Characterization of functional properties of Enterococcus spp. isolated from Turkish white cheese

LWT ◽  
2017 ◽  
Vol 75 ◽  
pp. 358-365 ◽  
Author(s):  
Hümeyra İspirli ◽  
Fatmanur Demirbaş ◽  
Enes Dertli
Keyword(s):  
Functional Properties ◽  
White Cheese ◽  
Enterococcus Spp

scholarly journals Characterization of chemical composition and techno‐functional properties of oat cultivars

2021 ◽  
Author(s):  
Renáta Németh ◽  
Fanni Turóczi ◽  
Dorottya Csernus ◽  
Fanni Solymos ◽  
Edina Jaksics ◽  
...  
Keyword(s):  
Chemical Composition ◽  
Functional Properties ◽  
Oat Cultivars

scholarly journals Characterization of a specific form of protein kinase C overproduced by a C3H 10T½ cell line

1990 ◽  
Vol 266 (1) ◽  
pp. 173-178 ◽  
Author(s):  
S A Rotenberg ◽  
R S Krauss ◽  
C M B Borner ◽  
I B Weinstein
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Functional Properties ◽  
Genetically Engineered ◽  
Specific Form ◽  
Major Peak ◽  
Promoter Activation ◽  
Kinase C ◽  
Structural And Functional Properties

Murine embryo fibroblasts (C3H 10T1/2) which were genetically engineered to overproduce the beta 1 isoform of protein kinase C (PKC-beta 1) were used to obtain homogeneous preparations of PKC-beta 1 for the purpose of characterizing the specific structural and functional properties of this isoform. Fractionation of PKC activity from these cells by hydroxyapatite chromatography produced one major peak, which represented 93% of the total cellular PKC activity and was not detected in control cells. This major peak of activity was shown by Western-blotting analysis with a beta 1-specific antiserum to be the overproduced beta 1-isoform, and exhibited a band at 77 kDa. The functional properties of the overproduced PKC-beta 1 were established with regard to phospholipid-dependence, Ca2(+)-dependence, responsiveness to a phorbol ester tumour promoter, activation by arachidonic acid (plus Ca2+), and inhibition by known PKC inhibitors. From these studies we conclude that PKC-beta 1 overproduced by C3H 10T1/2 cells exhibits the structural and functional properties previously ascribed to native PKC. Furthermore, these data provide the first definitive biochemical characteristics of this isoform of PKC.

scholarly journals Preparation of glycosylated hydrolysate by liquid fermentation with Cordyceps militaris and characterization of its functional properties

2020 ◽  
Vol 40 (suppl 1) ◽  
pp. 42-50
Author(s):  
Shuang YANG ◽  
Mingzhu ZHENG ◽  
Sheng LI ◽  
Yu XIAO ◽  
Qi ZHOU ◽  
...  
Keyword(s):  
Functional Properties ◽  
Cordyceps Militaris ◽  
Liquid Fermentation

A new model system for endometritis: Basic concepts and characterization of phenotypic and functional properties of bovine uterine neutrophils

1996 ◽  
Vol 46 (8) ◽  
pp. 1339-1356 ◽  
Author(s):  
H. Zerbe ◽  
H.-J. Schuberth ◽  
M. Hoedemaker ◽  
E. Grunert ◽  
W. Leibold
Keyword(s):  
Functional Properties ◽  
Model System ◽  
New Model ◽  
Basic Concepts

Cloning and functional characterization of a superfamily of microbial inwardly rectifying potassium channels

2006 ◽  
Vol 26 (1) ◽  
pp. 1-7 ◽  
Author(s):  
Si Sun ◽  
Jo Han Gan ◽  
Jennifer J. Paynter ◽  
Stephen J. Tucker
Keyword(s):  
Functional Properties ◽  
Functional Characterization ◽  
Unicellular Eukaryote ◽  
Channel Blockers ◽  
E Coli ◽  
Inwardly Rectifying Potassium Channels ◽  
Genes Encoding ◽  
Functionally Diverse ◽  
Inwardly Rectifying

Our understanding of the mammalian inwardly rectifying family of K+ channels (Kir family) has recently been advanced by X-ray crystal structures of two homologous prokaryotic orthologs (KirBac1.1 and KirBac3.1). However, the functional properties of these KirBac channels are still poorly understood. To address this problem, we cloned and characterized genes encoding KirBac orthologs from a wide variety of different prokaryotes and a simple unicellular eukaryote. The functional properties of these KirBacs were then examined by growth complementation in a K+ uptake-deficient strain of Escherichia coli (TK2420). Whereas some KirBac genes exhibited robust growth complementation, others either did not complement or showed temperature-dependent complementation including KirBac1.1 and KirBac3.1. In some cases, KirBac expression was also toxic to the growth of E. coli. The KirBac family exhibited a range of sensitivity to the K+ channel blockers Ba2+ and Cs+ as well as differences in their ability to grow on very low-K+ media, thus demonstrating major differences in their permeation properties. These results reveal the existence of a functionally diverse superfamily of microbial KirBac genes and present an excellent resource for the structural and functional analysis of this class of K+ channels. Furthermore, the complementation assay used in this study provides a simple and robust method for the functional characterization of a range of prokaryotic K+ channels that are difficult to study by traditional methods.

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