Die Pulvillen vonCalliphora erythrocephala (Diptera,Brachycera) als Adhäsionsorgane

Zusammenfassung Die Pulvillen vonCalliphora erythrocephala wurden licht und fluoreszenzmikroskopisch, raster- und transmissions-elektronenmikroskopisch untersucht. Das Adhäsionssekret wurde dünnschichtchromatographisch mit dem Körperoberflächen-Lipid verglichen.Die Pulvillen tragen auf der Ventralseite mehrere Tausend langer dünner Hafthaare mit sohlenartigen Endverbreiterungen. Die Kutikula des Pulvillus besteht hauptsächlich aus elastischen Kutikulatypen (Endo- und Mesokutikula) in verschiedenen, spezifischen Ausbildungsformen.Die Pulvillen enthalten ein sekretorisches Epithel ohne Ausführgänge, das Protein- und Lipideinschlüsse zeigt.Das Pulvillensekret ist eine schwerflüchtige, ölige Flüssigkeit, die nicht identisch ist mit dem Körperoberflächen-Lipid. Das Sekret wird in der homogenen Kutikala des Pulvillus gespeichert und über das Porenkanalsystem der Ventralseite nach außen geleitet.Der Zusammenhang zwischen der Struktur der Pulvillen und ihrer Rolle beim Adhäsionsvorgang wird diskutiert.

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The pulvilli ofCalliphora erythrocephala (Diptera, Brachycera) as adhesive organs

Summary The pulvilli ofCalliphora erythrocephala were examined by light microscopy, fluorescent light microscopy, SEM and TEM. The adhesive secretion was compared with the general surface lipid layer by means of thinlayerchromatography.On the ventral surface the pulvilli bare several thousand long, slender tenent hairs with solelike spatulate tips. The pulvillar cuticle is composed on the whole of elastic cuticle types (endocuticle, mesocuticle) with specific modifications of structure. The pulvilli contain a secretory epithelium without transport ducts which has lipid and proteinaceous inclusions.The pulvillar secretion is a slowly volatile oily liquid which is not identical to the general surface lipid. The secretion is stored in the homogeneous cuticle within the pulvillus and transported to the ventral surface via the pore canal system.The correlation between the structure of pulvilli and their function in the adhesion process is discussed here.

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Abkürzungen bl Basales Labyrinth - cv coated vesicle - db dense body - dlk Dichter Lamellenkörper - dw Dorsalwand - e Epithel - ef Endokutikulafasern in der Übergangszone (meso 2b) - endo 1 lamelläre Endokutikula - endo 2 homogene Endokutikula - endo 3 gelatinöse Endokutikula - ep Empodium - epi Epikutikula - exo Exokutikula - fr Fersenregion - fs Faltensaum - hh Hafthaare - hs Haarschaft - k Kutikula - kr Kralle - ku Kutikulinschicht - l Lumen - li Lipid - lr Dorsale Längsrippen - m Mitochondrium - mb Mesokutikulabalken in der Übergangszone (meso 2b) - meso 1 helle homogene Mesokutikula - meso 2a dunkle homogene Mesokutikula, kompakt - meso 2b Übergangszone, in der dunkle homogene Mesokutikulabalken mit faseriger Endokutikula verzahnt sind - mt Mikrotubulus - mvbd Dunkler multivesikulärer Körper - n Kern - pc Porenkanal - ps Proximalsklerit - pt Prätarsus - rer Rauhes endoplasmatisches Retikulum - s Schulter - sd Sehnendrüse - se Sehne - so Sohle - sr Saumregion - t Tubulus - t₅ Tarsalglied 5 - ta Tasche - td Tarsaldrüse - te Tarsalepithel - tg Taschengrund - tk Terminalkanäle - utr Unguitractor - v Heller Vesikel - va Proteinvakuole - w Wachsschicht - z Zementschicht     

Additional evidence for separable responses to auxin in soybean hypocotyl

Additional evidence for two separable responses to auxin is presented. The average of 24 control experiments indicated lag times of 12.4 and 35.4 min, and maximum rates of 0.57 and 0.54 mm hr⁻¹, for the first and second response, respectively. The auxin analog 4-azido-2-chlorophenoxyacetic acid increased the lag time of the second response (but not the first), resulting in the temporal separation of the two responses. Plots of elongation rates against time, taken from the literature, allowed the characterization of the two responses in monocotyls and dicotyls. Study of published rate-time elongation curves showed that the maximum rate of the first response is frequently greater than the maximum rate of the second response; however, the maximum rate of the second response has not yet been shown to exceed the maximum rate of the first response.     

Two elongation responses to auxin respond differently to protein synthesis inhibition

The first and second responses to auxin react differently to the inhibition of protein synthesis by cycloheximide. It was determined that the protein with the shortest half-life, among the several necessary for the first response, is different from its counterpart among the several necessary for the second response. Specifically, the protein half-lives are 28 minutes and 11 minutes for the first and second responses, respectively.     

Intracellular appearance of nitrite and nitrate in nitrogen-starved cells of Ankistrodesmus braunii

Summary The occurrence of heterotrophic nitrification in nitrogen-starved cells of Ankistrodesmus braunii was confirmed. The levels of nitrate and nitrite were measured over a period of four weeks. The validity of quantitative determinations in the presence of highly active nitrate and nitrite reductases is discussed. Whereas free hydroxylamine as an intermediate could not be detected, increased hydroxylamine oxidase activity was found in nitrogen-starved cultures. Nitrite reductase and hydroxylamine oxidase can be assigned to particles by sucrose density gradient centrifugation. The possible involvement of microbodies, which were found to be present in Ankistrodesmus, in metabolic processes during nitrogen starvation is discussed.Abbreviations NR nitrate reductase - NiR nitrite reductase - NNEDA N-(1-naphthyl)ethylenediaminedihydrochloride - DCPIP 2,6-dichlorophenolindophenol - EDTA ethylenediaminetetraacetic acid - TCA trichloroacetic acid - DAB 3,3-diaminobenzidine - AT 3-amino-1H-1,2,4-triazole - AMP 2-amino-2-methyl-1,3-propanediol     

Clearance of lysosomal hydrolases following intravenous infusion. Kinetic and competition experiments with beta-glucuronidase and N-acetyl-beta-D-glucosaminidase.

Clearance experiments with highly purified lysosomal glycosidases, β-glucuronidase and N-acetyl-β-d-glucosaminidase, following intravenous infusion revealed widely varying clearance profiles which depended on the tissue source of the enzyme. Normal rat serum β-glucuronidase and epididymal N-acetyl-β-d-glucosaminidase were cleared slowly from the circulation when compared with rat preputial gland β-glucuronidase, liver lysosomal β-glucuronidase, and liver lysosomal N-acetyl-β-d-glucosaminidase, respectively, which were cleared rapidly. Experiments comparing the catalytic properties and molecular dimensions of the enzymes revealed no differences between rapid and slow clearance forms. Kinetic analysis using the rapid clearance forms of β-glucuronidase has allowed the resolution of at least two components, rapid and slow. Clearance of the rapid component is saturable and appears to reflect binding or uptake by a limited number of sites. By contrast, the clearance rate of the slow component increased linearly with respect to dose and may be due to nonspecific or low-affinity binding. Competition experiments with β-glucuronidase-free lysosomal extract and highly purified lysosomal enzymes, but not serum glycoproteins or colloidal silver, suggest that one lysosomal enzyme inhibits clearance of others and that a common mechanism may be involved in their binding.     

Clearance of lysosomal hydrolases following intravenous infusion. The role of liver in the clearance of beta-glucuronidase and N-acetyl-beta-D-glucosaminidase.

Certain highly purified forms of rat lysosomal glycosidases, β-glucuronidase and N-acetyl-β-d-glucosaminidase, are rapidly cleared from the circulation following intravenous infusion. Several lines of evidence are presented which indicate that the primary site of enzyme uptake is the liver. Clearance of the two enzymes was unaffected by nephrectomy, whereas it was abolished by evisceration. Tissue distribution experiments with native and [¹²⁵I]β-glucuronidase indicate the liver as the major, if not exclusive, site of enzyme uptake. Experiments with the isolated perfused liver showed clearance of certain enzyme preparations but not others. Those enzymes cleared by the isolated perfused liver were likewise cleared in vivo. Liver fractionation studies following infusion of large doses of β-glucuronidase revealed a rapid, short-lived increase in microsomal β-glucuronidase and a slower but larger increase in lysosomal β-glucuronidase. The results indicate that β-glucuronidase, N-acetyl-β-d-glucosaminidase, and probably other glycosidases are rapidly incorporated into the lysosomal compartment of liver.     

Interaction of a new fluorescent reagent with sulfhydryl groups of the (Na+ + K+)-stimulate ATPase.

The (Na+ + K+)-ATPase enzyme of rat brain microsomes can be reversibly inhibited by a new fluorescent sulfhydryl (SH) probe, dimethylaminoaphthalenecysteine-Hg+ (Dn-cys-Hg+). This reagent is more reactive than N-ethylamaleimide (MalNEt) toward membrane sulfhydryl groups. A procedure using the two SH reagents sequentially seems to permit a more selective labelling of the SH groups involved in the (Na+ + K+)-ATPase than is possible by using MalNEt alone. Brain microsomes treated by this method incorporate the fluorescent label within or near the active site of the enzyme. When the probe was bound a blue shift of its fluorescence emission maximum (from 540 to 495 nm) and a 20-fold increase in relative fluorescence occurred. This indicates that the Dn moiety is within a very non-polar region of the membrane.