Species-specific algal responses to zooplankton: experimental and field observations in three nutrient-limited lakes

A series of 4-day manipulations of zooplankton biomass and nutrientavailability was performed in enclosures in three lakes to determinespecies-specific algal responses to herbivory and nutrient enrichment.Algal performance in enclosures was compared to the relationshipsbetween weekly algal growth rates and the zooplankton in situ.When in situ growth rates were significant functions of zooplanktonbiomass, the responses were generally consistent with responsesin the enclosure experiments. The importance of both nutrientsand zooplankton in mediating algal growth was demonstrated bynumerous observations: strong algal community response to enrichment,unimodal or positive responses of certain algal taxa to zooplanktonbiomass, differences in degree of nutrient limitation amongthe algal response types, lack of nutrient limitation of non-grazedalgal taxa and a preponderance of taxa with no net responseto increasing zooplankton biomass. Variation in the zooplanktoncommunity may be the largest source of variability in nutrientsupply rate during summer in stratified lakes, and causes substationalvariability in the algae. Algae responded more strongly to changesin zooplankton composition than to changes in zooplankton biomass.We conclude that, due to the close coupling of phytoplanktonand zooplankton communities in these nutrient-limited lakes,major compositional changes in the zooplankton have greatereffects on the algae than do changes in biomass of grazers alreadypresent. ¹Present address: Division of Environmental Studies, Universityof California, Davis, CA 95616, USA ²Present address: Division of Biological Sciences, Universityof California, Davis, CA 95616, USA     

Bounding fluid viscosity and translational diffusion in a fluid lipid bilayer

Fluorescence recovery after photobleaching was used to investigate the translational diffusion of a fluorescent derivative of a membrane-spanning lipid in L phase multibilayers of 1-palmitoyl-2-oleoylphosphatidylcholine prepared in water and in glycerol. The translational diffusion coefficient in hydrated bilayers (D _w) ranged between 2 and 5x10^–8 cm²/s and in glycerinated bilayers (D _g) the range was between 3 and 24×10^–10 cm²/s between 10° and 40°C. These results are discussed in terms of models for diffusion in membranes.     

Two of the three influenza viral polymerase proteins expressed by using baculovirus vectors form a complex in insect cells.

Each of the influenza virus polymerase (P) genes PB1, PB2, and PA was inserted into a baculovirus vector under the control of the polyhedrin promoter. In insect (Spodoptera frugiperda) cells infected by each baculovirus recombinant containing a P gene insert, a large amount of the encoded P protein was synthesized. Gel electrophoretic analysis of the total proteins in infected cells revealed the presence of a new protein band corresponding to the encoded P protein that was abundant enough to be stained with Coomassie blue. In cells infected simultaneously with both the PB1 and PB2 baculovirus recombinants, a PB1-PB2 complex was formed that was immunoprecipitated with an antiserum specific for either PB1 or PB2. In cells infected simultaneously with all three P baculovirus recombinants, a PB1-PB2 complex lacking the PA protein was formed. Formation of this PB1-PB2 complex partially mimics events that occur in influenza virus-infected cells, where all three P proteins form a complex with each other (B. M. Detjen, C. St. Angelo, M. G. Katze, and R. M. Krug, J. Virol. 61:16-22, 1987). These results indicate that the ability of PB1 and PB2 to form a complex is an intrinsic property of these two proteins that does not require the participation of other influenza viral gene products. Possible reasons for the absence of the PA protein from the immunoprecipitable P protein complex in insect cells infected by the three P baculovirus recombinants are discussed.     

Free and conjugated gibberellins in dormancy and germination of apple seeds

Halińska, A. and Lewak, St. 1987. Free and conjugated gibberellins in dormancy and germination of apple seeds.
The presence of gibberellin A₄ (GA₄) was confirmed in partly stratified seeds of apple ( Malus domestica Borb., cv. Antonówka) by mass spectrometry of the methyl ester. Levels of free and conjugated gibberellins A₄₊₇ and A₉ changed during drying of mature seeds, during cold and warm stratification, as well as during germination of dormant and non-dormant embryos. The temporary rise in GA₄₊₇ during cold stratification and during the culture of dormant embryos as well as the lack of it under conditions of warm stratification, allowed us to postulate a role for GA₄₊₇ in the removal of dormancy. In addition, GA₉ was absent in dormant embryos and increased during cold stratification and during the culture of non-dormant embryos. This suggests the involvement of GA₉, in induction of normal development of the seedling. The equivalence between changes in free and conjugated GAs suggests that formation and hydrolysis of conjugates are involved in the control of the physiologically active levels of free GA₄₊₇ and GA₉.     

Regional differences in quantities of histochemically detectable mucosubstances in nasal, paranasal, and nasopharyngeal epithelium of the bonnet monkey

Inhaled irritants induce secretory cell hyperplasia in nasal epithelium of animals. To characterize this response histochemically it is first important to know the histochemical character and distribution of epithelial mucosubstance in the normal nasal cavity. An automated image analyzing method was used to detect and quantitate acidic, neutral, and sulfated mucosubstances in the epithelium lining the nasal and paranasal airways of eight bonnet monkeys. Tissue sections 2 micron thick from defined regions of these airways were stained with either alcian blue/periodic acid-Schiff to demonstrate acid and neutral mucosubstances or high iron diamine to demonstrate sulfated mucins. Respiratory epithelium covering maxilloturbinates had the largest volume of stainable mucosubstance per unit surface area of basal lamina, whereas the maxillary sinus epithelium had the least. There was a general anteroposterior increase in the quantity of total epithelial mucosubstance along the septal and lateral walls of the nasal cavity, and there was more acidic than neutral mucosubstance in the posterior nasal airway than in the anterior. Epithelial mucosubstance in the maxillary sinus was predominantly neutral. Therefore, we conclude that there are substantial regional quantitative differences in stainable mucosubstances in the primate nasal epithelium which must be considered when examining nasal mucosa for irritant-induced changes in epithelial mucins.     

Human carcinoma cell lines xenografted in athymic mice: biological and antigenic characteristics of an intraabdominal model

Summary In order to investigate in vivo clinical applications of murine monoclonal antibodies directed against human ovarian carcinoma a preclinical in vivo model was developed using BALB/c athymic mice. Three human carcinoma cell lines (MCF7, HT29, and SW626) were injected into the peritoneal cavity of pristane-primed animals and the biological and antigenic characteristics of the i.p. grown tumors were studied. The animals were killed when moribund or 6–8 weeks after tumor injection. At autopsy tumor take was observed in 85% of the injected animals, whereas palpable nodules were evident in only 83%. Examination of the peritoneal cavity revealed intraabdominal carcinomatosis with tumor masses varying in size between 0.2 and 0.5 cm in diameter and tumor sheets. The most frequently affected organs were the diaphragm, the liver, and the reproductive system. Ascitic fluid formation was rare and no animal developed tumors outside the peritoneal cavity. To determine whether the in vivo tumors retained the same antigenic characteristics as the in vitro cell lines, four monoclonal antibodies (MBrl, MOv2, MOv8, and MOv15) directed against ovarian carcinoma-associated antigens and two different experimental approaches (immunofluorescence and immunoblotting) were used. Variations at either a quantitative or a qualitative level were observed for some antigens, whereas no evident changes were apparent for others. In particular, the antigens detected by MBr1 and MOv15 on the MCF7 line both maintained high levels of expression and immunoblotting staining pattern, whereas the antigens detected by MOv2 on the HT29 and SW626 lines, although present at a high level, clearly changed their staining pattern. As regards the antigens recognized by MOv8 and MOv15 on the HT29 and SW626 lines, we observed a drastic decrease in the level of their expression and in many cases a drop below the threshold of detectability of the test. The intraabdominal carcinomatosis described partially mimics the growth characteristics of human ovarian cancer and maintains the expression of some antigenic markers associated with epithelial tumors of the ovary and may therefore be useful in devising immunodiagnostic and/or immunotherapeutic strategies for ovarian carcinoma.     

Localization of proteins L4, L5, L20 and L25 on the ribosomal surface by immuno-electron microscopy

Summary Ribosomal proteins L4, L5, L20 and L25 have been localized on the surface of the 50S ribosomal subunit of Escherichia coli by immuno-electron microscopy. The two 5S RNA binding proteins L5 and L25 were both located at the central protuberance extending towards its base, at the interface side of the 50S particle. L5 was localized on the side of the central protuberance that faces the L1 protuberance, whereas L25 was localized on the side that faces the L7/L12 stalk. Proteins L4 and L20 were both located at the back of the 50S subunit; L4 was located in the vicinity of proteins L23 and L29, and protein L20 was localized between proteins L17 and L10 and is thus located below the origin of the L7/L12 stalk.     

Specificity towards oligomannoside and hybrid type glycans of the endo-β-N-acetylglucosaminidase B from the basidiomy ceteSporotrichum dimorphosporum

We have previously shown that an endo--N-acetylglucosaminidase (EC 3.2.1.96) named Endo B, isolated from culture filtrates of the basidiomyceteSporotrichum dimorphosporum cleaves asialo-, and to some extent, monosialylated bi-antennary glycans of theN-acetyllactosamine type linked to the asparagine residue of peptide or protein moieties [Bouquelet S, Strecker G, Montreuil J, Spik G (1980) Biochimie 62:43–49]. In the present paper, the substrate specificity of the enzyme towards oligomannoside and hybrid type glycans has been analyzed. The results obtained indicate that ovalbumin glycopeptides containing four to seven mannose residues and bovine lactotransferrin glycopeptides containing four to nine mannose residues were completely hydrolyzed by the enzyme. The degree of cleavage was variable among hybrid type structures, since glycopeptides containing the following glycans: (Gal)₁(GlcNAc)₃(Man)₅(GlcNAc)₂; (GlcNAc)₃(Man)₅(GlcNAc)₂; (GlcNAc)₃(Man)₄(GlcNAc)₂ were not hydrolyzed by the enzyme while the percentage of hydrolysis of a glycopeptide containing (GlcNAc)₂(Man)₅(GlcNAc)₂ glycan reached 90%. The bovine lactotransferrin was partially deglycosylated (40%) in the absence of non-ionic detergent while native ovalbumin glycoprotein was not hydrolyzed by the enzyme.The oligomannoside-and theN-acetyllactosamine-type degrading activities present in the culture filtrates were not separated at any step of the purification procedure. Both activities were eluted as a single component with an apparent molecular mass of 89 kDa suggesting that they are located on the same enzyme molecule.Endo B represents a powerful tool for removing oligomannoside-andN-acetyllactosamine-type glycans fromN-glycopeptides andN-glycoproteins. Moreover, advantages in the use of Endo B in a soluble form as well as in an immobilized form result in its high activity and in its stability to heat denaturation and storage.Abbreviations Gal d-galactose - Man d-mannose - GlcNAc N-acetyl-d-glucosamine - Con A concanavalin A - Asn asparagine - GLC gas liquid chromatography - TLC thin layer chromatography - Endo endo--N-acetylglucosaminidase - Endo B endo--N-acetylglucosaminidase isolated fromSporotrichum dimorphosporum - PBE polybuffer exchanger - SDS-PAGE sodium dodecylsulfate-polyacrylamide gel electrophoresis