2 edition of Recognition of N-acetylgalactosamine by lectins from the Codium genus found in the catalog.
Recognition of N-acetylgalactosamine by lectins from the Codium genus
Lucy Jane Swain
by University of Portsmouth, School of Pharmacy and Biomedical Sciences in Portsmouth
Written in English
Thesis (Ph.D.) - University of Portsmouth, 1998.
|Statement||Lucy Jane Swain.|
GSL II is affinity purified tetramer that contains a single type of 30 kDa subunit. It has insecticidal structure/function, the first GlcNAc binding legume lectin proven to have insecticidal lectin has a carbohydrate specificity for αGal and αGalNAc and elutes with galactose or N-acetylgalactosamine. Incr Origin and epidemiology. Dengue virus (DENV) is a member of the Flavivirus genus within the family of the Flaviviridae and is the most common mosquito-borne viral iruses derived from a common viral ances years ago. DENV has a relative recent revolutionary history originating years ago and establishes transmission in humans since a few hundred ://
Deformation and curling of axillary hairs upon inoculation occurs in Arachis and Stylosanthes [29, 30], but root hair curling is not a prerequisite of infection and nodulation. Bradyrhizobium cells were even seen to be entrapped within ‘shepherd’s crooks’ (which are always observed with the infection thread mode), but penetration of the root hair by bradyrhizobia in the crook and An overview on the diversity of 39 lectins from the phylum Porifera is presented, including 38 lectins, which were identified from the class of demosponges, and one lectin from the class of hexactinellida. Their purification from crude extracts was mainly performed by using affinity chromatography and gel filtration techniques. Other protocols were also developed in order to collect and study
Kakiuchi M, Okino N, Sueyoshi N et al. Purification, characterization and cDNA cloning of alpha-N-acetylgalactosamine-specific lectin from starfish, Asterina pectinifera. Glycobiology ; 12(2)– PubMed Google Scholar N.J. Maeji, T. Inoue, and R. Chujo, The role of the N-acetyl group in determining the conformation of 2 acetamidodeoxy-D-galactopyranosyl-threonine-containing peptides. Carbohydr. Res. C4-C8 (). CrossRef Google Scholar
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Among these, the lectins from the Codium, C. fragile ssp. tomentosoides, 22)C. fragile ssp. atlanticum, C. tomentosum,23) and C. giraﬀa24) are commonly speciﬁc for N-acetylgalactosamine and/or N-acetylglucosamine and consist of oligomeric forms, except for a monomeric lectin from C.
giraﬀa. The resemblance of the lectin called this lectin, shares some characteristics with other lectins isolated from the same genus. It is a monomeric It is a monomeric protein with a relative molecular weight of 17, as shown by The R-type lectins are members of a superfamily of proteins, all of which contain a carbohydrate-recognition domain (CRD) that is structurally similar to the CRD in ricin.
Ricin was the first lectin discovered and it is the prototypical lectin in this category. R-type lectins are present in plants, animals, and bacteria, and the plant lectins often contain a separate subunit that is a potent lectins than isolation of lectins from fruit bodies.
This method allows full control of the process and, if necessary, the use of regulators for the synthesis of these :// In contrast, due usually algal lectins have binding specificity of complex sugars, affinity chromatography has been used a few times, such as the lectins of green algae of the genus Codium [83,84 The occurrence in nature of proteins with hemagglutinating activity that in later years were shown to be sugar-specific and eventually named lectins has been known since the turn of the 19th century, but until about two decades ago they aroused little interest (for a historical survey, see Ref.
1).My own involvement with these proteins began inadvertently and initially on a part-time basis in Recent crystal structure data (Table provides a list of microbial sialic acid-specific lectins of known structure) have done little to resolve the exact involvement, if any, of sialic acids in sialidase-insensitive rotavirus recognition of host r human sialidase-insensitive strains DS-1 or Wa VP8* have been crystallized with sialic acid or sialic acid-derivatives bound to the Some Codium lectin shows preferential affinity for a carbohydrate marker of cancer.
Thus, the lectins of the genus Codium are interesting targets for their application as biochemical and clinical reagents, as well as to provide insight into the molecular evolution of lectins in the plant kingdom.
This study was performed to clarify the A lectin from the alga Codium giraffa, reported as an endemic species of Mexico, was purified by a combination of ammonium sulfate fractionation, affinity and anion exchange chromatographies.
Giraffine, as we called this lectin, shares some characteristics with other lectins isolated from the same :// Volumenumber 2, FEB June The Second Datta Lecture Bacterial lectins, cell-cell recognition and infectious disease Nathan Sharon Department of Biophysics, The Weizmann Institute of Science, RehovotIsrael Received 22 April Numerous bacterial strains produce surface lectins, commonly in the form of fimbriae that are filamentous assemblies of protein Molecular Recognition of N-Acetylneuraminic Acid by Acyclic Pyridinium- and Quinolinium-Based Receptors in Aqueous Media: Recognition through Combination of Cationic and Neutral Recognition Sites.
The Journal of Organic Chemistry78 (2), DOI: /:// In contrast, due usually algal lectins have binding specificity of complex sugars, affinity chromatography has been used a few times, such as the lectins of green algae of the genus Codium [83,84,85], lectins from Ulva lactuca, Caulerpa cupressoides, Enteromorpha prolifera, Ulva pertusa, Bryopsis plumosa [90,91,92], Bryopsis hypnoides and One of the earliest reviews on plant lectins was published by Boyd (), going back as far as in his review.
Sharon wrote an early review in and co-published a more extensive one (Sharon and Lis) in Pusztai () devoted a book to Plant Lectins However there are a few reports showing that some of these molecules may be inhibited by simple sugars and are cation dependent as showed for the lectins from the green marine alga genus, Codium They show remarkable structural diversity and are generally found glycosidically linked to either galactose (Gal), N-acetylglucosamine (GlcNAc), N-acetylgalactosamine (GalNAc) or as α-(2→8)-linked homopolymers known as polysialic acid.
This chapter summarizes the role of sialic acid-specific lectins in mediating host cell attachment by The lectins, that can be used as tools to study glycobiological systems are defined as applied lectins (1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14).They are easily This chapter describes the sialic acid family of monosaccharides, with respect to their biosynthesis, structural diversity, and linkage to the underlying glycan chain.
Also mentioned are the general principles behind different methods for their study. The biological and pathophysiological roles of sialic acids are briefly considered, particularly the functional significance of lectins that ?report=reader.
Recognition of viral glycans by pattern recognition receptors (PRRs) in innate immunity contributes to antiviral immune responses. C-type lectin receptors (CLRs) are PRRs capable of sensing glycans present in viral pathogens to activate antiviral immune responses such as phagocytosis, antigen processing and presentation, and subsequent T cell :// Piller, V., Piller, F., Carton, J.P.
Isolation and characterization of an N-acetylgalactosamine specific lectin from Salvia sclarea seeds J. Biol. Chem. Google Scholar Piller, V., Piller, F., Carton, J.P. Comparison of the carbohydrate-binding specificities of seven N -acetyl-D-galactosamine-recognizing lectins Eur.
J Sialic acids possess contrasting character of working as masking element of an array of cell surface receptors whereas on the other side these function as a recognition site for various lectins and antibodies, indicating the unique nature of the molecule 2,3,4,://.
1. Introduction. Ricin (RCA 60) is a heterodimeric protein of ≈ 60–65 kDa molecular mass isolated from seeds of the castor plant, Ricinus communis (family Euphorbiaceae). It consists of two polypeptides A (32 kDa) and B (34 kDa), linked via a single disulfide bond.The heavy B-chain possesses the carbohydrate-binding sites (specific for galactose and N-acetylgalactosamine), In the same way, it has been proposed, that a high consumption of galactose-containing carbohydrates, such as galactose-containing vegetable fiber, would offer protection against binding and proliferative effects of galactose-N-acetylgalactosamine-binding dietary lectins (such as PNA) on colonic neoplastic epithelium [, ].Abstract.
In the current study, 55 Penicillium species were screened for lectin activity using erythrocytes of human ABO, pig, sheep, goat and rabbit. Only four Penicillium species, namely P.
duclauxii, P. griseoroseum, P. proteolyticum and P. caseifulfum exhibited lectin activity, while crude undiluted mycelial extract of six species (P. aragonense, P. coralligerum, P. lagena, P. pinophilum