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vulgaris
Chlorococcum humicola, Chlorella vulgaris, Chlamydomonas ovalis and Chlamydomonas sp.
      
coli 0101 amounts to 98.2; toProteus vulgaris 102, to 87.2; andStaphylococcus aureus 209p, to 83.2%.
      
?- Glucosidases from leaves and roots of the common beet,Beta vulgaris
      
?-Glucosidases detected in the leaves and roots of the common beet,Beta vulgaris, have been demonstrated to catalyze hydrolysis of native betacyanins.
      
The rate of CO2 gas exchange, transpiration, stomatal conductivity, and efficiency of the use of water were assessed in leaves of the sugar beet (Beta vulgaris var.
      
strain XL1 actively lysed pre-autoclaved cells of the gram-negative bacteria Proteus vulgaris and P.
      
The effect of the molecular weight of chitosan on its ability to suppress systemic infection of bean mild mosaic virus in bean (Phaseolus vulgaris L.) plants was studied.
      
Polysaccharides of cell cultures of Silene vulgaris
      
Callus and suspension cultures of campion (Silene vulgaris) produced pectin polysaccharides, similar in structure to the polysaccharides of intact plants.
      
The effect of ultraviolet radiation on the growth and polysaccharide composition of a callus culture of Silene vulgaris
      
The dynamics of hormonal status of developing red beet root (Beta vulgaris L.) in correlation with the dynamics of sugar accumul
      
Tryptophan Indole-Lyase from Proteus vulgaris: Kinetic and Spectral Properties
      
An efficient method for purification of recombinant tryptophanase from Proteus vulgaris was developed.
      
It was found that although the spectral properties of the holoenzymes and their complexes with amino acid inhibitors are different, the principal kinetic properties of the enzymes from Proteus vulgaris and Escherichia coli are analogous.
      
Four of them, Proteus penneri 4 (O72), Proteus vulgaris 63/57 (O37), Proteus mirabilis TG 277 (O69), and Proteus penneri 20 (O17), contain O-acetyl groups in non-stoichiometric quantities, and the polysaccharide of P.
      
Role of Arginine 226 in the Mechanism of Tryptophan Indole-Lyase from Proteus vulgaris
      
In the spatial structure of tryptophanase from Proteus vulgaris the guanidinium group of arginine 226 forms a salt bridge with the 3'-oxygen atom of the coenzyme.
      
Structure of Silenan, a Pectic Polysaccharide from Campion Silene vulgaris (Moench) Garcke
      
A pectic polysaccharide named silenan, [α]D20 +148.6° (c 0.1; H2O), was isolated earlier from the aerial part of campion, Silene vulgaris (Moench) Garcke.
      
Production of Polysaccharides by Silene vulgaris Callus Culture Depending on Carbohydrates of the Medium
      
 

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