scholarly journals Multiple proteins related to the soluble galactose-binding animal lectin revealed by a monoclonal anti-lectin antibody

1985 ◽  
Vol 228 (1) ◽  
pp. 147-153 ◽  
Author(s):  
S R Carding ◽  
R A Childs ◽  
R Thorpe ◽  
M Spitz ◽  
T Feizi
Keyword(s):  
Solid Phase ◽  
Cell Types ◽  
Binding Activity ◽  
Active Components ◽  
Muscle Tissues ◽  
Bovine Tissue ◽  
Tissue Homogenates ◽  
Binding Lectin ◽  
Animal Lectin ◽  
Galactose Binding Lectin

A monoclonal antibody (NIBy 142-36/8) raised against the soluble galactose-binding lectin of bovine heart muscle has been tested by solid-phase vinyl-plate radiobinding and nitrocellulose immunoblotting with homogenates of various bovine tissues, and the muscle tissues of pig, rabbit, chicken and rat. Muscle lectins of chicken, rabbit and rat differed from those of man and pig in their lack of reactivity with the 36/8 antibody. There was a good correlation of haemagglutinating activities and immunoreactivities of the bovine tissue homogenates, suggesting that the soluble galactose-binding protein is a major haemagglutinin in various tissues. Immunoblotting experiments revealed an array of antigenically active components in the homogenates in addition to the 13 and 26kDa proteins that were previously detected in preparations of purified lectin. These were in the range 36kDa to more than 200kDa, and a different spectrum of immunoreactive components was found in various cell types. Galactose-binding activity was demonstrable in 13, 26 and 36kDa components in certain bovine tissues, suggesting that the immunoreactive components of higher Mr may be inactive precursor forms of the lectin.

scholarly journals Production and characterization of monoclonal antibodies to β-galactoside-binding lectin of bovine heart muscle. Direct evidence that haemagglutinating activity is associated with a 13kDa protein

1984 ◽  
Vol 220 (1) ◽  
pp. 253-260 ◽  
Author(s):  
S R Carding ◽  
R Thorpe ◽  
R A Childs ◽  
M Spitz ◽  
T Feizi
Keyword(s):  
Heart Muscle ◽  
Direct Evidence ◽  
Solid Phase ◽  
Binding Activity ◽  
High Titre ◽  
Immunoglobulin M ◽  
Bovine Heart ◽  
Haemagglutinating Activity ◽  
Binding Lectin

With the aim of obtaining monospecific antibodies against the beta-galactoside-binding lectin of bovine heart muscle, spleen cells from Lou rats immunized with lectin were fused with the rat myeloma line Y3.Ag1.2.3. Two immunoglobulin M (IgM)-producing clones, designated NIBy 142-36/8 and NIBy 143-9/5, derived from separate fusions, were used to generate ascites containing high-titre binding activity against the 13kDa component in preparations of lectin. Direct evidence that haemagglutinating activity is associated with the 13kDa protein was obtained by the specific elution of 13kDa polypeptides with haemagglutinating activity from an immobilized antibody adsorbent. Solid-phase radiobinding assays and immunoblotting of isolated lectins and/or muscle homogenates confirmed the earlier indications with conventional antisera that the beta-galactoside-binding lectins of bovine, human and monkey muscle tissue are antigenically related.

scholarly journals Active Components from Cassia abbreviata Prevent HIV-1 Entry by Distinct Mechanisms of Action

2021 ◽  
Vol 22 (9) ◽  
pp. 5052
Author(s):  
Yue Zheng ◽  
Xian-Wen Yang ◽  
Dominique Schols ◽  
Mattia Mori ◽  
Bruno Botta ◽  
...  
Keyword(s):  
Crude Extract ◽  
Female Genital Tract ◽  
Binding Activity ◽  
Sub Saharan Africa ◽  
Active Components ◽  
Chemical Structures ◽  
3D Space ◽  
In Silico Study ◽  
Sub Saharan ◽  
Hiv 1

Cassia abbreviata is widely used in Sub-Saharan Africa for treating many diseases, including HIV-1 infection. We have recently described the chemical structures of 28 compounds isolated from an alcoholic crude extract of barks and roots ofC. abbreviata, and showed that six bioactive compounds inhibit HIV-1 infection. In the present study, we demonstrate that the six compounds block HIV-1 entry into cells: oleanolic acid, palmitic acid, taxifolin, piceatannol, guibourtinidol-(4α®8)-epiafzelechin, and a novel compound named as cassiabrevone. We report, for the first time, that guibourtinidol-(4α®8)-epiafzelechin and cassiabrevone inhibit HIV-1 entry (IC50 of 42.47 µM and 30.96 µM, respectively), as well as that piceatannol interacts with cellular membranes. Piceatannol inhibits HIV-1 infection in a dual-chamber assay mimicking the female genital tract, as well as HSV infection, emphasizing its potential as a microbicide. Structure-activity relationships (SAR) showed that pharmacophoric groups of piceatannol are strictly required to inhibit HIV-1 entry. By a ligand-based in silico study, we speculated that piceatannol and norartocarpetin may have a very similar mechanism of action and efficacy because of the highly comparable pharmacophoric and 3D space, while guibourtinidol-(4α®8)-epiafzelechin and cassiabrevone may display a different mechanism. We finally show that cassiabrevone plays a major role of the crude extract of CA by blocking the binding activity of HIV-1 gp120 and CD4.

Expression of an endogenous galactose-binding lectin correlates with neoplastic progression in the colon

Cancer ◽  
1995 ◽  
Vol 75 (12) ◽  
pp. 2818-2826 ◽  
Author(s):  
Harald L Schoeppner ◽  
Avraham Raz ◽  
Samuel B. Ho ◽  
Robert S. Bresalier
Keyword(s):  
Neoplastic Progression ◽  
Binding Lectin ◽  
Galactose Binding Lectin

scholarly journals Gastric Hyperplasia and Increased Proliferative Responses of Lymphocytes in Mice Lacking the COOH-terminal Ankyrin Domain of NF-κB2

1997 ◽  
Vol 186 (7) ◽  
pp. 999-1014 ◽  
Author(s):  
Hideaki Ishikawa ◽  
Daniel Carrasco ◽  
Estefania Claudio ◽  
Rolf-Peter Ryseck ◽  
Rodrigo Bravo
Keyword(s):  
T Cells ◽  
Lymphocyte Proliferation ◽  
Cytokine Production ◽  
Cell Types ◽  
Homozygous Deletion ◽  
Binding Activity ◽  
Activated T Cells ◽  
Physiological Relevance

The nfkb2 gene encodes the p100 precursor which produces the p52 protein after proteolytic cleavage of its COOH-terminal domain. Although the p52 product can act as an alternative subunit of NF-κB, the p100 precursor is believed to function as an inhibitor of Rel/NF-κB activity by cytoplasmic retention of Rel/NF-κB complexes, like other members of the IκB family. However, the physiological relevance of the p100 precursor as an IκB molecule has not been understood. To assess the role of the precursor in vivo, we generated, by gene targeting, mice lacking p100 but still containing a functional p52 protein. Mice with a homozygous deletion of the COOH-terminal ankyrin repeats of NF-κB2 (p100−/−) had marked gastric hyperplasia, resulting in early postnatal death. p100−/− animals also presented histopathological alterations of hematopoietic tissues, enlarged lymph nodes, increased lymphocyte proliferation in response to several stimuli, and enhanced cytokine production in activated T cells. Dramatic induction of nuclear κB–binding activity composed of p52-containing complexes was found in all tissues examined and also in stimulated lymphocytes. Thus, the p100 precursor is essential for the proper regulation of p52-containing Rel/NF-κB complexes in various cell types and its absence cannot be efficiently compensated for by other IκB proteins.

Cytotoxicity and Glycan-Binding Profile of a d-Galactose-Binding Lectin from the Eggs of a Japanese Sea Hare (Aplysia kurodai)

2011 ◽  
Vol 30 (7) ◽  
pp. 509-519 ◽  
Author(s):  
Sarkar M. A. Kawsar ◽  
Ryo Matsumoto ◽  
Yuki Fujii ◽  
Haruki Matsuoka ◽  
Naoko Masuda ◽  
...  
Keyword(s):  
Binding Profile ◽  
Sea Hare ◽  
Binding Lectin ◽  
Galactose Binding Lectin

Comparative analysis of the transferrin and lactoferrin binding proteins in the family Neisseriaceae

1989 ◽  
Vol 35 (3) ◽  
pp. 409-415 ◽  
Author(s):  
Anthony B. Schryvers ◽  
B. Craig Lee
Keyword(s):  
Binding Proteins ◽  
Solid Phase ◽  
Bacterial Species ◽  
Binding Activity ◽  
Intact Cells ◽  
Human Transferrin ◽  
Affinity Isolation ◽  
Lactoferrin Receptor ◽  
Solid Phase Binding ◽  
Branhamella Catarrhalis

Intact cells of several bacterial species were tested for their ability to bind human transferrin and lactoferrin by a solid-phase binding assay using horseradish peroxidase conjugated transferrin and lactoferrin. The ability to bind lactoferrin was detected in all isolates of Neisseria and Branhamella catarrhalis but not in isolates of Escherichia coli or Pseudomonas aeruginosa. Transferrin-binding activity was similarly detected in most isolates of Neisseria and Branhamella but not in E. coli or P. aeruginosa. The expression of transferrin- and lactoferrin-binding activity was induced by addition of ethylenediamine di-o-phenylacetic acid and reversed by excess FeCl3, indicating regulation by the level of available iron in the medium. The transferrin receptor was specific for human transferrin and the lactoferrin receptor had a high degree of specificity for human lactoferrin in all species tested. The transferrin- and lactoferrin-binding proteins were identified after affinity isolation using biotinylated human transferrin or lactoferrin and streptavidin–agarose. The lactoferrin-binding protein was identified as a 105-kilodalton protein in all species tested. Affinity isolation with biotinylated transferrin yielded two or more proteins in all species tested. A high molecular mass protein was observed in all isolates, and was of similar size (approximately 98 kilodaltons) in all species of Neisseria but was larger (105 kilodaltons) in B. catarrhalis.Key words: iron, Neisseria, transferrin, lactoferrin, receptor.

scholarly journals Antibacterial Effects of Leaf Extract of Nandina domestica and the Underlined Mechanism

2018 ◽  
Vol 2018 ◽  
pp. 1-9 ◽  
Author(s):  
Zhao-Yu Guo ◽  
Zhuo-Yang Zhang ◽  
Jia-Qi Xiao ◽  
Jin-Hong Qin ◽  
Wei Zhao
Keyword(s):  
Chronic Bronchitis ◽  
Leaf Extract ◽  
Solid Phase ◽  
Safety Issue ◽  
Dilution Method ◽  
Agar Dilution Method ◽  
Mice Model ◽  
Active Components ◽  
Bacterial Morphology ◽  
Guinea Pig Model

Aim. The study was conducted to investigate the antibacterial and antiasthmatic effects of Nandina domestica leaf extract, to find out its active components, and to assess its safety issue. Methods. (1) Solid-phase agar dilution method was used for antibacterial activity test of nandina leaf extract and the change of bacterial morphology after treatment was observed under the transmission microscope; (2) guinea pig model of asthma was used to test the asthma prevention effect of nandina leaf extract; (3) alkaloids and flavones were separated from nandina leaf extract and were further analyzed with HPLC-MS; (4) mice model was used to assessment of the safety issue of nandina leaf extract. Results. (1) Nandina leaf extract inhibited the growth of bacteria and destroyed bacterial membrane; (2) nandina leaf extract alleviated animal allergy and asthma; (3) the components reextracted by ethyl acetate were active, in which alkaloids inhibited Gram-positive bacteria and prevented asthma and flavones inhibited Gram-negative bacteria; (4) nandina leaf extract had no toxic effect on mice. Conclusion. Nandina leaves inhibit bacterial growth and prevent asthma through alkaloids and flavones, which had integrated function against chronic bronchitis. This study provided theoretical basement for producing new Chinese medicine against chronic bronchitis.

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