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Publication Details
AFRICAN RESEARCH NEXUS
SHINING A SPOTLIGHT ON AFRICAN RESEARCH
biochemistry, genetics and molecular biology
Purification, immunological and biochemical characterization of an Ap4A binding protein from Xenopus laevis oocytes
Nucleic Acids Research, Volume 16, No. 7, Year 1988
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Description
Diadenosine 5′,5″′-P1, P4-tetraphosphate (Ap4A) binding protein specifically binds Ap4A. The protein has been purified from Xenopus laevis oocytes and presents and estimated molecular weight of 100,000 by gek filtration. In the first stages of the purification, the Ap4A binding activity is found associated to DNA polymerase alpha-DNA primase, forming heterogeneous high molecular weight complexes.A monoclonal antibody has been prepared against the purified Ap4A binding protein. The antibody partially neutralizes the Ap4A binding activity. Using the immunoblot technique, it has been shown that the antibody is able to recognize either native or SDS-denaturated Ap4A binding protein. The monoclonal antibody immoreacted with a polypeptide of 90,000 which coincides with the molecular weight obtained by get chromatography and indicates that the native Ap4A binding protein from Xenopus oocytes is probably a monomeric protein. © 1988 IRL Press Limited.
Authors & Co-Authors
Zourgui, Lazhar
France, Bordeaux
Institut de Biochimie et Génétique Cellulaires
Baltz, Théo
France, Bordeaux
Institut de Biochimie et Génétique Cellulaires
France, Bordeaux
Université de Bordeaux
Statistics
Citations: 8
Authors: 2
Affiliations: 2
Identifiers
Doi:
10.1093/nar/16.7.2913
ISSN:
03051048
Research Areas
Genetics And Genomics