Abstract
An unusual phosphatase, which is resistant to treatment by 5% SDS and proteolytic enzymes, was isolated as two types, 1 and 2, from pronase-treated homogenates of Xenopus ovary. The molecular sizes of types 1 and 2 were estimated as about 140 kDa and more than 2 × 104 kDa, respectively, by gel filtration, but as 140 and 130 kDa as a catalytic unit, respectively, by electrophoresis, implying that whereas type 1 might be composed of catalytic unit alone, type 2 is a multicomponent complex consisting of a 130-kDa catalytic unit. Both activities were sensitive to nucleases but resistant to tested proteolytic enzymes. These findings suggest that the unusual phosphatase activity is attributable to a polynucleotide.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callMore From: Biochemical and Biophysical Research Communications
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
