scholarly journals The clinical cross-reactivity and immunological cross-antigenicity of wheat and barley

2021 ◽  
Author(s):  
Shohei Kubota ◽  
Yuji Aoki ◽  
Tomomi Sskai ◽  
Katsumasa Kitamura ◽  
Teruaki Matsui ◽  
...  
Keyword(s):  
Oral Immunotherapy ◽  
Cross Reactivity ◽  
The Other ◽  
Enzyme Linked Immunosorbent Assay ◽  
Wheat Allergy ◽  
Extract Concentration ◽  
Low Concentrations ◽  
High Concentrations ◽  
Food Challenges ◽  
Elisa Inhibition

Background: Some patients with a wheat allergy have been reported to show clinical cross-reactivity to barley. However, it is not clear whether the development of barley allergy in patients with a wheat allergy is due to cross-antigenicity between wheat and barley. In our study, we aimed to determine the clinical cross-reactivity and immunological cross-antigenicity of wheat and barley. Methods: We compared the results of barley oral food challenges (OFCs) before oral immunotherapy (OIT) for wheat with those after OIT in nine patients with a wheat allergy to estimate the clinical cross-reactivity of wheat and barley. Moreover, we performed enzyme-linked immunosorbent assay (ELISA) inhibition and immunoblotting inhibition using serum from seven patients allergic to wheat and barley. Results: Nine patients who had positive barley-OFC results performed before OIT for wheat were all negative on barley-OFC performed after OIT. In ELISA inhibition, preincubation of serum from patients allergic to wheat and barley with a high barley extract concentration inhibited binding of IgE to wheat extract by less than 10%. On the other hand, wheat and barley extracts equally inhibited binding to barley sIgE at high concentrations. In the immunoblotting inhibition test, the spots of wheat were inhibited but weakly by barley extracts, and most of the spots of barley were inhibited even by low concentrations of the wheat and barley extract. Conclusion: We showed that barley allergy associated with wheat allergy is caused by cross-reactivity from wheat. The OIT for wheat was one of the promising options for barley allergy.

scholarly journals Allergenic Characterization of Tropomyosin from the Dusky Brown Cockroach, Periplaneta fuliginosa

2004 ◽  
Vol 11 (4) ◽  
pp. 680-685 ◽  
Author(s):  
Kyoung Yong Jeong ◽  
Heeyu Hwang ◽  
Jongweon Lee ◽  
In-Yong Lee ◽  
Dong Soo Kim ◽  
...  
Keyword(s):  
Recombinant Protein ◽  
Periplaneta Americana ◽  
Immunoglobulin E ◽  
Expression System ◽  
Specific Ige ◽  
Cross Reactivity ◽  
Enzyme Linked Immunosorbent Assay ◽  
Inhibitor Concentration ◽  
The Cross ◽  
Elisa Inhibition

ABSTRACTHousehold arthropods are one of the most common causes of allergic diseases. Four species of cockroaches are found to reside in Korean homes, but published work deals almost exclusively with the German and American cockroaches. This study was undertaken to investigate the cross-reactive allergenic components of the dusky brown cockroach,Periplaneta fuliginosa. Enzyme-linked immunosorbent assay (ELISA) inhibition and immunoblot analyses for the dusky brown cockroach were performed withBlattella germanicaandDermatophagoides farinaeallergic sera. cDNA encoding tropomyosin, which is a well known cross-reactive pan-allergen, was cloned by reverse transcriptase PCR, and recombinant protein was produced by using a pET-28b expression system. Native tropomyosin was purified by ammonium sulfate fractionation and electroelution. The immunoglobulin E (IgE) reactivities of native and recombinant tropomyosins were compared by an ELISA inhibition study. All 30 sera tested showedP. fuliginosa-specific IgE, and the IgE-binding reactivity of theP. fuliginosaextract was inhibited as much as 79.4% by aB. germanicaextract and as much as 63.3% by aD. farinaeextract. The deduced amino acid sequence of cloned cDNA was identical with that ofPeriplaneta americanatropomyosin (98.5% nucleotide sequence identity). Seven of 26 (26.9%) allergic sera had IgE specific for recombinant protein, and the maximum inhibition ofP. fuliginosa-specific IgE achieved with recombinant tropomyosin was 37.7% at an inhibitor concentration of 10 μg/ml. Native tropomyosin inhibited the binding of IgE to theP. fuliginosa,B. germanica, andD. farinaeextracts by 65.0, 51.8, and 39% at an inhibitor concentration of 1 μg/ml.P. fuliginosaappears to possess allergens that are highly cross-reactive with allergens ofB. germanicaandD. farinae. Tropomyosin was found to be a major allergenic component accounting for the cross-reactivity between cockroaches and dust mites.

The influence of type and timing of protein supplementation on wool growth and protein synthesis in the skin of young Merino sheep

1999 ◽  
Vol 50 (4) ◽  
pp. 497 ◽  
Author(s):  
D. G. Masters ◽  
G. Mata ◽  
S. M. Liu
Keyword(s):  
Protein Synthesis ◽  
Experimental Period ◽  
Protein Supplementation ◽  
The Other ◽  
Canola Meal ◽  
Protein Supplements ◽  
Wool Growth ◽  
Low Concentrations ◽  
High Concentrations ◽  
Dietary Treatments

There is limited evidence that the response in wool growth resulting from feeding protected protein supplements continues after the feeding has stopped. Feeding such proteins, alternated with traditional supplements, may increase wool growth as much as continuous feeding but at a lower cost. This experiment aimed to determine whether the response to protected protein continued after the sheep were switched to a cereal supplement. Over a 2-month experimental period, 56 weaners (5 months old, weighing 26 kg) were used in a 2 × 2 factorial experiment. Half were fed a diet containing 25% canola meal [partially protected protein with high concentrations of sulfur amino acids (SAA)] mixed with oaten hay, urea, and minerals. The other half were fed the same diet but with lupin seed (highly degradable protein with low concentrations of SAA) replacing the canola meal. Within each of the 2 dietary treatments and in each of 2 months, half of the weaners were fed the diet continuously, the other half were fed the diet for 2 weeks followed by 2 weeks of a barley, oats, hay, urea, and minerals diet. Another group of 8 weaners was fed the oats–barley diet continuously for 2 months. All sheep were fed to lose 35 g liveweight/day. Weaners fed canola meal grew 11% more wool during the experiment and had a higher rate of protein synthesis in the skin than weaners fed lupins. The response to canola meal of wool and skin was the same whether feeding was continuous or alternated with oats–barley, indicating that the benefits from feeding partially protected proteins continues after feeding has stopped.

Effect of Disused Battery on Germination Characteristics of Wheat

2012 ◽  
Vol 610-613 ◽  
pp. 284-287
Author(s):  
Heng Zhang ◽  
Zhao Tang Xu ◽  
Yu Liang Han ◽  
Zhi Chen
Keyword(s):  
Protease Activity ◽  
Germination Rate ◽  
Germination Index ◽  
Extract Concentration ◽  
Low Concentrations ◽  
Vigor Index ◽  
Germination Characteristics ◽  
High Concentrations ◽  
Wheat Germination

The aim was to study the effect of disused battery on wheat germination. The germination characteristics such as germination rate, germinating, germination index, vigor index, and activity changes of amylase and protease were determinated by germination bed method. The results showed that the disused battery affected wheat germination. With the increase of extract concentration of disused battery, the vigor index based on germination rate at 72h dropped, which indicated that the decrement was more pronounced than germination index of that. The change trends of amylase and protease activity were not difference, which the activities were promoted in the range of low concentrations of extract, but it were inhibited in the range of high concentrations.

Antibodies against lepirudin are polyspecific and recognize epitopes on bivalirudin

Blood ◽  
2004 ◽  
Vol 103 (2) ◽  
pp. 613-616 ◽  
Author(s):  
Petra Eichler ◽  
Norbert Lubenow ◽  
Ulrike Strobel ◽  
Andreas Greinacher
Keyword(s):  
Cross Reactivity ◽  
Enzyme Linked Immunosorbent Assay ◽  
Antibody Testing ◽  
Recombinant Hirudin ◽  
Elisa System ◽  
Microtiter Plates ◽  
Clinical Consequences ◽  
High Concentrations ◽  
Clinically Significant ◽  
High Doses

Abstract Bivalirudin is a synthetic antithrombin sharing a sequence of 11 amino acids with the recombinant hirudin lepirudin. We investigated whether antilepirudin antibodies recognize epitopes on bivalirudin. Antilepirudin antibody–positive sera of 43 patients, treated with lepirudin for heparin-induced thrombocytopenia, were analyzed. Lepirudin- and bivalirudin-coated microtiter plates were used for antibody testing in an enzyme-linked immunosorbent assay (ELISA) system. Of the 43 sera-containing antibodies binding to lepirudin, 22 (51.2%) contained antibodies that also recognized bivalirudin. Binding of these antibodies to bivalirudin was inhibited by more than 70% by preincubation with high doses of bivalirudin. However, if lepirudin-coated microtiter plates were used, high concentrations of bivalirudin inhibited only 2 of the 43 positive sera by more than 30%. Therefore antihirudin antibodies must be polyspecific. The clinical consequences of this cross-reactivity are unknown but bivalirudin, targeted by antibodies of patients treated with lepirudin previously, could potentially boost antibody titers in such patients or even trigger an immune response by itself. Clinically significant antibody formation in response to bivalirudin monotherapy has not been observed, however. Yet, as lepirudin and antilepirudin antibodies have recently been implicated in severe anaphylactic reactions, caution is warranted when using bivalirudin in patients previously treated with lepirudin.

Fibrinolytic Activity of Thrombin Preparations

1964 ◽  
Vol 11 (01) ◽  
pp. 234-242 ◽  
Author(s):  
Pieter Brakman ◽  
Panpit Klug ◽  
Tage Astrup
Keyword(s):  
Protease Activity ◽  
Fibrinolytic Activity ◽  
The Other ◽  
Fibrinolytic Agents ◽  
Fibrinolytic Agent ◽  
Low Concentrations ◽  
Fibrin Plate ◽  
Simple Chemical ◽  
Per Se ◽  
High Concentrations

SummarySome thrombin samples have a slight unspecific protease activity probably caused by contaminating plasmin. All investigated samples were fibrinolytically active. This activity was caused by an activator of plasminogen. Fibrinolytic activity was apparently produced by two components of the thrombin preparations. One of these components was a contaminant with fibrinolytic activity but with no thrombin activity. This component could be separated from the thrombin by simple chemical procedures. The other fibrinolytic component appeared to be the thrombin molecule per se. It was not fibrinolytically active when used in the low concentrations required for clotting of fibrinogen, but in high concentrations, assayed on the fibrin plate, it activated plasminogen. In the accurate assay of fibrinolytic agents it is necessary to use preparations of thrombin from which the contaminating fibrinolytic agent has been removed.

Transport and exchange diffusion of l-tryptophan in Ehrlich cells

1961 ◽  
Vol 200 (5) ◽  
pp. 1063-1068 ◽  
Author(s):  
John A. Jacquez
Keyword(s):  
Amino Acid ◽  
Initial Velocity ◽  
The Other ◽  
Preliminary Loading ◽  
Exchange Diffusion ◽  
Diaminobutyric Acid ◽  
Low Concentrations ◽  
Ehrlich Ascites ◽  
Ehrlich Ascites Cells ◽  
High Concentrations

The initial velocity of uptake of l-tryptophan by Ehrlich ascites cells can be explained as the sum of two processes: diffusion and an active transport that shows a saturation effect. Azaserine, l-2,4 diaminobutyric acid, l-histidine, and l-leucine, at low concentrations, increase the initial velocity of uptake of l-tryptophan but compete with l-tryptophan at high concentrations. Preliminary loading of the cells with glycine decreases the initial tryptophan flux: preliminary loading of the ascites cells with azaserine or tryptophan markedly increases the initial flux of uptake of the other amino acid.

PATTERNS OF PLASMA PROLACTIN IN POST-PARTUM SUCKLED COWS

1981 ◽  
Vol 90 (3) ◽  
pp. 391-396 ◽  
Author(s):  
R. WEBB ◽  
G. E. LAMMING
Keyword(s):  
Post Partum ◽  
Significant Negative Correlation ◽  
Prolactin Secretion ◽  
The Other ◽  
Plasma Prolactin ◽  
Blood Samples ◽  
Biphasic Pattern ◽  
Stage Of Lactation ◽  
Low Concentrations ◽  
High Concentrations

Blood samples taken on alternate days through indwelling jugular venous catheters from 12 suckled cows between days 14 and 48 post partum contained significantly less prolactin than samples collected on intermediate days by jugular venepuncture. Samples taken through the catheter every 2 h for 72 h periods revealed a repetitive daily biphasic pattern of prolactin secretion with low concentrations at 09.00 and 19.00 h and high concentrations at 13.00 and 23.00 h. In two groups of cows, one group calving at the beginning of March (increasing photoperiod) and the other calving during June (decreasing photoperiod), there was a significant negative correlation between stage of lactation and plasma prolactin concentrations in samples taken by venepuncture.

Existence of two types of postjunctional α-adrenoceptors in the isolated canine internal carotid artery

1988 ◽  
Vol 66 (5) ◽  
pp. 655-659 ◽  
Author(s):  
Yasuaki Kawai ◽  
Shigeaki Kobayashi ◽  
Toshio Ohhashi
Keyword(s):  
Response Curve ◽  
Carotid Arteries ◽  
Internal Carotid ◽  
The Other ◽  
Low Concentrations ◽  
Selective Agonists ◽  
High Concentrations ◽  
The Right ◽  
Internal Carotid Arteries ◽  
Concentration Response Curve

The pharmacological characteristics of postjunctional α-adrenoceptors in isolated canine internal carotid arteries were investigated by the use of selective agonists and antagonists for α1 and α2-adrenoceptors. Norepinephrine, phenylephrine, and xylazine caused concentration-dependent contractions in the helical strips. The contraction induced by 10−4 M xylazine was significantly smaller than that produced by 10−4 M norepinephrine or 10−4 M phenylephrine. The contraction induced by 10−4 M phenylephrine was almost the same value as that induced by 10−4 M norepinephrine. Phentolamine (10−8 and 10−7 M) caused a parallel shift to the right of the concentration–response curve to norepinephrine. The contractile responses to low concentrations of norepinephrine were significantly suppressed by pretreatment with an α2-antagonist such as yohimbine (10−9 and 10−8 M) or DG 5128(10−7 and 10−6 M). On the other hand, the responses to higher concentrations of norepinephrine were mainly reduced by low concentrations of an α1-antagonist, prazosin (3 × 10−10 and 3 × 10−9 M). These results suggest that both α1- and α2-adrenoceptors are located on the plasma membrane of smooth muscle cells in canine internal carotid arteries and that the norepinephrine-induced contractions at low and high concentrations are mainly mediated by activation of α2- and α1-adrenoceptors, respectively.

scholarly journals Effects of calmodulin antagonists on antibody binding to calmodulin. Distinct conformers of calmodulin induced by the binding of drugs

1992 ◽  
Vol 284 (3) ◽  
pp. 803-808 ◽  
Author(s):  
F Orosz ◽  
K Liliom ◽  
N A Barkhudaryan ◽  
L Horváth ◽  
J Ovádi
Keyword(s):  
Tertiary Structure ◽  
Antibody Binding ◽  
Enzyme Linked Immunosorbent Assay ◽  
Calmodulin Antagonists ◽  
Long Distance ◽  
Equilibrium Conditions ◽  
Terminal Fragment ◽  
Low Concentrations ◽  
High Concentrations ◽  
Stimulate Antibody

An indirect enzyme-linked immunosorbent assay has been used to study the interactions between calmodulin and two calmodulin antagonists, trifluoperazine and a neuropeptide isolated from the hypothalamus. The binding of a monospecific anti-calmodulin antibody, raised in rabbit against dinitrophenylated calmodulin, to calmodulin was tested at various concentrations of these drugs under equilibrium conditions. Trifluoperazine at low concentrations stimulated, but at relatively high concentrations inhibited, immunocomplex formation. The neuropeptide displaced the antibody from calmodulin at nanomolar concentrations. Enzyme-linked immunosorbent assays were also carried out with the large tryptic fragments of calmodulin. The results suggest that (i) the C-terminal fragment binds the antibody with an affinity which is comparable with that of intact calmodulin; (ii) the neuropeptide can form complexes with both N- and C-terminal fragments, but with two orders of magnitude less activity in case of the C-terminal fragment; and (iii) trifluorperazine does not stimulate antibody binding to the C-terminal fragment. Therefore the tertiary structure of calmodulin must be intact to ensure long-distance interactions between the binding sites of trifluoperazine, the neuropeptide and the antibody. These interactions may produce distinct conformers of calmodulin which may exhibit altered potency, not only for antibody binding but also for stimulation/inhibition of target enzymes.

ION PAIRS IN A SOLONETZIC SOIL

1983 ◽  
Vol 63 (3) ◽  
pp. 479-484 ◽  
Author(s):  
A. ALZUBAIDI ◽  
G. R. WEBSTER
Keyword(s):  
Ion Pairs ◽  
Soil Samples ◽  
The Other ◽  
Sulfate Ion ◽  
Carbonate Ion ◽  
Low Concentrations ◽  
Solonetzic Soil ◽  
Ap Horizon ◽  
Ion Activities ◽  
High Concentrations

The kinds and concentrations of the major ion pairs were determined in saturation extracts of 141 soil samples collected from a Solonetzic soil treated with various kinds of tillage combined with surface-applied chemical amendments. The correlations between concentrations of ion pairs and EC and pH of saturation extracts were statistically tested. Sulfate ion pairs NaSO4−, MgSO40 and CaSO40 occurred in relatively high concentrations. The other ion pairs were of low concentrations. Of the total soluble Ca, ion pairs ranged from 20.8% in the Ap horizon to 50.5% in the Csk horizon and Mg was approximately the same. The comparable values for Na were 0.8% and 4.6%, respectively. Ion pairs NaSO4−, KSO4−, MgSO40 and CaSO40 were significantly correlated with EC. Only carbonate ion pairs were significantly correlated with pH. Correcting concentrations of Na, Ca and Mg for ion pairs and activities changed considerably the SAR values in the Bnt1 horizon. Key words: Ion pairs, Solonetzic soils, ion activities

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