Under normal growth conditions wheat shows 100% non-host resistance to the barley powdery mildew Erysiphe graminis f. sp. hordei (Egh.). Primary inoculation of 7-day-old wheat seedlings with this fungus induced partial (60-70%) local resistance to challenge inoculation 12 hours later with the compatible pathogen Erysiphe graminis f. sp. tritici (Egt). mRNA was isolated from induced resistant first leaves (13 hours after primary inoculation) and a cDNA library was established in lambda ZAP. Differential screening of the library with sDNA probes (from induced resistant versus non-inoculated plants) resulted in isolation of 6 cDNA clones corresponding to 6 different induced, plant-encoded mRNA species. Hybridization of in vitro transcripts derived from wheat nuclei to cDNA dot blots showed that the transcription of these genes was induced rapidly, 3 hours after inoculation with either Egt or Egh. At this time point neither fungus had formed appressorial germ tubes yet. When induced resistant first leaves were challenged with the compatible pathogen (Egt), transcription of the host genes was enhanced a second time. No difference in kinetics of induction of transcription could be observed between noninduced and induced resistant leaves. One of the cloned induced mRNAs codes for a peroxidase, as shown by cDNA derived partial peptide sequence analysis. Peroxidase activity increased in intercellular washing fluids of first leaves from 6 to 36 hours after inoculation.
The effects of tetanus duration on the relaxation rate of extensor digitorum longus (EDL) and flexor digitorum brevis (FDB) muscles were studied in normal (wild‐type, WT) and parvalbumin‐deficient (PVKO) mice, at 20 °C.
In EDL of PVKO, the relaxation rate was low and unaffected by tetanus duration (< 3.2 s). In contrast, the relaxation rate of WT muscles decreased when tetanus duration increased from 0.2 to 3.2 s. In WT muscles, fast relaxation recovered as the rest interval increased.
Specific effect of parvalbumin was asserted by calculating the difference in relaxation rate between WT and PVKO muscles. For EDL, the rate constant of relaxation slowing was 1.10 s−1 of tetanization; the rate constant of relaxation recovery was 0.05 s−1 of rest.
In FDB, the effects of tetanus duration on WT and PVKO muscles were qualitatively similar to those observed in EDL.
Relaxation slowing as tetanus duration increases, reflects the progressive saturation of parvalbumin by Ca2+, while recovery as rest interval increases reflects the return to Ca2+‐free parvalbumin.
At all tetanus durations, relaxation rate still remained slightly faster in WT muscles. This suggested that parvalbumin facilitates calcium traffic from myofibrils to the SR.
No difference was found between WT and PVKO muscles for: (i) the expression of the fast isoforms of myosin heavy chains, (ii) the force‐velocity relationship and maximal shortening velocity and (iii) the Ca2+‐activated ATPase activity from isolated preparations of the sarcoplasmic reticulum (SR).
Antibodies to synthetic human calcitonin (hCT) were developed in rabbits, goats and mice. The free peptide (32 amino-acid residues, Mwt. 3418) was administered together with adjuvant, and the effect of various immunization procedures, as well as of different dose-levels, was evaluated comparatively. Synthetic hCT was found to be a good immunogen for the three animal species examined. The relative importance of various structural parts of the hCT molecule with regard to immunological specificity was determined by reference to the inhibition of the specific binding of 125I-hCT to antibodies by peptide fragments of hCT.All the antisera studied were directed to structural and/or conformational properties of the 11\p=n-\28 or 11\p=n-\32amino acid sequence of hCT. Six different antisera from rabbits and goats were selected for radioimmunological assay of hCT on the basis of their inhibitory dose50-values and immunological specificity. To improve the sensitivity of the radioimmunoassay (RIA), we studied the preparation of radioiodinated hCT and assessed various parameters determining the sensitivity of the assay. Despite all the efforts, CT in human plasma from healthy subjects could not be determined with certainty. The difficulties encountered in the
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