Kinova Sepova H.,Katedra Bunkovej a Molekularnej Biologie Lieciv |
Bilkova A.,Katedra Bunkovej a Molekularnej Biologie Lieciv |
Bilka F.,Katedra Bunkovej a Molekularnej Biologie Lieciv |
Bezakova L.,Katedra Bunkovej a Molekularnej Biologie Lieciv
Ceska a Slovenska Farmacie | Year: 2010
Lactic acid bacteria comprise several genera of Gram-positive bacteria that are known for the production of different antimicrobial substances. Lactic acid and related organic acids, usual metabolites of saccharide metabolism, inhibit the growth of other microbes mainly by lowering pH. Bacteriocins, proteinaceous antimicrobial substances, are produced ribosomally and those of lactic acid bacteria are well examined. Some species, for example Lactobacillus reuteri, are able to produce specific substances with miscellaneous structures. One of them, reutericyclin, a derivate of tetramic acid, is the first discovered antibiotic produced by a lactic acid bacterium. Reuterin, a complex of 3- hydroxypropionaldehyde and its related forms, is a strong antimicrobial substance produced by several species of the genus Lactobacillus. Because of a non-pathogenic character of lactic acid bacteria, they can be used as food preservatives or as promising antimicrobials in human and/or animal therapy.
Bilkova A.,Katedra Bunkovej A Molekularnej Biologie Lieciv |
Sepova H.K.,Katedra Bunkovej A Molekularnej Biologie Lieciv |
Bilka F.,Katedra Bunkovej A Molekularnej Biologie Lieciv |
Balazova A.,Katedra Bunkovej A Molekularnej Biologie Lieciv
Ceska a Slovenska Farmacie | Year: 2011
Lactic acid bacteria comprise several genera of gram-positive bacteria that are known for the production of structurally different antimicrobial substances. Among them, bacteriocins are nowadays in the centre of scientific interest. Bacteriocins, proteinaceous antimicrobial substances, are produced ribosomally and have usually a narrow spectrum of bacterial growth inhibition. According to their structure and the target of their activity, they are divided into four classes, although there are some suggestions for a renewed classification. The most interesting and usable class are lantibiotics. They comprise the most widely commercially used and well examined bacteriocin, nisin. The non-pathogenic character of lactic acid bacteria is advantageous for using their bacteriocins in food preservation as well as in feed supplements or in veterinary medicine.
Animal lipoxygenases - mechanism of catalysis in relation to formation of biologically active eicosanoids [Živočíšne Lipoxygenázy - Mechanizmus Katalýzy Vo Vzťahu K Tvorbe Biologicky Účinných Eikozanoidov]
Hoffman P.,Katedra bunkovej a molekularnej biologie lieciv |
Bezakova L.,Katedra bunkovej a molekularnej biologie lieciv |
Holkova I.,Katedra bunkovej a molekularnej biologie lieciv |
Pekarova M.,Katedra bunkovej a molekularnej biologie lieciv |
Oblozinsky M.,Katedra bunkovej a molekularnej biologie lieciv
Chemicke Listy | Year: 2012
Lipoxygenases form a family of nonheme ironcontaining enzymes involved in the lipid peroxidation processes. They participate, together with cyclooxygenases and cytochrome P-450, in the arachidonic acid metabolism, forming a group of cell signal molecules and secondary messengers called eicosanoids. The lipoxygenasecatalyzed reactions are highly controlled processes mediated by steric shielding of substrate by bulky amino acid side chains in the reaction center. Equally important is the channeling of molecular oxygen and the anchoring of substrate in a substrate-binding cavity. From the viewpoint of development of new effective drugs, study of lipoxygenases and biologically active eicosanoids opens new horizons for affecting pathological processes.
PubMed | Katedra bunkovej a molekularnej biologie lieciv
Type: Journal Article | Journal: Ceska a Slovenska farmacie : casopis Ceske farmaceuticke spolecnosti a Slovenske farmaceuticke spolecnosti | Year: 2012
Lipoxygenases (LOX) represent a family of lipid peroxidising enzymes which catalyse the reaction of achiral polyunsaturated fatty acids by oxygen forming chiral peroxide products possessing high positional stereospecific purity. The four double bonds of arachidonic acid, the main substrate of animal LOX, present the position for a wide range of enzymatic modifications enabling eicosanoid creation, unique molecules with biological significance. In this study, lipoxygenase from rat lung cytoplasma was isolated and purified to 40-fold by combining hydrophobic and gel chromatography. The forming positional specific fatty acid hydroxyl-isomers were separated on a nonpolar system (RP-HPLC) and identified on a polar adsorbent (SP-HPLC). In the purified enzyme, dual positional specificity was demonstrated by the production of 12- and 15-HETE in the ratio of 1,0:1,38, which responds to the product spectrum of mammalian 15-LOX-1.