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- W2066546178 abstract "Cytosolic protein-tyrosine kinase from porcine spleen (CPTK-40) is strongly activated by poly-L-lysine using bovine serum albumin, ovalbumin, phosphorylase b, calmodulin and H1 histone as substrate proteins. However, this polyamine inhibited the enzyme activities when myelin basic protein, tubulin and H2B histone were used as substrate proteins. These stimulatory and inhibitory effects on CPTK-40 are not specific for polylysine, but polyarginine and polyornithine have similar effects on this phosphorylation reaction. Effect of poly-basic amino acids on CPTK-40 seems to be mainly on the substrate proteins, rather than on the enzyme itself." @default.
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- W2066546178 date "1989-02-01" @default.
- W2066546178 modified "2023-10-17" @default.
- W2066546178 title "Effect of poly-basic amino acids on the phosphorylation of various substrate proteins by cytosolic protein-tyrosine kinase from porcine spleen" @default.
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- W2066546178 doi "https://doi.org/10.1016/0006-291x(89)92827-1" @default.
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