The effect of sedimentation and microbial nitrogen regeneration in a plankton community: a simulation investigation

A computer simulation model was developed to investigate nitrogenfluxes associated with microbial interactions in plankton communities.A short time scale was used, appropriate to the build-up anddecline of phytoplankton blooms in temperate shelf waters aftera mixing or upwelling event. The model depicts a continuum ofevents, many of which have been observed in coastal, upwellingand oceanic systems, including two phytoplankton peaks correspondingto ‘new production’ and ‘regenerated production’.It predicts that nitrogen loss through sedimentation of phytoplanktonand faeces may result in a smaller bloom with a delayed onsetand prolonged duration. Microbial regeneration of nitrogen wasfound to be important in sustaining the middle stages of a phytoplanktonbloom, whereas micro- and meso-zooplankton regeneration occurredtowards the end of the bloom.     

Stimulation by glycerate 2,3-bisphosphate: a common property of cytosolic IMP-GMP 5'-nucleotidase in rat and human tissues

Glycerate 2,3-bisphosphate, a potent stimulator of the cytosolic 5'-nucleotidase which preferentially hydrolyzes IMP and GMP in human erythrocytes (Bontemps et al., 1988, Biochem. J. 250, 687-696), also stimulates the dephosphorylation of IMP in cytosol fractions of rat heart, liver, brain, kidney, spleen and erythrocytes, and of human polymorphonuclear leucocytes, mixed peripheral blood lymphocytes, platelets and fibroblasts. Depending on the cell type, stimulation by 5 mM glycerate 2,3-bisphosphate varied from 1.5- to 12-fold. Where investigated, glycerate 2,3-bisphosphate had an approx. 5-fold higher affinity for the enzyme than its other stimulator, ATP. These observations provide a useful tool to distinguish IMP-GMP 5'-nucleotidase from other 5'-nucleotidases, and suggest a common origin of the cytosolic IMP-GMP 5'-nucleotidase in various tissues.     

Purification and enzymatic characterization of CMP-sialic acid: beta-galactosyl1----3-N-acetylgalactosaminide alpha 2----3-sialyltransferase from human placenta

A CMP-NeuAc:Gal beta 1----3GalNAc-R alpha 2----3-sialyltransferase has been purified over 20,000-fold from a Triton X-100 extract of human placenta by affinity chromatography on concanavalin A-Sepharose and CDP-hexanolamine-Sepharose in a yield of 10%. Sodium dodecyl sulfate-gel electrophoresis under reducing conditions revealed that the enzyme consists of a major polypeptide species with a molecular weight of 41,000 and some minor forms with molecular weights of 40,000, 43,000, and 65,000, respectively, which can be resolved partially by gel filtration on Sephadex G-100. Isoelectric focusing revealed that the enzyme occurs in a major and a minor charged form with pI values of 5.0-5.5 and 6.0, respectively. Acceptor specificity studies indicated that the enzyme catalyzes the incorporation of sialic acid from CMP-NeuAc into glycoproteins, glycolipids, and oligosaccharides which possess a terminal Gal beta----3GalNAc unit. Analysis of the structure of the product chain by high-pressure liquid chromatography and thin layer chromatography as well as methylation analysis revealed that a NeuAc alpha 2----3Gal beta 1----3GalNAc sequence is elaborated. The best glycoprotein acceptors are antifreeze glycoprotein and porcine submaxillary asialo/afucomucin. The disaccharide Gal beta 1----3GalNAc-Thr shows values for Km and V which are close to those of the latter glycoprotein. Lactose as well as oligosaccharides in which galactose is linked beta 1----3 or beta 1----4 to N-acetylglucosamine are less efficient acceptors. Of the glycolipids tested only gangliosides GM1 and GD1b served as an acceptor. The enzyme does not show an absolute aglycon specificity, and attaches sialic acid regardless the anomeric configuration of the N-acetylgalactosaminyl residue in the accepting Gal beta 1----3GalNAc unit. By use of specific acceptor substrates it could be demonstrated that the purified enzyme is free from other known sialyltransferase activities. Studies with rabbit antibodies raised against a partially purified sialyltransferase preparation indicated that the enzyme is immunologically unrelated to a Gal beta 1----4GlcNAc-R alpha 2----3-sialyltransferase, which previously had been identified in human placenta (Van den Eijnden, D.H., and Schiphorst, W. E. C. M. (1981) J. Biol. Chem. 256, 3159-3162). Initial-rate kinetic studies suggest that the sialyltransferase operates through a mechanism involving a ternary complex of enzyme, sugar donor, and acceptor. This is the first report on the extensive purification and characterization of a sialyltransferase from a human tissue.     

Altered concentrations of gonadotrophin, prolactin and GnRH receptors, and endogenous steroids in the abdominal testes of adult unilaterally cryptorchid rats

Testicular descent was prevented unilaterally in newborn rats by cutting the gubernaculum testis. At 100 days of age, the number of Leydig and Sertoli cells per testis, the concentration of receptors for LH, FSH, prolactin and GnRH, and endogenous concentrations of progesterone and testosterone were determined. The weight of the abdominal testes was reduced by 80%, but in spite of this they contained as many Sertoli (32.8 +/- 1.3 X 10(6), mean +/- s.e.m., n = 6) and Leydig (28.2 +/- 1.7 X 10(6) cells as did scrotal testes (32.1 +/- 2.5 X 10(6) and 24.3 +/- 1.2 X 10(6) respectively). The numbers of receptors for LH (3.2 +/- 0.2 and 1.0 +/- 0.2 pmol/testis, mean +/- s.e.m., n = 11), FSH (358 +/- 11.0 and 96.3 +/- 12.6 fmol/testis) and prolactin (535 +/- 32.7 and 92.4 +/- 13.2 fmol/testis) were reduced (P less than 0.001) in abdominal testes, but the number of GnRH receptors was unaffected (8.9 +/- 1.4 and 12.1 +/- 1.8 fmol/testis, n = 6). Testicular testosterone concentration (30.9 +/- 4.4 vs 15.4 +/- 3.2 ng/g, n = 11, P less than 0.001), but not that of progesterone (0.87 +/- 0.10 vs 1.01 +/- 0.21 ng/g), was decreased in abdominal testes. The decreased receptor and androgen values reflect functional disturbances in the abdominal testes. The changed local milieu within abdominal testes may reduce hormone receptor concentrations which are then involved in the observed Leydig cell dysfunction.     

The nucleotide sequence of tobacco rattle virus RNA-2 (CAM strain).

The nucleotide sequence of the smaller genomic strand (RNA-2) of the bipartite tobacco rattle virus (CAM strain) has been determined. RNA-2 is capped at the 5' terminus and contains 1799 nucleotide residues. There is a single 223 codon long open reading frame extending from nucleotide 574 to 1242 which designates a protein of Mr 23,654. The derived amino acid composition, in percent, matches that previously determined for the virus capsid protein. The long open reading frame is flanked by 5' and 3' untranslated regions of 573 and 554 nucleotides, respectively. The 5' leader sequence contains two different sets of direct repeats, one of 119 nucleotides and the other of 76. It also contains 13 apparently unused AUG codons, four of which lie in the same frame as the capsid protein cistron. The 3' terminal sequence of RNA-2 is identical to that of the larger genomic strand (RNA-1) for 459 nucleotides.