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1.
Prikl Biokhim Mikrobiol ; 32(6): 646-9, 1996.
Article in Russian | MEDLINE | ID: mdl-9011863

ABSTRACT

The promoting effect of electromagnetic field (EMF) on biosynthesis and activity of extracellular proteinase and lectin in B. subtilis 316 M was observed. It caused 1.5- and 4-fold increase of the metabolites yield respectively. The EMF stimulated a 2-fold activation of lectin, rise of the enzyme activity and a shift of it pI from 11.4-11.5 to 9.2-9.3.


Subject(s)
Bacillus subtilis/radiation effects , Electromagnetic Fields , Lectins/radiation effects , Serine Endopeptidases/radiation effects , Bacillus subtilis/metabolism , Enzyme Stability , Isoelectric Focusing , Lectins/isolation & purification , Serine Endopeptidases/isolation & purification
2.
Ukr Biokhim Zh (1978) ; 65(1): 104-6, 1993.
Article in Russian | MEDLINE | ID: mdl-8351733

ABSTRACT

The influence of electromagnetic field on the subtilisin of Bacillus subtilis strain 316 M preparation has been studied. It is the increase 30-60% of the proteolytic activity during 60-100 min treatment was observed. The effect of activation is stable for a month at +4 degrees C. The increase of the proteolytic activity is connected with conformational changes of the enzyme molecule, with the decrease of pI from 11.4 to 9.2 in particular.


Subject(s)
Bacillus subtilis/enzymology , Electromagnetic Fields , Subtilisins/radiation effects , Chemical Phenomena , Chemistry, Physical , Enzyme Activation/radiation effects , Enzyme Stability/radiation effects , Protein Conformation , Subtilisins/chemistry
3.
Ukr Biokhim Zh (1978) ; 61(4): 103-7, 1989.
Article in Russian | MEDLINE | ID: mdl-2511650

ABSTRACT

The ultrafiltration method with application of Vladipor membranes YAM-300 has been used to obtain 8.9 times purified preparation of beta-D-galactosidase (EC 3.2.1.23) from the Escherichia coli lysate. The preparation activity is 43,400 u/g, specific activity--167.57 u/mg of protein. The preparation includes 25.9% of protein and does not possess the collateral proteolytic activity. The results of the ultraconcentrate isofocusing in the borate-polyol system within the pH range of 4.5-9.5 and electrophoresis in polyacrylamide gel testify to the presence of five basic protein fractions, one of which includes 57 +/- 2% of protein with the beta-galactosidase activity. This fraction is homogeneous, its isoelectric point corresponds to pH 7.8.


Subject(s)
Galactosidases/metabolism , beta-Galactosidase/metabolism , Electrophoresis, Polyacrylamide Gel , Escherichia coli/enzymology , Isoelectric Focusing , Ultrafiltration , beta-Galactosidase/isolation & purification
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