Tyrosine aminotransferase: a transaminase among others?

Tyrosine aminotransferase (L-tyrosine: 2 oxoglutarate aminotransferase; EC 2.6.1.5; TATase) is the first enzyme in the catabolic pathway of tyrosine. The gene of this transaminase is regulated by glucocorticoid hormones as well as via the cAMP pathway. This review gives a brief survey of the structural and physico-chemical properties of this well-known protein. A comparative study of the properties of TATase with other aminotransferases is also included to analyse this molecule for itself, and not only as a marker used in studies on enzymatic induction. Finally, the regulation of the gene expression is presented, in order to underline a few important features of this model.     

Chemotaxis and nod Gene Activity of Bradyrhizobium japonicum in Response to Hydroxycinnamic Acids and Isoflavonoids

For Bradyrhizobium japonicum, the chemotactic and the nod gene-inducing effects of hydroxycinnamic acids and two of their derivatives were compared with those of isoflavonoids. Only the hydroxycinnamic acids were strong chemoattractants, while the other substances tested were chemotactically inactive. Besides the known nod gene induction by isoflavonoids, a weak nod gene induction by coniferyl alcohol, chlorogenic acid, and ferulic acid was found.     

Changes of dipeptidylpeptidase IV as a membrane marker of lymphocytes in acute and chronic liver diseases--biochemical and cytochemical investigations.

Lymphocytic dipeptidylpeptidase IV (DPP-IV, E.C. 3.4.14.5) is described as a marker enzyme of immunostimulant T-lymphocytes as well as functional characteristic of interleukin-2-producing cells. Cytochemical staining of DPP-IV positive lymphocytes and measurements of DPP-IV activity in mononuclear cells and in sera of patients suffering from different kinds of liver diseases were performed to evaluate the average activities in positive cells. The results demonstrated that this serine exopeptidase exhibits extremely low activity in autoimmune chronic hepatopathies. On the contrary, hepatitis-B-associated liver diseases were connected with markedly increased values. Furthermore, significant differences of DPP-IV activity were found in different kinds of acute and chronic liver diseases. These findings are discussed in connection with the participation of dipeptidylpeptidase IV in impaired immunoregulation of the altered liver.     

Nitrate levels affect the development of the black locust-Rhizobium symbiosis

Summary Experiments with black locust (Robinia pseudoacacia L.) seedlings grown under strictly controlled laboratory conditions indicated that the availability of nitrate has a marked impact on nitrogen fixation. When nitrate concentrations were very low, both nodulation and seedling growth were impaired, whereas nitrate concentrations high enough to promote plant growth strongly inhibited symbiotic nitrogen fixation. When nitrate was added to the growth medium after infection, nodulation and nitrogen fixation of the seedlings decreased. This effect was even more marked when nitrate was applied before infection with rhizobia. Higher nitrogen concentrations also reduced nodule number and nodule mass when applied simultaneously with the infecting bacteria. The contribution of symbiotic nitrogen fixation to black locust shoot mass by far exceeded its effects on shoot length and root mass. When nitrate availability was very low, specific nitrogen fixation (i. e. nitrogenase activity per nodule wet weight) was improved with increasing nitrogen supply, but rapidly decreased with higher nitrogen concentrations.     

Ultrastructural evidence for a triple structure of the lateral element of the synaptonemal complex.

This study describes composition and localization of several substructures of the synaptonemal complex (SC) using different techniques. The techniques which were used were surface spreading, critical point drying of isolated SCs, and sectioning of Lowicryl embedded testis material. The lateral elements (LEs) of the SC appear to be composed of three lateral substructures: two morphologically identical major strands and a third strand which is considerably thinner. The thinner strand is localized on the inner side of the two major strands of the lateral element. In late pachytene/early diplotene stages when the SC starts to disintegrate more than three strands can be observed in the LEs. A model is presented and the function of the different substructures is speculated upon.     

Purification and substrate specificity of heparitinase I and heparitinase II from Flavobacterium heparinum. Analyses of the heparin and heparan sulfate degradation products by 13C NMR spectroscopy

The purification of two heparitinases and a heparinase, in high yields from Flavobacterium heparinum was achieved by a combination of molecular sieving and cation-exchange chromatography. Heparinase acts upon N-sulfated glucosaminido-L-iduronic acid linkages of heparin. Substitution of N-sulfate by N-acetyl groups renders the heparin molecule resistant to degradation by the enzyme. Heparitinase I acts on N-acetylated or N-sulfated glucosaminido-glucuronic acid linkages of the heparan sulfate. Sulfate groups at the 6-position of the glucosamine moiety of the heparan sulfate chains seem to be impeditive for heparitinase I action. Heparitinase II acts upon heparan sulfate producing disulfated, N-sulfated and N-acetylated-6-sulfated disaccharides, and small amounts of N-acetylated disaccharide. These and other results suggest that heparitinase II acts preferentially upon N,6-sulfated glucosaminido-glucuronic acid linkages. The total degradation of heparan sulfate is only achieved by the combined action of both heparitinases. The 13C NMR spectra of the disaccharides formed from heparan sulfate and a heparin oligosaccharide formed by the action of the heparitinases are in accordance to the proposed mode of action of the enzymes. Comparative studies of the enzymes with the commercially available heparinase and heparitinase are described.     

Selective Medium for Isolating Phanerochaete chrysosporium from Soil

A selective medium was developed that is capable of isolating Phanerochaete chrysosporium from soil. This medium contains 15 ppm of benomyl (15 μg g⁻¹) and 550 ppm of streptomycin sulfate in 2% malt agar and is held at 39°C after inoculation. P. chrysosporium was isolated from three nonsterile forest soils to which the fungus had been added. These soils contained large microbial populations.     

Enhancement of specific nitrogenase activity inAzospirillum brasilense andKlebsiella pneumoniae,inhibition inRhizobium japonicum under air by phenol

Specific nitrogenase activity inAzospirillum brasilense ATCC 29145 in surface cultures under air is enhanced from about 50 nmol C₂H₄·mg protein^-1·h^-1 to 400 nmol C₂H₄ by the addition of 1 mM phenol. 0.5 and 2 mM phenol added increase the rate 5-fold and 4-fold. This enhancement effect is observed only between 2 and 3 days after inoculation, with only a small reduction of the growth of the cells by the phenol added. In surface cultures under 1% O₂, nitrogenase activity is slightly reduced by the addition of 1–0.01 mM phenol. Utilization of succinate is enhanced during the period of maximum enhancement of nitrogenase activity by 60% by addition of 1 mM phenol. The cells did not produce¹⁴CO₂ from [U-¹⁴C] phenol, neither in surface cultures nor in liquid cultures and less than 0.1% of the phenol was incorporated into the cells. A smaller but significant enhancement of nitrogenase activity by about 100% in surface cultures under air was found withKlebsiella pneumoniae K 11 after addition of 1 mM phenol. However, inRhizobium japonicum 61-A-101 all phenol concentrations above 0.01 mM reduced nitrogenase activity. With 1 mM phenol added activity was reduced to less than 10% with no effect on the growth in the same cultivation system. With thisRhizobium japonicum strain significant quantities of phenol (25 mol in 24 h by 2·10¹² cells) were metabolized to¹⁴CO₂, with phenol as sole carbon source. WithAzospirillum brasilense in liquid culture under 1% and 2% O₂ in the gas phase, no enhancement of nitrogenase activity by phenol was noticed.     

Primary structure of the southern bean mosaic virus coat protein: First results

Studies on the southern bean mosaic virus coat protein have established the molecular weight of this protein, its amino acid composition, the nature of its C-terminal amino acid, and the blockage of the N-terminal residue by an acetyl group. After hydrolysis of the protein by trypsin, the hydrolysate was fractionated by ion-exchange chromatography. Among the purified tryptic peptides were isolated the N- and the C-terminal peptides where sequences were determined, principally by mass spectrometry.