scholarly journals Identification of the Wheat Curl Mite as the Vector of the High Plains Virus of Corn and Wheat

Plant Disease ◽  
1997 ◽  
Vol 81 (10) ◽  
pp. 1161-1166 ◽  
Author(s):  
Dallas L. Seifers ◽  
Tom L. Harvey ◽  
T. J. Martin ◽  
Stanley G. Jensen
Keyword(s):  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Triticum Aestivum L ◽  
Enzyme Linked Immunosorbent Assay ◽  
High Plains ◽  
Serological Relationship ◽  
Hordeum Vulgare L ◽  
Wheat Curl Mite ◽  
Aceria Tosichella

Wheat with virus-like symptoms (extracts containing a 33-kDa protein in sodium dodecyl sulfate-polyacrylamide gel electrophoresis, negative in enzyme-linked immunosorbent assay to wheat streak mosaic virus, and not infectious in a backassay to other wheat) reacted positively to antiserum made against a protein purified from symptomatic corn infected with the High Plains virus (HPV), indicating a serological relationship between the corn and wheat pathogens. The wheat curl mite (WCM, Aceria tosichella Keifer) was identified as the vector of the virus and caused persistent infection of barley (Hordeum vulgare L.) and wheat (Triticum aestivum L.) in greenhouse experiments. The HPV was recovered in the field from naturally infected wheat where the number of HPV-infected plants decreased with increasing distance from the WCM source in volunteer wheat.

scholarly journals Differential Transmission of Isolates of the High Plains virus by Different Sources of Wheat Curl Mites

Plant Disease ◽  
2002 ◽  
Vol 86 (2) ◽  
pp. 138-142 ◽  
Author(s):  
Dallas L. Seifers ◽  
Tom L. Harvey ◽  
Raymond Louie ◽  
D. T. Gordon ◽  
T. J. Martin
Keyword(s):  
Sodium Dodecyl Sulfate ◽  
South Dakota ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
High Plains ◽  
Aceria Tosichella ◽  
Molecular Masses ◽  
Differential Transmission ◽  
Different Sources

High Plains virus (HPV) isolates from Colorado, Idaho, Kansas, Texas, and Utah were serologically related, had similar relative molecular masses (sodium dodecyl sulfate-polyacrylamide gel electrophoresis) for the 32-kDa diagnostic HPV protein, and were transmissible and maintained free of Wheat streak mosaic virus (WSMV) by vascular puncture inoculation. Collections of wheat curl mites (Aceria tosichella Keifer; WCM) from Kansas, Montana, Nebraska, South Dakota, and Texas differentially transmitted these isolates. For collections from South Dakota and Texas, little or no HPV transmission occurred, whereas WCM from Nebraska and Montana transmitted all five isolates. The collection from Kansas mostly transmitted only one HPV isolate. Aviruliferous or viruliferous WSMV Nebraska WCM transmitted HPV at similar rates and aviruliferous Montana WCM transmitted HPV at lower levels than viruliferous Montana WCM.

scholarly journals Antibody produced against isolated Rh(D) polypeptide reacts with other Rh-related antigens

Blood ◽  
1988 ◽  
Vol 72 (5) ◽  
pp. 1622-1626
Author(s):  
K Suyama ◽  
J Goldstein
Keyword(s):  
Gel Electrophoresis ◽  
High Titer ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Enzyme Linked Immunosorbent Assay ◽  
Rabbit Antibody ◽  
Immune Precipitation ◽  
D Cells ◽  
D Antigen ◽  
Related Proteins

Rh(D) antigen-containing polypeptide was prepared by immune precipitation of intact cDE/cDE erythrocytes by using a high-titer preparation of polyclonal anti-D. when isolated Rh(D) polypeptide was administered to rabbits, antibody was produced that was unresponsive toward Rh-positive and -negative cells but reacted strongly with the immunogen in enzyme-linked immunosorbent assay-type immunobinding and Western blot immunostaining assays. Rabbit antibody also immunostains isolated Rh(c) polypeptide as well as the Rh antigen-containing components of sodium dodecyl sulfate-polyacrylamide gel electrophoresis- separated membrane proteins from Rh(D)-positive (cDE/cDE,CDe/CDe), Rh(D)-negative (cde/cde,Cde/Cde), and -D-/-D- cells. It does not react with any membrane protein from Rh-null regulator type cells, thus indicating a specificity for Rh-related proteins. We have also been able to demonstrate that polyclonal and monoclonal anti-D preparations that do not immunostain isolated Rh(D) polypeptide will react with it in our immunobinding assay.

Using Cell-Based Activity Assays In Support Of Carryover Calculations In Multi-Product Facilities

2021 ◽  
Vol 27 (4) ◽  
Author(s):  
Gabriella del Hierro ◽  
Emily Holz ◽  
Ed Contreras ◽  
Pauline Che ◽  
Shelley Elvington ◽  
...  
Keyword(s):  
Sodium Dodecyl Sulfate ◽  
Immunosorbent Assay ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Analytical Techniques ◽  
Polyacrylamide Gel ◽  
Enzyme Linked Immunosorbent Assay ◽  
Specific Cell ◽  
Therapeutic Antibodies

The calculation of cleaning carryover limits in multi-product facilities can be based on the inactivity of molecules after exposure to cleaning conditions if the inactivation of active molecules can be demonstrated. The demonstration of inactivation has been addressed in several publications that have shown degradation and/or denaturation using different analytical techniques such as sodium dodecyl sulfate-polyacrylamide gel electrophoresis and enzyme-linked immunosorbent assay, which directly or indirectly demonstrate that the product residue is no longer active. In this paper, authors expand the assay options by demonstrating the use of molecule-specific cell-based activity assays, which provide a “catch all” measurement of sample bioactivity, to assess the inactivation of therapeutic antibodies after exposure to cleaning conditions.

PAP, a pancreatic secretory protein induced during acute pancreatitis, is expressed in rat intestine

1993 ◽  
Vol 265 (4) ◽  
pp. G611-G618 ◽  
Author(s):  
J. L. Iovanna ◽  
V. Keim ◽  
A. Bosshard ◽  
B. Orelle ◽  
J. M. Frigerio ◽  
...  
Keyword(s):  
Acute Pancreatitis ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Secretory Protein ◽  
Enzyme Linked Immunosorbent Assay ◽  
Rat Intestine ◽  
Mrna Concentration ◽  
Initial Content ◽  
Pancreatitis Associated Protein

The pancreatitis-associated protein (PAP) is a lectin-related secretory protein present in small amounts in the rat pancreas and rapidly overexpressed during the acute phase of pancreatitis. We demonstrate in this report that PAP is also expressed in rat intestine. A cDNA library from rat jejunum was probed with pancreatic PAP cDNA. The inserts of the selected recombinant clones corresponded to a transcript whose nucleotide sequence was identical to that of pancreatic PAP mRNA. The transcript was detected in duodenum, jejunum, ileum, and colon. A protein with same molecular mass (16 kDa) and pI (8.2) as pancreatic PAP was actually immunodetected in ileum homogenate after separation by two-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Intestinal PAP was immunolocalized to the epithelial cells of the lower part of the villi. The protein accounted respectively for 0.02, 0.05, and 0.1% of soluble proteins in duodenum, jejunum, and ileum homogenates, as measured by enzyme-linked immunosorbent assay, and could not be detected in stomach and colon. Influence of fasting and feeding on PAP mRNA concentration was analyzed in ileum. Concentration decreased by 81 and 94% after animals were fasted for 24 and 48 h, respectively. Feeding restored the initial content within 6 h. On the other hand, intestinal PAP mRNA concentration was not altered during acute pancreatitis

Diversity of seed storage proteins in common wheat (Triticum aestivum L.)

2011 ◽  
Vol 9 (2) ◽  
pp. 256-259
Author(s):  
Zuzana Šramková ◽  
Edita Gregová ◽  
Svetlana Šliková ◽  
Ernest Šturdík
Keyword(s):  
Triticum Aestivum ◽  
Common Wheat ◽  
Gel Electrophoresis ◽  
Storage Proteins ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Triticum Aestivum L ◽  
Polyacrylamide Gel

The objective of our study was to determine the composition of high-molecular weight-glutenin subunits (HMW-GS) in 120 cultivars of common wheat (Triticum aestivum L.). Fourteen alleles and 34 allelic compositions were detected using sodium dodecyl sulphate-polyacrylamide gel electrophoresis. The most frequent HMW-GS alleles at the Glu-A1, Glu-B1 and Glu-D1 loci were null (57.1%), 7+9 (43.3%) and 5+10 (61.9%), respectively. However, low-frequency HMW-GS alleles were also observed, such as 13+16, 20, 21, 7 and 18, encoded by the Glu-B1 locus, and 4+12, encoded by the Glu-D1 locus. The wheat–rye 1BL.1RS translocation was identified in 25 cultivars, using acid polyacrylamide gel electrophoresis. The Glu-score varied greatly, and some lines reached the maximum value of 10.

INFLUENCE OF SOURCE OF WHEAT CYTOPLASM ON THE NATURE OF PROTEINS IN HEXAPLOID TRITICALE

1974 ◽  
Vol 16 (3) ◽  
pp. 529-537 ◽  
Author(s):  
S. L. K. Hsam ◽  
E. N. Larter
Keyword(s):  
Molecular Weight ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Seed Proteins ◽  
Triticum Aestivum L ◽  
The Other ◽  
Hexaploid Triticale ◽  
Electrophoretic Patterns ◽  
High Molecular Weight Proteins

Sodium dodecyl sulfate-polyacrylamide gel electrophoresis was used to study seed proteins in 4 pairs of reciprocal F1 isogenic hybrids of hexaploid triticales differing only in their source of cytoplasm. One member of each reciprocal pair possessed the cytoplasm of hexaploid (6x) wheat (Triticum aestivum L. em. Thell), the other, the cytoplasm from tetraploid (4x) wheat (T. turgidum L). Qualitative as well as quantitative differences were observed in the electrophoretic patterns of the albumins and globulins. High molecular weight proteins (> 34,000 daltons) were synthesized in triticale with 6x wheat cytoplasm in greater quantity than in triticale with 4x wheat cytoplasm. Differences in the patterns of gliadin and reduced glutenin of the reciprocal triticale populations were quantitative. The relevance of these findings to seed development in triticales is discussed.

scholarly journals Humoral Immune Responses to S-Layer-Like Proteins of Bacteroides forsythus

2003 ◽  
Vol 10 (3) ◽  
pp. 383-387 ◽  
Author(s):  
Masahiro Yoneda ◽  
Takao Hirofuji ◽  
Noriko Motooka ◽  
Koji Nozoe ◽  
Kayoko Shigenaga ◽  
...  
Keyword(s):  
Immune Responses ◽  
Gel Electrophoresis ◽  
Early Onset ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Enzyme Linked Immunosorbent Assay ◽  
Humoral Immune ◽  
Humoral Immune Responses ◽  
Healthy Control ◽  
Specific Antigens

ABSTRACT Bacteroides forsythus is one of the important periodontopathic bacteria, and this microorganism is known to have an S-layer outside the outer membrane. The S-layer-like antigens were recently isolated from B. forsythus, and they were found to be 270- and 230-kDa proteins in the envelope fraction. In this study, these proteins were confirmed to be specific to B. forsythus by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and they were clearly recognized by sera from patients with adult and early-onset periodontitis in Western immmunoblot analysis. We compared the immunoglobulin G (IgG) responses against the purified S-layer-like antigen by enzyme-linked immunosorbent assay. IgG responses against this antigen were low in healthy control subjects, but they were significantly higher in subjects with adult and early-onset periodontitis. Together with the fact that the IgG responses against the crude extract of B. forsythus did not rise significantly in patients with periodontitis, S-layer-like proteins are considered to be specific antigens of B. forsythus and may play an important role in the progression of periodontitis.

scholarly journals Plasma Proteolytic Cascade Activation during Neonatal Cardiopulmonary Bypass Surgery

2018 ◽  
Vol 118 (09) ◽  
pp. 1545-1555 ◽  
Author(s):  
Susan Maroney ◽  
Julie Peterson ◽  
Wes Zwifelhofer ◽  
Nicholas Martinez ◽  
Ke Yan ◽  
...  
Keyword(s):  
Cardiopulmonary Bypass ◽  
Protease Inhibitors ◽  
Gel Electrophoresis ◽  
Surgical Procedure ◽  
Heart Defects ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Enzyme Linked Immunosorbent Assay ◽  
Heparin Administration ◽  
Operative Recovery

Background Neonates undergoing cardiopulmonary bypass (CPB) surgery to correct congenital heart defects often experience excessive bleeding. Exposure of blood to artificial materials during CPB may activate coagulation, complement and inflammatory pathways. In addition, the surgical stress placed on the haemostatic system may result in cross-activation of other plasma proteolytic cascades, which could further complicate physiological responses to the surgical procedure and post-operative recovery. Plasma protease inhibitors undergo distinct conformational changes upon interaction with proteases, and, thereby, can serve as endogenous biosensors to identify activation of the different proteolytic cascades. We tested the hypothesis that changes in the concentration and conformation of protease inhibitors regulating plasma proteolytic cascades during neonatal CPB are associated with post-operative bleeding. Patients and Methods Plasma samples from 44 neonates were obtained at four time points across the surgical procedure. Anti-thrombin, antitrypsin, anti-chymotrypsin, anti-plasmin, C1-inhibitor and tissue factor pathway inhibitor (TFPI) concentrations and conformations were evaluated by enzyme-linked immunosorbent assay, transverse urea gradient gel electrophoresis and sodium dodecyl sulphate-polyacrylamide gel electrophoresis. Results/Conclusion The most striking changes were observed following heparin administration and were associated with the appearance of inactive forms of anti-thrombin and an increase in the plasma concentration of TFPI. Changes in anti-thrombin and TFPI remained evident throughout surgery and into the post-operative period but were not different between patients with or without post-operative bleeding. The concentration of antitrypsin decreased across surgery, but there was no significant accumulation of inactive conformations of any inhibitor besides anti-thrombin, indicating that widespread cross-activation of other plasma proteolytic cascades by coagulation proteases did not occur.

Effects of Gamma Radiation on the Allergenic and Antigenic Properties of Milk Proteins

2001 ◽  
Vol 64 (2) ◽  
pp. 272-276 ◽  
Author(s):  
JU-WOON LEE ◽  
JAE-HUN KIM ◽  
HONG-SUN YOOK ◽  
KUN-OK KANG ◽  
SOO-YOUNG LEE ◽  
...  
Keyword(s):  
Gel Electrophoresis ◽  
Immunoglobulin E ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Milk Proteins ◽  
Food Irradiation ◽  
Enzyme Linked Immunosorbent Assay ◽  
Antigenic Properties ◽  
Β Lactoglobulin ◽  
Irradiation Technology

This study was carried out to evaluate the application of food irradiation technology as a method for reducing milk allergies. Bovine α-casein (ACA) and β-lactoglobulin (BLG) were used as milk proteins. Using milk-hypersensitive patients' immunoglobulin E (IgE) and rabbit IgGs individually produced to ACA and BLG, the changes of allergenicity and antigenicity of irradiated proteins were observed by competitive indirect enzyme-linked immunosorbent assay. Allergenicity and antigenicity of the irradiated proteins were changed with different slopes of the inhibition curves. The disappearance of the band on sodium dodecyl sulfate-polyacrylamide gel electrophoresis and increase of the turbidity showed that solubility of the proteins decreased by radiation, and this decrease might be caused by agglomeration of the proteins. These results indicated that epitopes on milk allergens were structurally altered by gamma irradiation.

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