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Wyszukujesz frazę "enzyme purification" wg kryterium: Temat


Wyświetlanie 1-4 z 4
Tytuł:
Isolation and characterization of pigeon breast muscle cytosolic 5´-nucleotidase-I (cN-I)
Autorzy:
Tkacz-Stachowska, Kinga
Lechward, Katarzyna
Skladanowski, Andrzej
Powiązania:
https://bibliotekanauki.pl/articles/1041318.pdf
Data publikacji:
2005
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
skeletal muscle
pigeon
enzyme purification
tissue distribution
5´-nucleotidase
Opis:
5´-Nucleotidase specific towards dCMP and AMP was isolated from avian breast muscle and characterized. It was found to be similar to a type-I form (cN-I) identified earlier as the AMP-selective 5´-nucleotidase responsible for adenosine formation during ATP breakdown in transfected COS-7 cells. Expression pattern of the cN-I gene in pigeon tissues indicated breast muscle as a rich source of the transcript. We purified the enzyme from this source using two-step chromatography and obtained an active homogenous preparation, free of ecto-5´-nucleotidase activity. The tissue content of the activity was calculated at 0.09 U/g wet weight. The specific activity of the enzyme preparation was 4.33 U/mg protein and it preferred dCMP and AMP to dAMP and IMP as a substrate. Its kinetic properties were very similar to those of the enzyme purified earlier from heart tissue. It was strongly activated by ADP. Inhibition by inorganic phosphate was more pronounced than in heart-isolated cN-I. Despite this difference, a similar physiological function is suggested for cN-I in both types of muscle.
Źródło:
Acta Biochimica Polonica; 2005, 52, 4; 789-796
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Mass spectrometry identification of membrane-bound respiratory nitrate reductase from Bradyrhizobium sp. (Lupinus)
Autorzy:
Polcyn, Władysław
Powiązania:
https://bibliotekanauki.pl/articles/1040683.pdf
Data publikacji:
2008
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
immunoblot screening
membrane-bound nitrate reductase [EC 1.7.99.4]
enzyme purification
Bradyrhizobium sp. (Lupinus)
rhizobia
mass spectrometry sequencing
Opis:
Respiratory nitrate reductase (NR) from Bradyrhizobium sp. (Lupinus) USDA 3045 has biochemical properties of the membrane-bound NR type. However, in the completely sequenced rhizobium genomes only genes for the periplasmic type of dissimilatory NR were found. Therefore purification and identification of the enzyme by tandem mass spectrometry (MS/MS) was undertaken. MS/MS spectra representing 149 unique tryptic peptides derived from purified 137-kDa subunit matched the NCBInr-deposited NarG sequences. MS/MS sequencing of two other SDS/PAGE bands (65- and 59-kDa) identified them as derivatives of the NarH-type protein. Applying additional validation criteria, 73% of the sequence of the NarG subunit (902 aa) and 52% of NarH sequence (266 aa) was assembled (UniProt KB acc. no. P85097 and P85098). This is the first unambiguous identification of an active NarGH-like NR in rhizobia. Moreover, arguments are provided here for the existence of a functional enzyme of this type also among other rhizobial species, basing on immunoblot screening and the presence of membrane-associated NR-active electrophoretic forms.
Źródło:
Acta Biochimica Polonica; 2008, 55, 4; 753-760
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Effects of Tremella fuciformis-Derived Polysaccharides with Different Molecular Weight on D-Galactose-Induced Aging of Mice
Autorzy:
Luo, Donghui
Liu, Xiaofei
Guan, Jingjing
Jang, Guili
Hua, Yanglin
Zhang, Xinfei
Xu, Xiaofei
Powiązania:
https://bibliotekanauki.pl/articles/16538544.pdf
Data publikacji:
2023-05-25
Wydawca:
Instytut Rozrodu Zwierząt i Badań Żywności Polskiej Akademii Nauk w Olsztynie
Tematy:
mushroom
polysaccharide purification
anti-oxidant activity
anti-aging activity
structure-function relationship
anti-oxidant enzyme
Opis:
The structure-bioactivity relationship of Tremella fuciformis polysaccharides (TFPs) in anti-aging in vivo is rarely reported. In the present study, a purified TFP, named HM, mainly composed of mannose, fucose, xylose, and glucose in a molar ratio of 4.14:0.98:0.81:0.62, was obtained from the fruiting body of T. fuciformis. Subsequently, two differentially degraded TFPs, named MM and LM, respectively, were prepared by a combined method of ultrasonic irradiation (US) and H2O2 treatment. Their structural properties, scavenging activities against free radicals in vitro, and anti-aging effects on D-galactose-induced aging of mice were determined. The average molecular weight of HM, MM, and LM was 58.3×106, 4.68×106, and 3.14×105 Da, respectively. All three TFPs were devoid of triple helix conformation and exhibited concentration- and molecular weight-dependent scavenging activity against radicals. The TFPs markedly relieved skin aging, effectively attenuated oxidative stress, and significantly decreased inflammation in D-galactose-induced aging mice. MM exhibited the best anti-aging effect among the TFPs. Additionally, TFPs partially restored the alterations in pH and the total content of short-chain fatty acids (SCFAs) in the colon but exhibited various impacts on the content of the individual SCFAs. These findings would provide rational guidance for a better application of TFPs in anti-aging foods and expand our understanding of the structure-function relationship of mushroom polysaccharides.
Źródło:
Polish Journal of Food and Nutrition Sciences; 2023, 73, 2; 163-174
1230-0322
2083-6007
Pojawia się w:
Polish Journal of Food and Nutrition Sciences
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Alkaline trypsin from the viscera and heads of Engraulis anchoita: partial purification and characterization
Autorzy:
Lamas, D.L.
Yeannes, M.I.
Massa, A.E.
Powiązania:
https://bibliotekanauki.pl/articles/951322.pdf
Data publikacji:
2017
Wydawca:
Polska Akademia Nauk. Czytelnia Czasopism PAN
Tematy:
alkaline protease
trypsin
viscera
head
Engraulis anchoita
purification
proteinase activity
ethylenediaminetetraacetic acid
sodium dodecyl sulphate-polyacrylamide gel electrophoresis
proteolytic enzyme
Źródło:
BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology; 2017, 98, 2
0860-7796
Pojawia się w:
BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology
Dostawca treści:
Biblioteka Nauki
Artykuł
    Wyświetlanie 1-4 z 4

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