Hordein variation in the genus Hordeum as recognized by monoclonal antibodies

Genome ◽  
1992 ◽  
Vol 35 (2) ◽  
pp. 200-207 ◽  
Author(s):  
Susanne Pelger ◽  
Roland Von Bothmer
Keyword(s):  
Monoclonal Antibodies ◽  
Gel Electrophoresis ◽  
Wild Barley ◽  
Antigenic Site ◽  
Barley Cultivar ◽  
Close Relationship ◽  
Major Storage Protein ◽  
Cultivated Barley ◽  
Similarities And Differences ◽  
Hordeum Species

The composition of the major storage protein, hordein, in wild barley species has been studied by using gel electrophoresis, Coomassie staining, and immunoblot assays. We have shown earlier that it is possible to obtain cross-reaction outside the cultivated barley, with monoclonal antibodies raised against hordeins from the barley cultivar Bomi. These antibodies have now been used to investigate the hordein composition in all species of the Hordeum genus. The results showed that polypeptides similar to the two major hordein groups of cultivated barley, the B- and C-hordeins, are produced in all wild Hordeum species, and that there are both similarities and differences between the two hordein groups. The similarities indicate a common evolutionary origin, while the distinction between B- and C-hordeins in the entire genus clearly shows that the divergence of their coding genes preceded the divergence of the Hordeum species. The presence of the same antigenic site in two different species indicates that they are evolutionarily related. Among the wild species, two rarely occurring sites were exclusively found in H. vulgare ssp. spontaneum and H. bulbosum, which confirms that they are the cultivated barley's closest relatives. Some of the antibodies also gave an extensive reaction pattern with H. murinum, which suggests a fairly close relationship to H vulgare, though not as close as between H. vulgare and H. bulbosum.Key words: Hordeum, hordein, monoclonal antibodies, evolution, multigene family.

scholarly journals Genotypic Difference in the Responses to Nitrogen Fertilizer Form in Tibetan Wild and Cultivated Barley

Plants ◽  
2021 ◽  
Vol 10 (3) ◽  
pp. 595
Author(s):  
Shama Naz ◽  
Qiufang Shen ◽  
Jonas Lwalaba Wa Lwalaba ◽  
Guoping Zhang
Keyword(s):  
Wild Barley ◽  
Growth Parameters ◽  
Inorganic Nitrogen ◽  
N Uptake ◽  
Total Soluble Protein ◽  
Organic N ◽  
Genotypic Difference ◽  
N Availability ◽  
Tibetan Wild Barley ◽  
Cultivated Barley

Nitrogen (N) availability and form have a dramatic effect on N uptake and assimilation in plants, affecting growth and development. In the previous studies, we found great differences in low-N tolerance between Tibetan wild barley accessions and cultivated barley varieties. We hypothesized that there are different responses to N forms between the two kinds of barleys. Accordingly, this study was carried out to determine the response of four barley genotypes (two wild, XZ16 and XZ179; and two cultivated, ZD9 andHua30) under 4Nforms (NO3−, NH4+, urea and glycine). The results showed significant reduction in growth parameters such as root/shoot length and biomass, as well as photosynthesis parameters and total soluble protein content under glycine treatment relative to other N treatments, for both wild and cultivated barley, however, XZ179 was least affected. Similarly, ammonium adversely affected growth parameters in both wild and cultivated barleys, with XZ179 being severely affected. On the other hand, both wild and cultivated genotypes showed higher biomass, net photosynthetic rate, chlorophyll and protein in NO3− treatment relative to other three N treatments. It may be concluded that barley undisputedly grows well under inorganic nitrogen (NO3−), however in response to the organic N wild barley prefer glycine more than cultivated barely.

scholarly journals Inhibition of acanthamoeba actomyosin-II ATPase activity and mechanochemical function by specific monoclonal antibodies.

1984 ◽  
Vol 99 (3) ◽  
pp. 1024-1033 ◽  
Author(s):  
D P Kiehart ◽  
T D Pollard
Keyword(s):  
Monoclonal Antibodies ◽  
Atpase Activity ◽  
Conformational Changes ◽  
Binding Sites ◽  
Polyclonal Antibodies ◽  
Myosin Ii ◽  
Antigenic Site ◽  
Actin Binding ◽  
Filamentous Form ◽  
Antibody Effects

Monoclonal and polyclonal antibodies that bind to myosin-II were tested for their ability to inhibit myosin ATPase activity, actomyosin ATPase activity, and contraction of cytoplasmic extracts. Numerous antibodies specifically inhibit the actin activated Mg++-ATPase activity of myosin-II in a dose-dependent fashion, but none blocked the ATPase activity of myosin alone. Control antibodies that do not bind to myosin-II and several specific antibodies that do bind have no effect on the actomyosin-II ATPase activity. In most cases, the saturation of a single antigenic site on the myosin-II heavy chain is sufficient for maximal inhibition of function. Numerous monoclonal antibodies also block the contraction of gelled extracts of Acanthamoeba cytoplasm. No polyclonal antibodies tested inhibited ATPase activity or gel contraction. As expected, most antibodies that block actin-activated ATPase activity also block gel contraction. Exceptions were three antibodies M2.2, -15, and -17, that appear to uncouple the ATPase activity from gel contraction: they block gel contraction without influencing ATPase activity. The mechanisms of inhibition of myosin function depends on the location of the antibody-binding sites. Those inhibitory antibodies that bind to the myosin-II heads presumably block actin binding or essential conformational changes in the myosin heads. A subset of the antibodies that bind to the proximal end of the myosin-II tail inhibit actomyosin-II ATPase activity and gel contraction. Although this part of the molecule is presumably some distance from the ATP and actin-binding sites, these antibody effects suggest that structural domains in this region are directly involved with or coupled to catalysis and energy transduction. A subset of the antibodies that bind to the tip of the myosin-II tail appear to inhibit ATPase activity and contraction through their inhibition of filament formation. They provide strong evidence for a substantial enhancement of the ATPase activity of myosin molecules in filamentous form and suggest that the myosin filaments may be required for cell motility.

Monoclonal antibodies against surface antigens of schistosomula of Schistosoma mansoni

Parasitology ◽  
1982 ◽  
Vol 84 (1) ◽  
pp. 65-82 ◽  
Author(s):  
D. W. Taylor ◽  
A. F. Butterworth
Keyword(s):  
Monoclonal Antibodies ◽  
Gel Electrophoresis ◽  
Primary Infection ◽  
Polyacrylamide Gel Electrophoresis ◽  
Apparent Molecular Weight ◽  
Surface Antigens ◽  
Soft Agar ◽  
Surface Proteins ◽  
Spleen Cells

SUMMARYMonoclonal antibodies have been produced after fusion of NS-1 murine myeloma cells with spleen cells from mice immunized either by chronic primary infection or with irradiated cercariae: in both cases, animals were challenged with live cercariae 7 days before fusion. The initial cultures were screened for anti-schistosomular antibodies both by a radioimmunoassay with whole schistosomulum extracts and by immunofluorescence. There was no correlation between the two techniques and subsequent screening was carried out by immunofluorescence. Cloning was carried out in soft agar and 7 cloned cell lines, from 5 initial cultures, were selected for detailed study. Products of 6 of these 7 lines were monoclonal, as judged by isoelectricfocusing of [35S]methionine-labelled supernatant fluids, and their binding to live schistosomula was specific. None of the antibodies showed detectable activity in mediating eosinophil- or complement-dependent damage to schistosomula in vitro. However, 2 antibodies were successfully used to isolate surface proteins with an apparent molecular weight of 24000 on SDS-polyacrylamide gel electrophoresis.

Reaction of Hordeum species to the smut fungi Ustilago nuda and U. tritici

1987 ◽  
Vol 65 (10) ◽  
pp. 2024-2027 ◽  
Author(s):  
J. Nielsen
Keyword(s):  
Hordeum Chilense ◽  
Smut Fungi ◽  
New Hosts ◽  
Cultivated Barley ◽  
Ustilago Nuda ◽  
Hordeum Species ◽  
Eleven Species

Eleven species of Hordeum were tested for their reaction to Ustilago nuda (Jens.) Rostr. and U. tritici (Pers.) Rostr., the causes of the embryo-infecting loose smuts of cultivated barley and wheat, respectively. The species Hordeum chilense and H. depressum were resistant, while H. euclaston, H. halophilum, H. procerum, H. pusillum, and H. stenostachys were susceptible to both fungi. Hordeum muticum was susceptible only to U. nuda, while H. arizonicum, H. lechleri, and H. roshevitzii were susceptible only to U. tritici. The susceptible species are new hosts for these pathogens. It is proposed that these results, together with those of an earlier study, indicate that U. nuda evolved from U. tritici.

scholarly journals Monoclonal antibodies prepared against Dictyostelium actin: characterization and interactions with actin.

1984 ◽  
Vol 99 (1) ◽  
pp. 287-295 ◽  
Author(s):  
P A Simpson ◽  
J A Spudich ◽  
P Parham
Keyword(s):  
Monoclonal Antibodies ◽  
Antigenic Site ◽  
Amino Acid Sequences ◽  
Cellular Slime Mold ◽  
Antigenic Sites ◽  
Critical Residue ◽  
Slime Mold Dictyostelium Discoideum ◽  
Cellular Slime ◽  
B Lymphoid ◽  
Alpha Actins

Three mouse monoclonal antibodies, Act I, Act II, and Act IV, against actin from the cellular slime mold Dictyostelium discoideum, have been made and characterized. All three antibodies are IgG1 and share the following properties: They form stable complexes with monomeric Dictyostelium actin, which prevents polymerization of the actin into filaments. On addition to preformed actin filaments, they cause a reduction in filament size and in the viscosity of the actin solution. They cross-react strongly with actins from the lower eucaryotes Physarum and Acanthamoeba, but not with alpha-actins from rabbit and human muscle or beta- and gamma-actins from human erythrocytes and a human B lymphoid cell line. Act II and Act IV recognize a similar antigenic determinant that is topographically distinct from that identified by Act I. In protein immunoblotting, only Act I bound strongly to Dictyostelium actin. Analysis of actin fragments with this technique showed that amino acids 13 to about 50 are required for Act I binding to actin. A comparison of the amino acid sequences of actins from lower eucaryotes and higher vertebrates implicates threonine 41 as a critical residue in the Act I antigenic site. The properties of Act II and Act IV suggest that they recognize antigenic sites involving the NH2-terminal six residues.

Giemsa C-banded karyotypes of Hordeum marinum and H. murinum

Genome ◽  
1989 ◽  
Vol 32 (4) ◽  
pp. 629-639 ◽  
Author(s):  
Ib Linde-Laursen ◽  
Roland von Bothmer ◽  
Niels Jacobsen
Keyword(s):  
Chromosome Morphology ◽  
Similar Distribution ◽  
Banding Patterns ◽  
Homologous Chromosomes ◽  
C Banding ◽  
Linear Relationships ◽  
Close Relationship ◽  
Different Populations ◽  
Pattern Polymorphism ◽  
Hordeum Species

Giemsa C-banding patterns of the predominantly self-pollinating, annual species Hordeum marinum (2x, 4x) and H. murinum (2x, 4x, 6x) showed mostly very small to small bands at centromeric and telomeric positions, at one or both sides of the nucleolar constrictions, and at intercalary positions with no preferential disposition. A similar distribution of bands has been observed in other Hordeum species, suggesting that the pattern is the basic one in the genus Hordeum. Hordeum murinum, especially the hexaploid cytotype, was distinguished from H. marinum by having more numerous and more conspicuous bands, resulting in a significantly higher percentage of constitutive heterochromatin (9–17 vs. 4–8%). The differences in C-banding patterns supported by differences in chromosome morphology confirm that H. marinum and H. murinum are not closely related. Banding-pattern polymorphism was prevalent among populations but unobserved within populations. In spite of this polymorphism, banding patterns in combination with chromosome morphology identified homologous chromosomes of different populations of a taxon and indicated that the chromosome complements of the polyploids of both species comprised the genome of the related diploid as well as one or two "unidentified" genomes. This agrees with an alloploid origin of polyploids. The C-banding patterns of H. marinum ssp. marinum and H. marinum ssp. gussoneanum (2x) showed some divergence in spite of the close relationship. The C-banded karyotypes of H. murinum ssp. murinum and H. murinum ssp. leporinum (4x) were very similar, supporting conspecificity. Chromosome lengths and longest/shortest chromosome ratios were fairly similar to those previously published, supporting the conclusion that linear relationships of chromosomes are normally stable within genomes. The taxonomy of the two species is discussed.Key words: C-banding, karyotypes, Hordeum.

STUDY OF IIA VON WILLEBRAND'S DISEASE (VWD) VARIANTS TO DETERMINE DEGREE AND TYPES OF HETEROGENEITY

1987 ◽  
Author(s):  
S M Enayat ◽  
F G H Hill ◽  
Y Sultan ◽  
C W Williams
Keyword(s):  
Monoclonal Antibodies ◽  
Factor Viii ◽  
Structure Function ◽  
Gel Electrophoresis ◽  
Agarose Gels ◽  
Factor Viii Related Antigen ◽  
The Third ◽  
Edta Plasma ◽  
Abnormal Pattern ◽  
The Common

Thirty four IIA vWD patients (16 from kindred I, 2 from kindred II and 17 unrelated patients) from 19 families were studied to compare multimer patterns using discontinuous SDS gel electrophoresis on a variety of agarose gels. Platelet multi-mers and effect of EDTA on plasma multimers were also studied in some.The large kindred and 9 other patients showed identical multimer and triplet abnormalities. The 11 other patients showed different multimer patterns either by having intermediate multimers or different triplet patterns. The second kindred had a similar triplet abnormality to kindred I but had intermediate multimers. Two other patients showed similar patterns except on 2% agarose gels when differences in the lowest multimer was seen. Of the 3 patients of YS, one showed the common IIA pattern but also had intermediate multimers, another had an unusually faint upper triplet band, while the third in addition to a faint upper triplet band with ESVWF 2+ had no identification of minor or major bands with ESVWF 10+ Another patient lacked high and some intermediate multimers but had a normal triplet pattern. The pattern we have seen in Kernoff's patient (1) still appears unique. In kindred II abnormal triplets persisted and high multimers appeared in EDTA plasma. In kindred I (and similar patients) intermediate multimers and a change in triplet pattern was observed in EDTA while lysed platelets showed an abnormal pattern different to the plasma one.This emphasizes the heterogeneity of IIA vWD and the need to consider multimer deletion, triplet pattern, platelet multimers, effect of EDTA in trying to subclassify in order to study structure function relationships of vWF.1. Kernoff PBA, Gruson R, Rizza CR. (1974) A variant of factor VIII related antigen. Br. J. Haematol. 26: 435.+ESVWF 2 and 10 are monoclonal antibodies to vWF epitopes.

scholarly journals Clonal variation within a mucosal isolate derived from a patient with Leishmania (Viannia) braziliensis infection

1991 ◽  
Vol 33 (5) ◽  
pp. 343-350 ◽  
Author(s):  
César Augusto Cuba-Cuba ◽  
David Evans ◽  
Ana de Cassia Rosa ◽  
Philip Davis Marsden
Keyword(s):  
Monoclonal Antibodies ◽  
Cellulose Acetate ◽  
Phenotypic Variation ◽  
Gel Electrophoresis ◽  
Clonal Variation ◽  
Starch Gel Electrophoresis ◽  
Mucosal Leishmaniasis ◽  
Starch Gel

Three isolates over 5 years from a patient with persistent relapsing mucosal leishmaniasis due to Leishmania (Viannia) braziliensis and 7 clones from one of these isolates were studied by zymodemes and scrodemes analysis. Results showed evidences of clonal phenotypic variation. Eight isoenzymes markers demonstrated clear differences on Cellulose Acetate (CA) and thin starch gel electrophoresis. Also a panel of specific monoclonal antibodies showed such differences. Our observations provide additional evidence that Leishmania (Viannia) braziliensis is composed by subpopulations of parasites with peculiar biochemical and antigenic characteristics.

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