[Catalytic properties of Rhodotorula aurantiaca KM-1 phenylalanine ammonia-lyase].

L-Phenylalanine ammonia-lyase (PAL, EC 4.3.1.

[Transgenic Tobacco plants expressing bacterial genes encoded the thermostable glucanases].

It is shown that bacterial genes for thermostable beta-glucanases are expressed retaining their activity and substrate specificity. The leader peptide of the carrot extensin exerts effective secretion of the bacterial enzymes into the intercellular space of the plant tissue. Expression of the bacterial gene for beta-1,3-glucanase in plant tissues alters their morphogenetic potential.

[Construction and analysis of transgenic plants of Nicotiana tabacum L. expressing a bacterial gene for beta-1,3-glucanase. II. Transgenic tobacco plants expressing the bacterial beta-glucanase gene from Clostridium thermocellum,--a model for studying the differential expression of stress response-related genes].

The modified hybrid beta-1,3-glucanase gene (glc) of Clostridium thermocellum was expressed in tobacco Nicotiana tabacum. The glc gene was cloned into two plasmids, pC27-glc and pC29-glc, in which its expression was controlled by the TR2' promoter of the 2' gene of T-DNA and the rbcS promoter of Arabidopsis, respectively. These constructions were used for transformation of agrobacteria followed by transfer into plants.

[Construction and analysis of transgenic plants of Nicotiana tabacum L. expressing a bacterial gene for beta-1,3-glucanase. I. Construction of vector plasmids for transfer into plants and expression of a modified gene for beta-1,3-glucanase from Clostridium thermocellum in tobacco protoplasts].

We constructed two vectors, pC27-glc and pC29-glc, that allow expression of the beta-1,3-glucanase gene (glc) in plant cells. The glc gene was previously cloned from anaerobic thermophilous bacterium Clostridium thermocellum. To increase the efficiency of expression, the N-terminal fragment of the glc gene encoding bacterial transient peptide was deleted, and hybrid variants of lacZ-glc were obtained.

[The effect of L-glutamic acid on the ADP-induced aggregation and Ca, Mg-ATpase activity of human thrombocytes].

In the study of L-glutaminic acid effects on human platelet functional activity it was established that 30-60-min treatment of platelet-rich plasma with glutamate in concentration 0.1-1.0 mM at 37 degrees C results in a marked platelet activation.

[The regulation of protein kinase C activity in normal, immortalized and transformed rat fibroblasts].

In view of recent studies showing that cell proliferation of E1Aad5+c-Ha-ras-transformed fibroblasts cannot be regulated by growth factors and phorbol eaters in contrast to normal and E1Aad5-immortalized cell lines, the present work was undertaken to examine the role of protein kinase C (PKC) in the mitogenic signal transduction machinery in rat embryonal fibroblasts. It is shown that PKC is activated by acidic growth factor and phorbol esters in all the three cell lines. These findings suggest the existence of an additional, not associated with PKC-, growth-signaling pathway in E1Aad5-Ha-ras-transformed rat embryonal fibroblasts.

[Glutamate-binding membrane proteins from human platelets].

Solubilization of the total membrane fraction of human platelets in a 2% solution of sodium deoxycholate and subsequent affinity chromatography on glutamate agarose resulted in two protein fractions possessing a glutamate-binding activity. As can be evidenced from radioligand binding data, the first fraction contains two types of binding sites (Kd1 = 1 microM, Bmax 1 = 100 pmol/mg of protein; Kd2 = 9.3 microMm Bmax2 = 395 pmol/mg of protein).

[A rapid method of isolation of platelet membranes for radioligand and enzymatic assays].

A simple and rapid procedure for isolation of the total platelet membrane fraction by chromatography on Sepharose CL 6B has been developed. This method allows a rapid (25-30 min) one-step separation of the membrane fraction on 26 x 150 mm columns with a 20-21 mg recovery. The high degree of purity of membrane preparations was confirmed by a radioligand assay using [3H]adenosine and L-[3H]glutamic acid.

[The sites of high affinity binding of L-[3H]glutamic acid in human platelets. A new type of platelet receptor?].

The total membrane fraction of human platelets was found to contain high affinity sites of L-[3H]glutamic acid binding (Kd = 100 nM, Bmax = 1.06 pmol/mg protein). The pH optimum for binding is at pH approximately 6.