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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Tsuiki, S. Kikuchi, K. Larner, J. Suzuki, Y. Tamura, S. Lynch, K. R. Fox, J. Yasui, A. |
| Description | Author Affiliation: Tamura S ( Biochemistry Laboratory, Tohoku University, Sendai, Japan.); |
| Abstract | A full-length cDNA encoding rat type 2C (IA) protein phosphatase was isolated from a kidney cDNA library. The cDNA was identified by screening the library with oligonucleotides based on a partial amino acid sequence determined from purified rat liver phosphatase. This clone is 2.35 kilobase pairs long and has a single extended translation reading frame that predicts a 382-amino acid protein of 42,416 daltons. The deduced amino acid sequence contains segments corresponding to three peptides from rat liver type 2C protein phosphatase and two peptides from rabbit skeletal muscle type 2C phosphatase. Rat kidney type 2C protein phosphatase is distantly related to yeast adenylate cyclase but is not related to the catalytic subunits of two other protein phosphatases (types 1 and 2A). |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 6 |
| Volume Number | 86 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 1989-04-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Cloning, Molecular Phosphoprotein Phosphatases Genetics RNA, Messenger Adenylate Cyclase Amino Acid Sequence Animals DNA Deoxyribonuclease EcoRI Kidney Liver Molecular Sequence Data Nucleic Acid Hybridization Oligonucleotide Probes Saccharomyces Cerevisiae Enzymology Sequence Homology, Nucleic Acid Comparative Study Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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