Abstract
The primary structure of the neuronal Type II calmodulin-dependent protein kinase has been examined by protein sequence analysis and compared to cDNA-derived sequence . Tandem mass spectroscopic analysis was used for the sequence determination. Comparison with published cDNA sequence data for the alpha subunit revealed that the difference between the alpha- and beta-subunits lay in two insertions into the sequence for the alpha-subunit and a short alpha-specific sequence. The N-terminal amino acid of the alpha subunit which is blocked to Edman degradation has been tentatively identified as N-acetyl-alanine.
| Original language | English |
|---|---|
| Pages (from-to) | 1104-1109 |
| Number of pages | 6 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 148 |
| Issue number | 3 |
| DOIs | |
| State | Published - Nov 13 1987 |
Bibliographical note
Funding Information:The authors would like to thank Brad MacDonald and Julie Giles of Wellcome Research Laboratories for cytoskeletal preparation and alpha-subunit purification. Special thanks is due to Drs. Carol A. Ohmstede and Naji Sahyoun (Wellcome) for fruitful discussions. We are also indebted to Dr. Dave Brent (Wellcome) for suggesting and facilitating the mass spectrometry collaborative effort. Instrument developmental funds awarded to D.F.H. from the Monsanto Co. and from the NSF (CHE-8319728) are gratefully acknowledged.
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Molecular Biology
- Cell Biology