Literature DB >> 728467

Maturation dependent decline of adenylate cyclase in rabbit red blood cell membranes.

J P Piau, S Fischer, J G Delaunay, M Tortolero, G Schapira.   

Abstract

Adenylate cyclase (EC 4.6.1.1) was studied in membrane preparations of reticulocyte-rich blood obtained from phenylhydrazine-treated rabbits and compared to that of untreated animals. Basal and fluoride-stimulated activities were decreased 2- and 4-fold, respectively, during the process of maturation. Catalytic parameters such as time course, protein, ATP, Mg2+ concentration curves and Km have been determined and were found to be similar in the reticulocyte and the erythrocyte. Adenylate cyclase was sensitive to GTP, 5'-guanylyl imidodiphosphate, prostaglandin E1 and prostaglandin E2. Activation by prostaglandin E1 was higher than that produced by prostaglandin E2. Only additive effect was found when 5'-guanylyl imidodiphosphate or GTP was added to hormone-stimulated activity. The sensitivity of the enzyme to these effectors was decreased over the transition reticulocyte-erythrocyte. In either cell the enzyme was not activated by catecholamines (epinephrine, norepinephrine, isoproterenol).

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Year:  1978        PMID: 728467     DOI: 10.1016/0304-4165(78)90322-7

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  2 in total

1.  Lipid peroxidation in rabbit reticulocytes.

Authors:  Y Kobayashi; T Usui
Journal:  Experientia       Date:  1984-04-15

2.  Superoxide dismutase activity in rabbit reticulocytes.

Authors:  Y Kobayashi; Y Yoshimitsu; S Okahata; T Usui
Journal:  Experientia       Date:  1983-01-15
  2 in total

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