Evolution des activités protéolytiques digestives chez les Jeunes Mulgilidae

Proteolytic activity in the stomach, pyloric caeca and intestine decreases with increasing size in the three fish species Mugil auratus, M. capito and M. saliens. Differences between these species are found mainly in the gastric proteolytic activity which appears to be related to diet. This activity is pronounced in M. saliens whose diet is mainly carnivorous. Comparison of regression lines relating gastric proteolytic activity to size reveals differences which distinguish M. auratus from both of the other species. Total proteolytic activity exhibits high variability depending on the types of diet.     

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     

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     

Bromine oxidation of methyl α- and β-pyranosides of D-galactose,D-glucose,and D-mannose

Methyl α- and β-pyranosides of D-galactose, D-glucose, and D-mannose have been oxidized with bromine in aqueous solution at various pH values. The resulting keto glycosides were converted into their more-stable O-methyloxime derivatives which were characterized by spectroscopy and chromatography. Oxidation at a ring carbon atom where the hydrogen is axial is hindered by bulky substituents in syn (i.e., a 1,3) diaxial relationship. Thus, the aglycon group in the α anomers protects position 3, the axial HO-4 in galactopyranosides protects position 2, and the axial HO-2 in mannopyranosides protects position 4 from oxidation.     

Further evidence for a phycobilisome model from selective dissociation,fluorescence emission,immunoprecipitation, and electron microscopy

Phycobilisomes, isolated in 500 mM Sorensen's phosphate buffer pH 6.8 from the red alga, Porphyridium cruentum, were analyzed by selective dissociation at various phosphate concentrations. The results are consistent with a structural model consisting of an allophycocyanin core, surrounded by a hemispherical layer of R-phycocyanin, with phycoerythrin being on the periphery. Such a structure also allows maximum energy transfer.Intact phycobilisomes transfer excitation energy ultimately to a pigment with a fluorescence emission maximum at 675 nm. This pigment is presumed to be allophycocyanin in an aggregated state. Uncoupling of energy transfer among the pigments, and physical release of the phycobiliproteins from the phycobilisome follow a parallel time-course; phycoerythrin is released first, followed by R-phycocyanin, and then allophycocyanin. In 55 mM phosphate buffer, the times at which 50% of each phycobiliprotein has dissociated are: phycoerythrin 40 min, R-phycocyanin 75 min, and allophycocyanin 140 min.The proposed arrangement of phycobiliproteins within phycobilisomes is also consistent with the results from precipitation reactions with monospecific antisera on intact and dissociated phycobilisomes. Anti-phycoerythrin reacts almost immediately with intact phycobilisomes, but reactivity with anti-R-phycocyanin and anti-allophycocyanin is considerably delayed, suggesting that the antigens are not accessible until a loosening of the phycobilisome structure occurs. Reaction with anti-allophycocyanin is very slow in P. cruentum phycobilisomes, but is much more rapid in phycobilisomes of Nostoc sp. which contains 6–8 times more allophycocyanin. It is proposed that allophycocyanin is partially exposed on the base of isolated intact phycobilisomes of both algae, but that in P. cruentum there are too few accessible sites to permit a rapid formation of a precipitate with anti-allophyocyanin.Phycobilisome dissociation is inversely proportional to phosphate concentration (500 mM to 2 mM), and is essentially unaffected by protein concentration in the range used (30–200 μg/ml). Phycobiliprotein release occurs in the same order (phycoerythrin > R-phycocyanin > allophycocyanin) in the pH range 5.4–8.0.     

Differentiation in cultures derived from embryonic chicken muscle: I. Muscle-specific enzyme changes before fusion in EGTA-synchronized cultures

It is known that myoblast fusion fails to occur in cultures containing EGTA (a calcium-specific chelator) but occurs very rapidly after EGTA medium is replaced with standard high-calcium medium. On the basis of a careful analysis of the time course of fusion in cultures switched from EGTA to standard medium, it is proposed that this method of synchronization be used routinely in studies of the timing of different processes during in vitro myogenesis. The kinetics of accumulation of total enzyme activity for creatine kinase and fructose diphosphate aldolase indicate that the increases characteristic of terminal muscle differentiation begin prior to the experimentally imposed onset of fusion in EGTA-synchronized cultures. Additionally, the accumulation of M-creatine kinase subunits, also typical for muscle differentiation, is shown by microcomplement fixation to begin before the switch from EGTA to standard medium. Creatine kinase isoenzyme patterns also show that the transition from B- to M-subunit-containing creatine kinases occurs in EGTA cultures not switched to standard medium. Like EGTA, 5-bromodeoxyuridine (BrdUrd) reversibly prevents myoblast fusion. By adding EGTA and BrdUrd in different sequences to muscle cell cultures, it is shown that they act at different stages in the course of in vitro myogenesis. Cells cultured in EGTA from 23 to 69 hr after plating fused very rapidly when switched to medium containing BrdUrd. In the reverse experiment, in which BrdUrd preceded EGTA, no fusion occurred. Parallel experiments with 5-fluorodeoxyuridine suggest that cell division is necessary to reverse the inhibitory effect of BrdUrd, but not that of EGTA; this is consistent with the observed kinetics of fusion after switching to standard medium. These data strongly support a model of myogenesis in vitro in which two processes (one BrdUrd-sensitive, the other EGTA-sensitive) occur sequentially. In the first process, myogenic cells give rise to cells capable of producing molecules necessary for (terminal) skeletal muscle differentiation, including both those required for cell fusion and specific isoenzymes. The second process, fusion itself, can occur in the presence of BrdUrd or in the absence of cell division.