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    Wyświetlanie 1-4 z 4
    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:
    DIAGNOSTIC POTENTIAL OF SELECTED SALIVARY PROTEOMICS FOR AUTONOMIC NERVOUS SYSTEM ACTIVITY ASSESSMENT
    Autorzy:
    Dobrek, Lukasz
    Powiązania:
    https://bibliotekanauki.pl/articles/2137800.pdf
    Data publikacji:
    2020-05-14
    Wydawca:
    Fundacja Edukacji Medycznej, Promocji Zdrowia, Sztuki i Kultury Ars Medica
    Tematy:
    saliva
    vasoactive intestinal peptide
    neuropeptide Y
    chromogranin A
    α-amylase
    Opis:
    The clinical assessment of autonomic nervous system (ANS) functioning, enabling the diagnosis of autonomic neuropathy present in the course of many diseases, is currently based on performing simple cardiovascular reflexes (Ewing tests), analyzing heart rate variability (HRV) or heart rate turbulence (HRT), examining skin sweating or recording neurophysiological tests (e.g. microneurography). Laboratory assessment of ANS function is very scarce and practically only includes the plasma assessment of noradrenaline as a surrogate for the biochemical indicator of sympathetic activity. Recently, the possibility of evaluation of selected compounds present in saliva as laboratory markers of not only oral diseases but also systemic diseases has been raised. This work focuses on a brief description of the anatomy and physiology of the salivary glands and describes the formation of saliva, its composition and the use of this bodily fluid in laboratory diagnostics. In addition, the paper specifically discusses the possibility of determining selected compounds that are considered to reflect autonomic activity. A review of the literature indicates primarily four proteomics: two neuropeptides (vasoactive intestinal peptide (VIP) and neuropeptide Y (NPY) that are co-transmitters in autonomic fibers, chromogranin A, a synaptic vesicle protein and α-amylase, a hydrolytic enzyme pre-digesting carbohydrates in the oral cavity. These are currently the most widely investigated agents for their usefulness as laboratory markers of ANS activity.
    Źródło:
    Acta Neuropsychologica; 2020, 18(2); 285-303
    1730-7503
    2084-4298
    Pojawia się w:
    Acta Neuropsychologica
    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 1-4 z 4

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