Amino acid sequence of a 12‐kDa inhibitor of protein kinase C
Open Access
- 1 November 1990
- journal article
- retracted article
- Published by Wiley in European Journal of Biochemistry
- Vol. 194 (1), 19-23
- https://doi.org/10.1111/j.1432-1033.1990.tb19421.x
Abstract
The complete primary structure of a bovine‐brain‐derived inhibitor of protein kinase C has been established. Fragments of the purified protein were obtained by cleavage with cyanogen bromide, Staphylococcus aureus V8 protease, trypsin and chymotrypsin. Subsequent analysis of the resulting fragments by fast‐atom‐bombardment mass spectrometry and Edman degradation revealed a calculated molecular mass of 11779 Da with the following 107‐amino‐acid sequence: This inhibitor does not share significant primary structural identity with any other known protein.This publication has 17 references indexed in Scilit:
- Protein kinase C inhibition by plant flavonoidsBiochemical Pharmacology, 1989
- Evidence for negative control in protein kinase C substrate specificityInternational Journal of Peptide and Protein Research, 1989
- The molecular heterogeneity of protein kinase C and its implications for cellular regulationNature, 1988
- Protein Kinase C Contains a Pseudosubstrate Prototope in Its Regulatory DomainScience, 1987
- Pharmacology of the isoquinoline sulfonamide protein kinase C inhibitorsTrends in Pharmacological Sciences, 1987
- Properties and distribution of the protein inhibitor (Mr 17,000) of protein kinase CBiochemical Journal, 1987
- Studies and Perspectives of Protein Kinase CScience, 1986
- Regulation of protein kinase C activity by natural inhibitorsBiochemical Society Transactions, 1986
- Inhibition of the Ca2+-and phospholipid-dependent protein kinase by a novel Mr 17,000 Ca2+-binding proteinBiochemical and Biophysical Research Communications, 1985
- Prediction of protein conformationBiochemistry, 1974