Literature DB >> 2841890

Stimulation of the ATP, Mg-dependent protein phosphatase by p-nitrophenyl phosphate.

J Goris1, W Merlevede.   

Abstract

The phosphorylase phosphatase activity of the ATP,Mg-dependent protein phosphatase is stimulated by p-nitrophenyl phosphate (pNPP). All the active forms of this type of enzyme show this property, which seems to be unrelated to any pNPP-hydrolyzing activity. The increase in activity is due to an increase in Vm, the Km being unchanged. The possibility that pNPP acts as a deinhibitor is excluded. pNPP acts as a competitive inhibitor on the phosphorylase phosphatase activity of the different polycation-stimulated protein phosphatases. Stimulation by pNPP can be used as a differential criterion in a specific assay of the active forms of the ATP,Mg-dependent phosphatase.

Entities:  

Mesh:

Substances:

Year:  1988        PMID: 2841890     DOI: 10.1016/0003-2697(88)90509-x

Source DB:  PubMed          Journal:  Anal Biochem        ISSN: 0003-2697            Impact factor:   3.365


  3 in total

1.  Human cytomegalovirus carries serine/threonine protein phosphatases PP1 and a host-cell derived PP2A.

Authors:  S Michelson; P Turowski; L Picard; J Goris; M P Landini; A Topilko; B Hemmings; C Bessia; A Garcia; J L Virelizier
Journal:  J Virol       Date:  1996-03       Impact factor: 5.103

2.  Identification of the ATP + Mg-dependent and polycation-stimulated protein phosphatases in the germinal vesicle of the Xenopus oocyte.

Authors:  C Jessus; J Goris; S Staquet; X Cayla; R Ozon; W Merlevede
Journal:  Biochem J       Date:  1989-05-15       Impact factor: 3.857

3.  The association of type 1, type 2A and type 2B phosphatases with the human T lymphocyte plasma membrane.

Authors:  D R Alexander; J M Hexham; M J Crumpton
Journal:  Biochem J       Date:  1988-12-15       Impact factor: 3.857

  3 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.