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• W2000515925 abstract "The eosinophil cationic protein (ECP), a potent helminthotoxin with considerable neurotoxic activity, was recently shown to also have ribonucleolytic activity. In this work the substrate preference of ECP ribonuclease action was studied in detail. With single-stranded RNA or synthetic polyribonucleotide substrates ECP showed significant but low activity, 70- to 200-fold less than that of bovine RNase A. ECP hydrolyzed RNA more rapidly than it did any synthetic polynucleotide. Poly(U) was degraded more rapidly than poly(C), and poly(A) and double-stranded substrates were extremely resistant. Defined low molecular weight substrates in the form of the 16 dinucleoside phosphates (NpN') and uridine and cytidine 2',3'-cyclic phosphates were tested, and none showed hydrolysis by ECP at a significant rate. The results link ECP ribonucleolytic activity to the 'non-secretory' liver-type enzymes rather than to the 'secretory' pancreatic-type RNases." @default.
• W2000515925 created "2016-06-24" @default.
• W2000515925 creator A5028520897 @default.
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• W2000515925 date "1991-08-19" @default.
• W2000515925 modified "2023-09-26" @default.
• W2000515925 title "Ribonuclease activity and substrate preference of human eosinophil cationic protein (ECP)" @default.
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• W2000515925 doi "https://doi.org/10.1016/0014-5793(91)80994-e" @default.
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