English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
Add to Basket
  Local TagsRelease HistoryDetailsSummary

Released
Journal Article

Characterization of 2':3'-cyclic nucleotide 3'-phosphodiesterase: rapid isolation, native enzyme analysis, identification of a serum-soluble activity, and kinetics

MPS-Authors
/persons/resource/persons289504

Clapshaw,  PA
Seifert Group, Friedrich Miescher Laboratory, Max Planck Society;

/persons/resource/persons286540

Müller,  HW
Seifert Group, Friedrich Miescher Laboratory, Max Planck Society;

/persons/resource/persons15822

Seifert,  W
Seifert Group, Friedrich Miescher Laboratory, Max Planck Society;

External Resource
No external resources are shared
Fulltext (restricted access)
There are currently no full texts shared for your IP range.
Fulltext (public)
There are no public fulltexts stored in PuRe
Supplementary Material (public)
There is no public supplementary material available
Citation

Clapshaw, P., Müller, H., & Seifert, W. (1981). Characterization of 2':3'-cyclic nucleotide 3'-phosphodiesterase: rapid isolation, native enzyme analysis, identification of a serum-soluble activity, and kinetics. Journal of Neurochemistry, 36(6), 1996-2003. doi:10.1111/j.1471-4159.1981.tb10825.x.


Cite as: https://hdl.handle.net/21.11116/0000-000D-2E67-D
Abstract
The enzyme 2':3'-cyclic nucleotide 3'-phosphodiesterase (CNPase) was isolated from bovine brain white matter by a rapid (72 h) procedure. The minimum molecular weight (MW) of the enzyme was approximately 52,500 as estimated by sucrose density gradient analysis. When this isolated enzyme was stimulated with bovine serum albumin (BSA), the peak of activity was shifted to approximately 90,000 MW. Prior treatment by trypsin blocked the expression of the higher MW form of CNPase, but not the BSA activation of the enzyme. If the trypsin digestion was allowed to progress, the MW was gradually lowered to a broad peak sedimenting between 20,000 and 50,000 MW. An apparently soluble form of CNPase found in serum is described. Kinetic and MW comparisons between the serum soluble enzyme and CNPase isolated from bovine brain, as well as an analysis of substrate specificity, were made and it was concluded that the two enzymes were identical.