Open AccessCharacterization of an Adenosine Triphosphatase from Myeloblasts Infected with the Avian Myeloblastosis Virus
Author(s) -
BANERJEE Ranajit K.
Publication year - 1979
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1979.tb13085.x
Subject(s) - enzyme , adenosine triphosphatase , biochemistry , trypsin , atpase , activator (genetics) , microbiology and biotechnology , ouabain , molecular mass , chemistry , biology , sodium , gene , organic chemistry
An adenosine triphosphatase (ATPase EC 3.6.1.3) was partially purified from myeloblasts of chicken infected with the avian myeloblastosis virus and some of its molecular, catalytic and immunological properties were compared with that of the ATPase purified from the virus. Both the enzymes possessed almost same electrophoretic mobility, molecular weight, s 20,w value, substrate specificity, metal‐ion requirement, apparent K value and sensitivity to inhibitors and activator. Evidence also indicated immunological identity of the two enzymes. The insensitivity of this enzyme to rutamycin or ouabain and extreme sensitivity to most of the detergents, trypsin and mercurials are the remarkable properties of this enzyme.