Literature DB >> 3016194

NAD+ glycohydrolase of the plasma membrane prepared from glial and neuronal cells.

T Honma, P Mandel.   

Abstract

NAD+ glycohydrolase (EC 3.2.2.5) activity was detected in the plasma membrane prepared from the primary culture of rat astrocytes. The enzyme has a broad optimum pH range. From the kinetic analysis, a Michaelis constant of 91.2 microM and a maximum velocity of 0.785 mumol/min/mg protein were obtained. ADPribose exhibited a competitive inhibition with respect to NAD. The inhibition by nicotinamide was shown to be of a non-competitive type. ATP and GTP were found to be competitive inhibitors. NAD+ glycohydrolase activity was not detected in the plasma membrane prepared from the primary culture of neuronal cells of chick embryos.

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Year:  1986        PMID: 3016194     DOI: 10.1111/j.1471-4159.1986.tb00706.x

Source DB:  PubMed          Journal:  J Neurochem        ISSN: 0022-3042            Impact factor:   5.372


  1 in total

1.  Arginine-specific mono(ADP-ribosyl)transferase activity on the surface of human polymorphonuclear neutrophil leucocytes.

Authors:  L E Donnelly; N B Rendell; S Murray; J R Allport; G Lo; P Kefalas; G W Taylor; J MacDermot
Journal:  Biochem J       Date:  1996-04-15       Impact factor: 3.857

  1 in total

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