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Glycogen phosphorylase molecular weight

Fig. 33. Experimentally observed molecular-weight dependence of (S2)z for amylose chains grafted onto glycogen (filled circles) and partially debranched amylopectin (open circles). Grafting was achieved by potato phosphorylase (15 rays for glycogen and 12000 per amylopectin molecule), and by muscle phosphorylase (400 rays per glycogen molecule)142,143)... Fig. 33. Experimentally observed molecular-weight dependence of (S2)z for amylose chains grafted onto glycogen (filled circles) and partially debranched amylopectin (open circles). Grafting was achieved by potato phosphorylase (15 rays for glycogen and 12000 per amylopectin molecule), and by muscle phosphorylase (400 rays per glycogen molecule)142,143)...
Thus, it is possible to distinguish relatively small groups of atoms. For example, in glycogen phosphorylase b [149] (molecular weight, 97 (XX)), the binding of a single phosphate ion can be detected at 3 A resolution. [Pg.380]

The problem of crystal reactivity and diffusion limitations has been considered in detail by Makinen and Fink [170]. They provide a simple treatment for crystals approximated as a plane sheet of material which leads to the definition of a limiting crystal thickness below which kinetic measurements of second-order rate constants are not affected by rate-limiting diffusion processes. For papain [172], ribonuclease A [173] and deoxyhaemoglobin [174], where the crystal thicknesses are comparable to the critical crystal thickness, reactivities are the same in the crystal and solution. In the case of glycogen phosphorylase b Kasvinsky and Madsen [175] demonstrated that the values for both substrates, glucose 1-phosphate (37 + 8mM) and malto-heptaose (176 + 20 mM), were the same in the crystal and solution. The 10-100-fold reduction in rate, despite the fact that crystal thickness was only twice the critical thickness, may be attributable partly to the allosteric nature of this enzyme and partly to the fact that the large substrate maltoheptaose (molecular weight, 1152) may not obey the simple diffusion rules in the crystal. [Pg.387]

Methods of assay (m) = methylation (p) = periodate oxidation (e) = enzymic. B.V. = Blue Value (compare Refs. 3 and 4). Xmax = wavelength of maximum absorption of polysaccharide-iodine complex. Priming activity toward P-enzyme soluble starch = 1.0. Priming activity toward muscle phosphorylase glycogen = 100, corn amylopectin = 63. Molecular weight, 64,000 (compared with about 100,000 for the parent amylose). [Pg.386]


See other pages where Glycogen phosphorylase molecular weight is mentioned: [Pg.193]    [Pg.727]    [Pg.192]    [Pg.83]    [Pg.191]    [Pg.351]    [Pg.1423]    [Pg.259]    [Pg.406]    [Pg.422]    [Pg.711]    [Pg.177]    [Pg.138]    [Pg.2870]    [Pg.157]    [Pg.233]    [Pg.288]    [Pg.289]    [Pg.259]    [Pg.585]    [Pg.588]   
See also in sourсe #XX -- [ Pg.91 ]




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