Informacja

Drogi użytkowniku, aplikacja do prawidłowego działania wymaga obsługi JavaScript. Proszę włącz obsługę JavaScript w Twojej przeglądarce.

English (EN)·Polski (PL)·Yкраїнський (UK)
Przejdź do strony domowej biblioteki Centralna Biblioteka Wojskowa Link otwiera się w nowym oknie Logo biblioteki Prolib Integro - strona głównaCentralna Biblioteka Wojskowa

Wyszukujesz frazę "Amylase" wg kryterium: Temat

  Lista filtrów
Wyrównaj
    Wyświetlanie 1-5 z 5
    Tytuł:
    Activity of glycogen depolymerizing enzymes in extracts from brain tumor tissue (anaplastic astrocytoma and glioblastoma multiforme).
    Autorzy:
    Kotoński, Bogusław
    Wilczek, Joanna
    Madej, Janusz
    Zarzycki, Andrzej
    Hutny, Jan
    Powiązania:
    https://bibliotekanauki.pl/articles/1044051.pdf
    Data publikacji:
    2001
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    glioblastoma
    α-amylase
    α-glucosidase
    phosphorylase
    astrocytoma
    Opis:
    An approximately threefold increase in glycogenolytic activity of the neutral α-1,4-glucosidase and a twofold increase in the same activity of the acid isoform have been found in extracts of anaplastic astrocytoma and glioblastoma multiforme tumors of brain tissue. "Maltase activity" of the respective enzymes increased by 60-80% in both kinds of tumor extracts. However a significant decrease in α-amylase and almost complete disappearance of phosphorylase activities have also been found in both kinds of tumors.
    Źródło:
    Acta Biochimica Polonica; 2001, 48, 4; 1085-1090
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Screening and characterization of thermo-active enzymes of biotechnological interest produced by thermophilic Bacillus isolated from hot springs in Tunisia
    Autorzy:
    Thebti, Wajdi
    Riahi, Yosra
    Gharsalli, Rawand
    Belhadj, Omrane
    Powiązania:
    https://bibliotekanauki.pl/articles/1038787.pdf
    Data publikacji:
    2016
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    temperature
    amylase
    protease
    cellulase
    xylanase
    mannanase
    Geobacillus
    Tunisian hot springs
    Opis:
    As part of the contribution to the global efforts in research of thermostable enzymes being of industrial interest, we focus on the isolation of thermophilic bacteria from Tunisian hot springs. Among the collection of 161 strains of thermophilic Bacillus isolated from different samples of thermal water in Tunisia, 20% are capable of growing at 100°C and the rest grow at 70°C or above. Preliminary activity tests on media supplemented with enzyme-substrates confirmed that 35 strains produced amylases, 37 - proteases, 43 - cellulases, 31 - xylanases and 37 - mannanases. The study of the effect of temperature on enzyme activity led to determination of the optimal temperatures of activities that vary between 60 and 100°C. Several enzymes were active at high temperatures (80, 90 and 100°C) and kept their activity even at 110°C. Several isolated strains producing enzymes with high optimal temperatures of activity were described for the first time in this study. Both strains B62 and B120 are producers of amylase, protease, cellulase, xylanase, and mannanase. The sequencing of 16S DNA identified isolated strains as Geobacillus kaustophillus, Aeribacillus pallidus, Geobacillus galactosidasus and Geobacillus toebii.
    Źródło:
    Acta Biochimica Polonica; 2016, 63, 3; 581-587
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Core structure of flavonoids precursor as an antihyperglycemic and antihyperlipidemic agent: an in vivo study in rats
    Autorzy:
    Najafian, Mahmoud
    Ebrahim-Habibi, Azadeh
    Yaghmaei, Parichehreh
    Parivar, Kazem
    Larijani, Bagher
    Powiązania:
    https://bibliotekanauki.pl/articles/1040323.pdf
    Data publikacji:
    2010
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    diabetes
    hyperglycemia
    trans-chalcone
    hyperlipidemia
    benzylideneacetophenone
    alpha-amylase inhibitor
    Opis:
    trans-Chalcone is the core structure of naringenin chalcone, located halfway in the biosynthesis pathway of flavonoids. Flavonoids have been reported as mammalian alpha-amylase inhibitors, a property which could be useful in the management of postprandial hyperglycemia in diabetes and related disorders. As a mammalian alpha-amylase inhibitor in vitro, the putative beneficial effect of trans-chalcone on diabetes was tested in a streptozotocin-induced rat model of diabetes type 1, and the results analyzed with commonly used statistical methods. Significant reduction of blood glucose levels and beneficial effect on dyslipidemia were observed in diabetic rats, as well as reduction of disturbing consequences of diabetes such as high urine volume and water intake. trans-chalcone was observed to have a weight loss-inductive effect, alongside with a reduction in food intake, which is suggestive of a therapeutic potential of this compound in overweight and obese patients.
    Źródło:
    Acta Biochimica Polonica; 2010, 57, 4; 553-560
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Purification and characterization of α-amylases from the intestine and muscle of Ascaris suum (Nematoda).
    Autorzy:
    Żółtowska, Krystyna
    Powiązania:
    https://bibliotekanauki.pl/articles/1044107.pdf
    Data publikacji:
    2001
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    Ascaris suum
    α-amylase
    starch digestion
    glycogen metabolism
    nematode
    Opis:
    α-Amylase (EC 3.2.1.1) was purified from the muscle and intestine of the parasitic helminth of pigs Ascaris suum. The enzymes from the two sources differed in their properties. Isoelectric focusing revealed one form of α-amylase from muscles with pI of 5.0, and two forms of amylase from intestine with pI of 4.7 and 4.5. SDS/PAGE suggested a molecular mass of 83 kDa and 73 kDa for isoenzymes of α-amylases from intestine and 59 kDa for the muscle enzyme. α-Amylase from intestine showed maximum activity at pH 7.4, and the enzyme from muscle at pH 8.2. The muscle enzyme was more thermostabile than the intestinal α-amylase. Both the muscle and intestine amylase lost half of its activity after 15 min at 70°C and 50°C, respectively. The Km values were: for muscle amylase 0.22 μg/ml glycogen and 3.33 μg/ml starch, and for intestine amylase 1.77 μg/ml glycogen and 0.48 μg/ml starch. Both amylases were activated by Ca2+ and inhibited by EDTA, iodoacetic acid, p-chloromercuribenzoate and the inhibitor of α-amylase from wheat. No significant differences were found between the properties of α-amylases from parasites and from their hosts.
    Źródło:
    Acta Biochimica Polonica; 2001, 48, 3; 763-774
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    In vitro α-glucosidase and α-amylase enzyme inhibitory effects of Andrographis paniculata extract and andrographolide
    Autorzy:
    Subramanian, Rammohan
    Asmawi, M
    Sadikun, Amirin
    Powiązania:
    https://bibliotekanauki.pl/articles/1040761.pdf
    Data publikacji:
    2008
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    α-glucosidase
    α-amylase
    Andrographis paniculata
    andrographolide
    peak blood glucose
    post prandial hyperglycaemia.
    Opis:
    There has been an enormous interest in the development of alternative medicines for type 2 diabetes, specifically screening for phytochemicals with the ability to delay or prevent glucose absorption. The goal of the present study was to provide in vitro evidence for potential inhibition of α-glucosidase and α-amylase enzymes, followed by a confirmatory in vivo study on rats to generate a stronger biochemical rationale for further studies on the ethanolic extract of Andrographis paniculata and andrographolide. The extract showed appreciable α-glucosidase inhibitory effect in a concentration-dependent manner (IC50=17.2±0.15 mg/ml) and a weak α-amylase inhibitory activity (IC50=50.9±0.17 mg/ml). Andrographolide demonstrated a similar (IC50=11.0±0.28 mg/ml) α-glucosidase and α-amylase inhibitory activity (IC50=11.3±0.29 mg/ml). The positive in vitro enzyme inhibition tests paved way for confirmatory in vivo studies. The in vivo studies demonstrated that A. paniculata extract significantly (P<0.05) reduced peak blood glucose and area under curve in diabetic rats when challenged with oral administration of starch and sucrose. Further, andrographolide also caused a significant (P<0.05) reduction in peak blood glucose and area under the curve in diabetic rats. Hence α-glucosidase inhibition may possibly be one of the mechanisms for the A. paniculata extract to exert antidiabetic activity and indicates that AP extract can be considered as a potential candidate for the management of type 2 diabetes mellitus.
    Źródło:
    Acta Biochimica Polonica; 2008, 55, 2; 391-398
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
      Wyświetlanie 1-5 z 5

      Ta witryna wykorzystuje pliki cookies do przechowywania informacji na Twoim komputerze. Pliki cookies stosujemy w celu świadczenia usług na najwyższym poziomie, w tym w sposób dostosowany do indywidualnych potrzeb. Korzystanie z witryny bez zmiany ustawień dotyczących cookies oznacza, że będą one zamieszczane w Twoim komputerze. W każdym momencie możesz dokonać zmiany ustawień dotyczących cookies