Antibody to spermine: a natural biological constituent

Science ◽  
1980 ◽  
Vol 208 (4448) ◽  
pp. 1178-1181 ◽  
Author(s):  
D Bartos ◽  
F Bartos ◽  
RA Campbell ◽  
DP Grettie ◽  
P Smejtek
Keyword(s):  
Affinity Chromatography ◽  
Gel Electrophoresis ◽  
Binding Constants ◽  
Cross Reactivity ◽  
Polyamine Metabolism ◽  
Regulatory Function ◽  
Rabbit Serum ◽  
Normal Rabbit Serum ◽  
Immunodiffusion Test ◽  
Gradient Gel Electrophoresis

A protein that binds spermine specifically was separated from normal rabbit serum by affinity chromatography. Immunoelectrophoresis, the Ouchterlony immunodiffusion test, and gradient gel electrophoresis indicated that this protein has immunoglobulin characteristics and consists of several populations of antibodies to spermine. These were sequentially released from Sepharose-spermine gel by step-wise elution with solutions ranging in pH from 4 to 1. The binding constants varied from 5.0 x 10(8) to 11.1 x 10(8) liters per mole. These globulins did not react with monoacetylputrescine, L-ornithine, L-lysine, and histamine. Negligible cross-reactivity was detected with spermidine, putrescine, N8-monoacetylspermidine, cadaverine, and diaminopropane. Since perturbations in polyamine metabolism have been identified in several diseases, the study of extracellular polyamine homeostasis may reveal an important regulatory function for this protein.

scholarly journals Purification and partial characterization of human polyamine synthases

1989 ◽  
Vol 259 (3) ◽  
pp. 879-886 ◽  
Author(s):  
E O Kajander ◽  
L I Kauppinen ◽  
R L Pajula ◽  
K Karkola ◽  
T O Eloranta
Keyword(s):  
Gel Electrophoresis ◽  
Cross Reactivity ◽  
Specific Pattern ◽  
Native Enzyme ◽  
Spermidine Synthase ◽  
Enzyme Preparations ◽  
Spermine Synthase ◽  
Apparent Homogeneity ◽  
Gradient Gel Electrophoresis ◽  
Pore Gradient

Spermidine synthase was purified to apparent homogeneity from human spleens (8700-fold) by affinity chromatography. The native enzyme was composed of two subunits of identical Mr (35,000) and showed an apparent Mr of 62,000 in pore-gradient gel electrophoresis. Its pI was 5.1, Spermine synthase was purified to apparent homogeneity from placenta (5300-fold) and from kidney (4600-fold). The native enzyme was composed of two subunits of identical Mr (45,000) and showed an apparent Mr of 78,000 in pore-gradient gel electrophoresis. In isoelectric focusing it revealed two bands, with pI values of 4.9 and 5.0. Both synthases were present in all human tissues studied, but revealed a clear tissue-specific pattern. Mouse antisera against spermidine synthase revealed only one band, of Mr 35,000, in all purified enzyme preparations and in crude human tissue extracts in immunoblotting. Antisera against spermine synthase showed an immunoreactive band corresponding to the Mr of the subunit of spermine synthase. These antisera did not indicate any cross-reactivity in immunoblotting. Thus spermine synthase and spermidine synthase do not share homologous antigenic sites and are totally different proteins.

Artificially transformed schistosomula of Schistosoma mansoni: mechanism of acquisition of protection against antibody-mediated killing

Parasitology ◽  
1980 ◽  
Vol 80 (1) ◽  
pp. 95-104 ◽  
Author(s):  
C. A. P. Tavares ◽  
M. N. Cordeiro ◽  
T. A. Mota-Santos ◽  
G. Gazzinelli
Keyword(s):  
Amino Acid ◽  
Schistosoma Mansoni ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Rabbit Serum ◽  
Normal Rabbit Serum ◽  
Serum Factors ◽  
Quantitative Fluorescence

SummaryIncorporation of labelled amino acid into tegumental proteins and acquisition of protection by schistosomula against antibody-mediated killing in vitro were simultaneously stimulated by serum factors and inhibited by puromycin. Comparison of polyacrylamide gel electrophoresis patterns with fluorographic autoradiography indicates that the majority of proteins in the parasite tegument were labelled with the isotope after incubation for 3 h. No new, clearly defined band was observed in the autoradiography pattern. During this period a decreasing susceptibility of the schistosomula to antibody plus complement was observed. Quantitative fluorescence assay shows that schistosomula insensitive to antibody plus complement were still able to bind the same amount of antibody as the unprotected parasites. Pre-culture of schistosomula in the presence of inactivated normal rabbit serum also decreased the susceptibility of the parasites to the in vivo killing mechanism.

Identification of Maize Rayado Fino Virus by Immunoelectron Microscopy

1985 ◽  
Vol 43 ◽  
pp. 636-637
Author(s):  
O. E. Bradfute
Keyword(s):  
Electron Microscopy ◽  
Zea Mays ◽  
Costa Rica ◽  
Severe Disease ◽  
Rabbit Serum ◽  
Normal Rabbit Serum ◽  
Virus Particles ◽  
Far North ◽  
Maize Rayado Fino Virus ◽  
Antibody Coating

Maize rayado fino virus (MRFV) causes a severe disease of corn (Zea mays) in many locations throughout the neotropics and as far north as southern U.S. MRFV particles detected by direct electron microscopy of negatively stained sap from infected leaves are not necessarily distinguishable from many other small isometric viruses infecting plants (Fig. 1).Immunosorbent trapping of virus particles on antibody-coated grids and the antibody coating or decoration of trapped virus particles, was used to confirm the identification of MRFV. Antiserum to MRFV was supplied by R. Gamez (Centro de Investigacion en Biologia Celular y Molecular, Universidad de Costa Rica, Ciudad Universitaria, Costa Rica).Virus particles, appearing as a continuous lawn, were trapped on grids coated with MRFV antiserum (Fig. 2-4). In contrast, virus particles were infrequently found on grids not exposed to antiserum or grids coated with normal rabbit serum (similar to Fig. 1). In Fig. 3, the appearance of the virus particles (isometric morphology, 30 nm diameter, stain penetration of some particles, and morphological subunits in other particles) is characteristic of negatively stained MRFV particles. Decoration or coating of these particles with MRFV antiserum confirms their identification as MRFV (Fig. 4).

Localization of oxytocin and neurophysin in baboon (Papio anubis) corpus luteum by immunocytochemistry

1986 ◽  
Vol 113 (4) ◽  
pp. 570-575 ◽  
Author(s):  
Firyal S. Khan-Dawood
Keyword(s):  
Corpus Luteum ◽  
Rabbit Serum ◽  
Corpora Lutea ◽  
Positive Staining ◽  
Normal Rabbit Serum ◽  
Fallopian Tubes ◽  
Papio Anubis ◽  
Luteal Cells ◽  
Luteal Tissue ◽  
Immunocytochemical Reaction

Abstract. Immunoreactive oxytocin is detectable in the corpora lutea of women and cynomolgus monkeys by radioimmunoassay. To localize the presence of oxytocin and neurophysin I in ovarian tissues of subhuman primates, three corpora lutea and ovarian stromal tissues and two Fallopian tubes obtained during the menstrual cycle of the baboon and decidua from two pregnant baboons were examined using highly specific antisera against either oxytocin or neurophysin I and preoxidase-antiperoxidase light microscopy immunohistochemistry. Oxytocin-like as well as neurophysin I-like immunoreactivities were found in some cells of all the corpora lutea only, but could not be demonstrated in ovarian stromal tissues, Fallopian tubes and decidua. Specificity of the immunocytochemical reaction was further confirmed by immunoabsorption of the antiserum with excess oxytocin or neurophysin, after which the immunoreactivities for both oxytocin and neurophysin in the luteal tissue were negative. Similar controls using normal rabbit serum gave no positive staining for either oxytocin or neurophysin. Counterstaining of the positive immunoreactivities for oxytocin and neurophysin I with Mayer's haematoxylin and eosin demonstrated clearly that the oxytocin and neurophysin I appeared as granular material mainly within the cytoplasm of the luteal cells. The localization of immunoreactive oxytocin and neurophysin I in the corpus luteum of the baboon demonstrates directly the presence of these two neurohypophysial peptides within primate luteal cells and suggests their local production.

Allelopathic and Medicinal plant. 26. Millettia speciosa

2020 ◽  
Vol 51 (2) ◽  
pp. 125-146
Author(s):  
Nasiruddin Nasiruddin ◽  
Yu Zhangxin ◽  
Ting Zhao Chen Guangying ◽  
Minghui Ji
Keyword(s):  
Community Structure ◽  
Medicinal Plant ◽  
Gel Electrophoresis ◽  
Denaturing Gradient Gel Electrophoresis ◽  
Wiener Index ◽  
Pseudomonas Spp ◽  
Evenness Index ◽  
Gradient Gel Electrophoresis ◽  
Rhizosphere Pseudomonas

We grew cucumber in pots in greenhouse for 9-successive cropping cycles and analyzed the rhizosphere Pseudomonas spp. community structure and abundance by PCR-denaturing gradient gel electrophoresis and quantitative PCR. Results showed that continuous monocropping changed the cucumber rhizosphere Pseudomonas spp. community. The number of DGGE bands, Shannon-Wiener index and Evenness index decreased during the 3rd cropping and thereafter, increased up to the 7th cropping, however, however, afterwards they decreased again. The abundance of Pseudomonas spp. increased up to the 5th successive cropping and then decreased gradually. These findings indicated that the structure and abundance of Pseudomonas spp. community changed with long-term cucumber monocropping, which might be linked to soil sickness caused by its continuous monocropping.

scholarly journals Application of temperature gradient gel electrophoresis to the characterization of a nitrifying bioaugmentation product

2003 ◽  
Vol 43 (2) ◽  
pp. 277-286 ◽  
Author(s):  
Melissa A. Fouratt ◽  
Jeremy S. Rhodes ◽  
Charles M. Smithers ◽  
Nancy G. Love ◽  
Ann M. Stevens
Keyword(s):  
Temperature Gradient ◽  
Gel Electrophoresis ◽  
Gradient Gel Electrophoresis ◽  
Temperature Gradient Gel Electrophoresis

scholarly journals Factors influencing Lp[a]- particle size as determined by gradient gel electrophoresis.

1996 ◽  
Vol 37 (8) ◽  
pp. 1655-1663
Author(s):  
D O'Neal ◽  
G Grieve ◽  
D Rae ◽  
G Dragicevic ◽  
J D Best
Keyword(s):  
Particle Size ◽  
Gel Electrophoresis ◽  
Factors Influencing ◽  
Gradient Gel Electrophoresis
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