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Wyszukujesz frazę "Sillero, Antonio" wg kryterium: Autor

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    Wyświetlanie 1-3 z 3
    Tytuł:
    An easy procedure to transform the ratio of two polynomials of first degree into Michaelis-Menten-type equations. Application to the ordered Uni Bi enzyme mechanism.
    Autorzy:
    Fontes, Rui
    Ribeiro, João
    Sillero, Antonio
    Powiązania:
    https://bibliotekanauki.pl/articles/1044439.pdf
    Data publikacji:
    2000
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    rectangular hyperbolas
    enzyme inhibition
    enzyme equations
    enzyme kinetics
    graphical presentations
    Opis:
    It is not always clear that some equations affected by complicated factors can, actually, be interpreted as a ratio of two polynomials of first degree and so that they can be, in general, represented by rectangular hyperbolas. In this paper we present an easy procedure to rearrange those equations into Michaelis-Menten-type equations and so to make the aspects of these rectangular hyperbolas more clear, particularly for researchers familiar with general biochemistry. As an example, the method is applied to transform the classical rate equation of the Cleland×s Ordered Uni Bi enzyme mechanism.
    Źródło:
    Acta Biochimica Polonica; 2000, 47, 1; 259-268
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Inhibition and activation of enzymes. The effect of a modifier on the reaction rate and on kinetic parameters.
    Autorzy:
    Fontes, Rui
    Ribeiro, João
    Sillero, Antonio
    Powiązania:
    https://bibliotekanauki.pl/articles/1044438.pdf
    Data publikacji:
    2000
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    enzyme inhibition
    enzyme modifier
    rapid equilibrium kinetics
    I50
    enzyme activation
    enzyme kinetics
    graphical presentations
    Opis:
    A combined analysis of enzyme inhibition and activation is presented, based on a rapid equilibrium model assumption in which one molecule of enzyme binds one molecule of substrate (S) and/or one molecule of a modifier X. The modifier acts as activator (essential or non-essential), as inhibitor (total or partial), or has no effect on the reaction rate (v), depending on the values of the equilibrium constants, the rate constants of the limiting velocity steps, and the concentration of substrate ([S]). Different possibilities have been analyzed from an equation written to emphasize that v = Ł([X]) is, in general and at a fixed [S], a hyperbolic function. Formulas for Su (the value of [S], different from zero, at which v is unaffected by the modifier) and vsu (v at that particular [S]) were deduced. In Lineweaver-Burk plots, the straight lines related to different [X] generally cross in a point (P) with coordinates (Su, vsu). In certain cases, point P is located in the first quadrant which implies that X acts as activator, as inhibitor, or has no effect, depending on [S]. Furthermore, we discuss: (1) the apparent Vmax and Km displayed by the enzyme in different situations; (2) the degree of effect (inhibition or activation) observed at different concentrations of substrate and modifier; (3) the concept of Ke, a parameter that depends on the concentration of substrate and helps to evaluate the effect of the modifier: it equals the value of [X] at which the increase or decrease in the reaction rate is half of that achieved at saturating [X]. Equations were deduced for the general case and for particular situations, and used to obtain computer-drawn graphs that are presented and discussed. Formulas for apparent Vmax, Km and Ke have been written in a way making it evident that these parameters can be expressed as pondered means.
    Źródło:
    Acta Biochimica Polonica; 2000, 47, 1; 233-257
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Selective splitting of 3-adenylated dinucleoside polyphosphates by specific enzymes degrading dinucleoside polyphosphates.
    Autorzy:
    Guranowski, Andrzej
    Sillero, Antonio
    Günther Sillero, María
    Powiązania:
    https://bibliotekanauki.pl/articles/1043653.pdf
    Data publikacji:
    2003
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    diadenosine triphosphate
    diadenosine tetraphosphatase
    diadenosine triphosphatase
    3'-adenylated dinucleoside polyphosphates
    diadenosine tetraphosphate
    diguanosine tetraphosphate
    Opis:
    Several 3'-[32P]adenylated dinucleoside polyphosphates (NpnN'p*As) were synthesized by the use of poly(A) polymerase (Sillero MAG et al., 2001, Eur J Biochem.; 268 : 3605-11) and three of them, ApppA[32P]A or ApppAp*A, AppppAp*A and GppppGp*A, were tested as potential substrates of different dinucleoside polyphosphate degrading enzymes. Human (asymmetrical) dinucleoside tetraphosphatase (EC 3.6.1.17) acted almost randomly on both AppppAp*A, yielding approximately equal amounts of pppA + pAp*A and pA + pppAp*A, and GppppGp*, yielding pppG + pGp*A and pG + pppGp*A. Narrow-leafed lupin (Lupinus angustifolius) tetraphosphatase acted preferentially on the dinucleotide unmodified end of both AppppAp*A (yielding 90% of pppA + pAp*A and 10 % of pA + pppAp*A) and GppppGp*A (yielding 89% pppG + pGp*A and 11% of pG + pppGp*A). (Symmetrical) dinucleoside tetraphosphatase (EC 3.6.1.41) from Escherichia coli hydrolyzed AppppAp*A and GppppGp*A producing equal amounts of ppA + ppAp*A and ppG + ppGp*A, respectively, and, to a lesser extent, ApppAp*A producing pA + ppAp*A. Two dinucleoside triphosphatases (EC 3.6.1.29) (the human Fhit protein and the enzyme from yellow lupin (Lupinus luteus)) and dinucleoside tetraphosphate phosphorylase (EC 2.7.7.53) from Saccharomyces cerevisiae did not degrade the three 3'-adenylated dinucleoside polyphosphates tested.
    Źródło:
    Acta Biochimica Polonica; 2003, 50, 1; 123-130
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
      Wyświetlanie 1-3 z 3

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