S albumin to the protein storage vacuoles of developing castor bean (Ricinus communis L.) endosperm. Immunoelectron microscopy and cell fractionation reveal that both proteins travel through the Golgi apparatus and co-localize throughout their route
Solution structure of RicC3, a 2S albumin storage protein from Ricinus communis.
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The three-dimensional structure in aqueous solution of recombinant (15)N labeled RicC3, a 2S albumin protein from the seeds of castor bean (Ricinus communis), has been determined by NMR methods. The computed structures were based on 1564 upper limit distance constraints derived from NOE
A 2S Albumin from the Seed Cake of Ricinus communis Inhibits Trypsin and Has Strong Antibacterial Activity against Human Pathogenic Bacteria.
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Hospital-acquired infections caused by antibiotic-resistant bacteria threaten the lives of many citizens all over the world. Discovery of new agents to hinder bacterial development would have a significant impact on the treatment of infections. Here, the purification and characterization of
RcAlb-PepII, a synthetic small peptide bioinspired in the 2S albumin from the seed cake of Ricinus communis, is a potent antimicrobial agent against Klebsiella pneumoniae and Candida parapsilosis.
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Antimicrobial peptides (AMPs) are important constituents of the innate immunity system of all living organisms. They participate in the first line of defense against invading pathogens such as viruses, bacteria, and fungi. In view of the increasing difficulties to treat infectious diseases due to
Assignment of 1H and 15N resonances and secondary structure of the recombinant RicC3 of 2S albumin storage protein from Ricinus communis.
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Nucleotide sequence of a Ricinus communis 2S albumin precursor gene.
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Ricin and Ricinus communis agglutinin subunits are all derived from a single-size polypeptide precursor.
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Antibodies have been raised in rabbits against the individually purified A and B subunits of the toxic castor bean lectin, ricin, and against the A' and B' subunits of Ricinus communis agglutinin type I. Each of the antisera recognised a single polypeptide species of Mr 60 500 when maturing castor
Mapping IgE-binding epitopes of Ric c 1 and Ric c 3, allergens from Ricinus communis, by mast cell degranulation assay.
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Ric c 1 and Ric c 3 are the major castor bean allergens. In order to identify continuous IgE-epitopes in Ric c 1 and Ric c 3, pools of sera from rats immunized with a pool of 2S albumin from these seeds, Ric c 1 and Ric c 3 overlapping synthetic peptides, were used to screen for IgE-binding
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