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Interaction amongst calcineurin subunits
Author(s) -
Gupta Ramesh C.,
Khandelwal Ramji L.,
Sulakhe Prakash V.
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)80210-1
Subject(s) - protein subunit , phosphatase , calmodulin , calcineurin , enzyme , chemistry , urea , biochemistry , gamma aminobutyric acid receptor subunit alpha 1 , microbiology and biotechnology , interleukin 10 receptor, alpha subunit , biology , g alpha subunit , medicine , transplantation , gene
Calcineurin was dissociated into subunits A and B by 6 M urea in the presence (method A) and absence (method B) of MnCI 2 and dissociated subunits were isolated by gel filtration in urea in the absence (method B) or presence (method A) of MnCI 2 . Phosphatase activity was associated with the A subunit isolated by either method. The phosphatase activity ( ) of subunit A isolated by method A was greater (2‐5‐fold) than by method B. Mn 2+ increased subunit A phosphatase and calmodulin further increased the enzyme activity. Subunit B isolated by method A or B increased Mn 2+ + calmodulin stimulated subunit A phosphatase prepared by method B but interestingly and unexpectedly inhibited such stimulated activity of the subunit A prepared by method A. These results imply the tightly bound cation (in our case, most likely Mn 2+ ) with subunit A dramatically and differentially influences the effects of two Ca 2+ ‐binding proteins, calmodulin and subunit B, on the subunit A phosphatase.