Published January 16, 1984
| Version v1
Journal article
Mutual stimulation by phosphatidylinositol-4-phosphate and myelin basic protein of their phosphorylation by the kinases solubilized from rat brain myelin
Creators
- 1. New York State Inst. for Basic Research in Developmental Disabilities, Staten Island
Description
Myelin basic protein and phosphatidylinositol-4-phosphate are phosphorylated in vitro by ATP and solubilized rat brain myelin. When both substrates are present together, the rate of phosphorylation of each is increased about eight-fold. It appears likely that the phosphate turnover of myelin basic protein and of phosphatidylinositol-4-phosphate are coupled in vivo
Additional details
Publishing Information
- Journal Title
- Life Sci.
- Journal Volume
- 34
- Journal Issue
- 3
- Series
- Life Sci.
- Journal Page Range
- 259-264
- ISSN
- 0024-3205
INIS
- Country of Publication
- United States
- Country of Input or Organization
- United States
- INIS RN
- 16030587
- Subject category
- S60: APPLIED LIFE SCIENCES; S62: RADIOLOGY AND NUCLEAR MEDICINE;
- Descriptors DEI
- ATP; BIOCHEMISTRY; BRAIN; IN VITRO; MYELIN; PHOSPHOLIPIDS; PHOSPHORUS 32; PHOSPHORYLATION; PHOSPHOTRANSFERASES; RADIOASSAY; RATS
- Descriptors DEC
- ANIMALS; BETA DECAY RADIOISOTOPES; BETA-MINUS DECAY RADIOISOTOPES; BODY; CENTRAL NERVOUS SYSTEM; CHEMICAL REACTIONS; CHEMISTRY; DAYS LIVING RADIOISOTOPES; ENZYMES; ESTERS; ISOTOPES; LIGHT NUCLEI; LIPIDS; LIPOPROTEINS; MAMMALS; NERVOUS SYSTEM; NUCLEI; NUCLEOTIDES; ODD-ODD NUCLEI; ORGANIC COMPOUNDS; ORGANIC PHOSPHORUS COMPOUNDS; ORGANS; PHOSPHORUS ISOTOPES; PROTEINS; RADIOISOTOPES; RODENTS; TRANSFERASES; VERTEBRATES