A protein tyrosine kinase with an apparent Mr of 60,000 was highly purified from bovine spleen and used to phosphorylate poly(Glu, Tyr) (4:1) on tyrosine residues for the study of phosphotyrosyl protein phosphatases from this tissue. About 70% of the phosphotyrosyl protein phosphatase activity in ex
Protein band 3 phosphotyrosyl phosphatase. purification and characterization
β Scribed by Pierre Boivin; Colette Galand; Olivier Bertrand
- Publisher
- Elsevier Science
- Year
- 1987
- Tongue
- English
- Weight
- 442 KB
- Volume
- 19
- Category
- Article
- ISSN
- 0020-711X
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
PTP-MEG2 is an intracellular protein tyrosine phosphatase with a putative lipid-binding domain at the N-terminus. The present study reports expression, purification, and characterization of the full-length form of the enzyme plus a truncated form containing the catalytic domain alone. Full-length PT
## Abstract Phosphotyrosyl protein phosphatase, purified from the hepatopancreas of __Panaeus japonicus__, is a monomeric enzyme with a relative mass (Mr) of 28,000, as estimated by sizeβexclusion FPLC on a Superose^TM^ 12. It has a hydrophobic domain and can be extracted with the detergent CHAPS.
Low molecular weight acid phosphatase/phosphotyrosyl protein phosphatase is largely expressed in chick brain tissue during development. The enzyme was purified from brain extract prepared from 19-day-old chick embryos and from adult chickens using ammonium sulfate fractionation, gel filtration on Se