Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: DrugBank:APRD00080 (Leaf)
 21,685 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The lectin from horse chestnut seeds was obtained by affinity chromatography on a sorbent prepared from the egg white, 95 mg of lectin per 1 kg of fresh seeds being obtained. Molecular weight was determined by gel-filtration on tojopearl HW-55 and it composed 132 kDa. SDS-polyacrylamide gel electrophoresis revealed the presence of one component with molecular weight of 33 kDa. One band has been revealed by means of disc-electrophoresis in acidic (pH 4.5) and alkaline system (pH 8.9). Sugar was not detected in the lectin. Amino acid composition of the lectin has been determined. The lectin agglutinated horse erythrocytes in minimal concentration of 9.5 ngml, to the less extent rabbit (4.9 mkg/ml), rat (62 mkg/ml), human (73 mkg/ml), but did not agglutinate erythrocytes of a sheep and cow. Purified lectin did not interact with monosaccharides, but interacted with O-glycans.
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PMID:[Isolation of lectin from horse chestnut (Aesculus hippocastanum L.) seeds and study of its interaction with carbohydrates and glycoproteins]. 146 70

Oral streptococci vary in their susceptibility to salivary agglutinin-mediated aggregation. To understand the molecular basis of this specificity, the structure and function of receptors for agglutinin from Streptococcus mutans KPSK2 (MSL-1) and Streptococcus sanguis M5 (SSP-5) were compared. Immunological screening of an S. mutans KPSK2 genomic DNA library yielded two identical clones expressing a streptococcal protein that co-migrated with a 220 kDa peptide in SDS extracts from this organism. This protein inhibited agglutinin-mediated aggregation of S. mutans KPSK2 in a dose-dependent manner. The MSL-1 gene is homologous to the S. mutans SpaP and pac genes although single base substitutions alter several amino acids. MSL-1 is also similar to the agglutinin receptor (SSP-5) cloned from S. sanguis M5. All three proteins, MSL-1, P1, and SSP-5 share at least one epitope since monoclonal and polyclonal anti-SSP-5 antibodies react with both MSL-1 and P1. However, other monoclonal antibodies are specific for SSP-5 and appear to react with a peptide domain exhibiting little homology to MSL-1 or P1. Sugar inhibition studies showed that agglutinin-mediated aggregation of S. mutans KPSK2 was most potently inhibited by fucose and lactose. Sialic acid, a potent inhibitor of S. sanguis aggregation, had no effect on the interaction of agglutinin with S. mutans KPSK2. These results suggest that while the MSL-1 and SSP-5 proteins are genetically and immunologically related, their specificity for binding sites on agglutinin differs.
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PMID:Comparison of Streptococcus mutans and Streptococcus sanguis receptors for human salivary agglutinin. 170 78

Physicochemical and immunological properties of buffalo pituitary lutropin (buffalo LH) are reported here. The preparation was shown to be homogeneous by several physicochemical criteria. The molecular weight was found to be 30,000-40,000 by SDS-PAGE, GP-HPLC, and ultracentrifugation analyses. It showed certain interesting features, such as anomalous sedimentation behavior, microheterogeneity due to sugar-linked sulfate, and weak immunogenicity in rabbits. The subunit nature of the hormone has been confirmed. Sugar composition showed similarities as well as differences with LH of other species. Preliminary data on the homologous and heterologous RIAs, using iodinated sheep LH and buffalo LH and the respective antisera, have also been given.
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PMID:Studies on buffalo pituitary lutropin (LH): physicochemical and immunological properties. 207 24

The sugar composition and the electrophoretic mobility in SDS-polyacrylamide gel electrophoresis of the various lipopolysaccharides (LPS) from clinical isolates of Haemophilus influenzae type b (Hib) were determined to correlate epidemiologic data with compositional data. Rabbit sera specific in Ouchterlony immunodiffusion for 10 different LPS (LPS 1-10) reacted with 647 or 690 Hib strains isolated from patients with invasive disease in various continents. Serotype 1 was predominant and was found in 550 isolates (80%). None of the Hib isolates reacted with antisera specific for LPS of two nonencapsulated isolates (LPS 5 and 6). Sugar analysis by gas-liquid chromatography of trimethylsilylated methyl glycosides revealed that the LPS of the 10 serotypes contained glucose, galactose, L-glycero-D-mannoheptose, and glucosamine in various proportions. LPS 1, 2, 8, and 9 contained the highest amounts of glucose and galactose relative to L-glycero-D-mannoheptose, which is considered present in constant amounts in H. influenzae LPS. LPS 1, 2, and 9 were most frequently found in invasive disease isolates.
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PMID:Biochemical characterization and worldwide distribution of serologically distinct lipopolysaccharides of Haemophilus influenzae type b. 211 26

An antibody has been raised against rape seed enoyl-ACP reductase. This recognizes both the alpha and beta polypeptides of the enzyme. Immunoblotting of fresh seed demonstrates that beta is not present in seed material, and that it is produced by proteolysis during isolation. It is thus deduced that rape seed enoyl reductase is an alpha 4 homotetramer. Leaf material from both rape and Arabidopsis have an enoyl reductase with a similar electrophoretic mobility to the rape seed enzyme when analyzed on SDS-PAGE. Quantitative immunoassay has demonstrated that the enzyme continually increases during lipid deposition, indicating that an increase in this enzyme is required to sustain high levels of lipid biosynthesis. In vitro translation experiments show that the enzyme is nuclear coded and synthesized as a precursor form. Immunogold electron microscopy has demonstrated that enoyl reductase is located in plastids. It is shown that ACP-Sepharose may be used as a matrix in the purification of enoyl-ACP reductase.
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PMID:Immunological detection of NADH-specific enoyl-ACP reductase from rape seed (Brassica napus)--induction, relationship of alpha and beta polypeptides, mRNA translation and interaction with ACP. 219 72

Lectin IV of Griffonia simplicifolia (Mr approximately 56,000), which has a strong affinity for both the Lewis b and Y blood-group determinants, is a dimeric protein of two subunits, alpha (29 kDa) and beta (27 kDa), separable by SDS/PAGE and containing covalently linked oligosaccharide. After digestion with N-glycanase, the protein migrates as a single band with a mobility identical with that of the beta-subunit. After cleavage with hydroxylamine of 3H-labelled, but otherwise intact, lectin, the radioactively labelled oligosaccharide was found to be associated with two blocked N-terminal peptides separable by h.p.l.c. and having identical amino acid compositions. One of these had three or four glucosamine residues per molecule, whereas the other had only one or two. Sequence analyses of these, as well as of a 21 kDa hydroxylamine-cleaved fragment and of the intact lectin pretreated with pyroglutamate aminopeptidase, have provided a unique sequence for residues 1-62 of the two subunits. Evidence is presented for two sites of N-linked oligosaccharide attachment at Asn-5 and Asn-18. Whereas the alpha-subunit has oligosaccharide linked to both sites, the beta-subunit has carbohydrate associated with only one (Asn-18). Sugar analyses of the whole lectin reveal a monosaccharide composition of (Xyl)3(Fuc)2(Man)10(GlcNAc)6, representing 6.4% of the mass of the molecule. Taken together with the susceptibility of the Asn-5 linkage (but not of Asn-18) to N-glycanase digestion, the observations indicate that the structures of the oligosaccharides at residues 5 and 18 are different.
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PMID:Molecular-mass heterogeneity of Griffonia simplicifolia lectin IV subunits. Differences in the oligosaccharide moieties in the N-terminal region. 226 64

Freeze-thaw (FT)-disrupted schistosomula or their membrane extract induced significant resistance in mice to Schistosoma mansoni infection (34 and 25%, respectively) without the use of adjuvant. Antigens identified in schistosome extracts by sera from immunized animals were then evaluated for protective potential. Immunization with schistosomal antigens of 97 and 68-70 kD resulted in significant protection that was equivalent to that obtained by FT schistosomula. Since the 97-kD antigen was suggested to be parasite paramyosin, we used a biochemical technique to purify this muscle protein. Purified schistosome paramyosin ran as a single band on 10% SDS-PAGE and was recognized both by sera from mice immunized with FT schistosomula and a polyclonal antiserum raised against the 97-kD parasite protein. Preincubation of schistosome paramyosin with sera from mice immunized with FT schistosomula resulted in the removal of reactivity with the 97-kD protein in crude worm extracts. Paramyosin was identified by Western blotting to be in the tegument of schistosomula. The purified schistosome paramyosin resulted in significant protection in three separate experiments (24, 46, and 53%) without the use of adjuvant. Addition of BCG to paramyosin resulted in enhanced protection.
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PMID:Induction of resistance to Schistosoma mansoni infection in mice by purified parasite paramyosin. 249 82

In Escherichia coli K-12, temperature-sensitive mutations in the secA gene have been shown to interfere with protein export. Here we show that the effect of a secA mutation is strongly pleiotropic on membrane biogenesis. Freeze-fracture experiments as well as cryosections of the cells revealed the appearance of intracytoplasmic membranes upon induction of the SecA phenotype. The permeability barrier of the outer membrane to detergents was lost. Two alterations in the outer membrane may be responsible for this effect, namely the reduced amounts of outer membrane proteins, or the reduction of the length of the core oligosaccharide of the lipopolysaccharide, which was observed in phage-sensitivity experiments and by SDS-polyacrylamide gel electrophoresis. Phospholipid analysis of the secA mutant, grown under restrictive conditions, revealed a lower content of the negatively charged phospholipid cardiolipin and of 18:1 fatty acid compared to those of the parental strain grown under identical conditions. These results are in line with the hypothesis that protein export and lipid metabolism are coupled.
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PMID:Membrane biogenesis in Escherichia coli: effects of a secA mutation. 267 87

Many homopteran insects feed on plant sap which contains solutes in very low concentration. Their digestive tract presents a complex called the "filter chamber" where the excess dietary water is believed to flow directly from the initial part of the midgut to the terminal part of the midgut and the proximal regions of the Malpighian tubules. Freeze-fracture experiments carried out on the filter chamber of Cicadella viridis revealed the presence of intramembrane particles on the whole surface of the microvilli and of basal membrane infoldings of the cells. Examination of negatively stained isolated membranes and of freeze-dried shadowed membranes revealed that the inner surface of the membrane is covered with particles protruding into the cytoplasm; they correspond to the numerous intramembrane particles observed on the P fracture face of the membrane. The outer surface of the membrane exhibits a regular network which corresponds to that observed on the E fracture face. SDS-PAGE analyses were performed on purified membranes of the filter chambers of C. viridis and Philaenus spumarius. In both cases 2 major components, 25 kDa and 75 kDa, were detected. These 2 components appear to be specific for the filter chambers since they were not found in membranes isolated from the other parts of the midgut. Thus, the membranes of these filter chambers, thought to be water-shunting complexes, possess structural and biochemical peculiarities which are probably related to water permeability.
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PMID:Structural and biochemical observations on specialized membranes of the "filter chamber", a water-shunting complex in sap-sucking homopteran insects. 280 56

The accessory layer of the cuticle of infective larvae of Trichinella spiralis has been studied with electron microscopy using cytochemical techniques and chemical extractions. The accessory layer lacks negative charges and carbohydrates demonstrable in vivo. Staining with ruthenium red and tannic acid is interpreted as being consistent with their reactions with phospholipids. Freeze fractures demonstrate an external layer of granules that can be partially released by means of detergents (CTAB and SDS). The granules are considered to be proteins. Their removal makes the worms acid sensitive and prevents them from infecting mice. Extraction of whole worms with ethanol, acetone and methanol (via reaction with 2,2-DMP), or chloroform and methanol destroys an internal layer of filaments. Thin-layer chromatography of chloroform/methanol extracts showed principally ethanolamine phospholipids from the surface of the worms. A model is presented for the molecular organization of the accessory layer. Ethanolamine phospholipids are suggested to occur as tubular micelles. Proteins may attach to these by lipophilic moieties and perhaps by a cryptic sugar group (demonstrated by others) that may penetrate into the hydrophilic core of the lipid micelles.
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PMID:Characterization of the accessory layer of the cuticle of muscle larvae of Trichinella spiralis. 337 25


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