doi: 10.1016/0076-6879(91)00132-g.
Assay of phosphorylation of small substrates and of synthetic random polymers that interact chemically with adenosine 5'-triphosphate
- PMID: 1956314
- DOI: 10.1016/0076-6879(91)00132-g
Item in Clipboard
Assay of phosphorylation of small substrates and of synthetic random polymers that interact chemically with adenosine 5'-triphosphate
Methods Enzymol.
1991.
No abstract available
Similar articles
-
Assay of protein kinases using peptides with basic residues for phosphocellulose binding.Methods Enzymol. 1991;200:115-20. doi: 10.1016/0076-6879(91)00133-h. Methods Enzymol. 1991. PMID: 1956315 No abstract available.
-
Use of synthetic amino acid polymers for assay of protein-tyrosine and protein-serine kinases.Methods Enzymol. 1991;200:107-11. doi: 10.1016/0076-6879(91)00131-f. Methods Enzymol. 1991. PMID: 1835510 No abstract available.
-
Use of synthetic peptides mimicking phosphorylation sites for affinity purification of protein-serine kinases.Methods Enzymol. 1991;200:169-78. doi: 10.1016/0076-6879(91)00137-l. Methods Enzymol. 1991. PMID: 1659651 No abstract available.
-
Design and use of peptide substrates for protein kinases.Methods Enzymol. 1991;200:121-34. doi: 10.1016/0076-6879(91)00134-i. Methods Enzymol. 1991. PMID: 1835511 Review. No abstract available.
-
Micro- and macropurification methods for protein kinases.Methods Enzymol. 1991;200:159-69. doi: 10.1016/0076-6879(91)00136-k. Methods Enzymol. 1991. PMID: 1956316 Review. No abstract available.
Publication types
MeSH terms
Substances
Grants and funding
LinkOut - more resources
Other Literature Sources