Flamigni F, Guarnieri C, Marmiroli S, Caldarera C M
Biochem J. 1985 Aug 1;229(3):807-10. doi: 10.1042/bj2290807.
Purified and partially purified ornithine decarboxylase (ODC) from rat heart was inhibited by basic polypeptides in vitro. Poly-L-arginine, the most effective, was inhibitory at a concentration as low as 0.1 microgram/ml; protamine and histone clearly inhibited ODC at concentrations higher than 2 micrograms/ml, but poly-L-lysine was less effective. The ability to inhibit ODC appeared to correlate with the arginine-residue content of basic polypeptides. The inhibition effect could be decreased by increasing substrate concentration and ionic strength.
从大鼠心脏中纯化和部分纯化的鸟氨酸脱羧酶(ODC)在体外受到碱性多肽的抑制。最有效的聚-L-精氨酸在低至0.1微克/毫升的浓度下就具有抑制作用;鱼精蛋白和组蛋白在浓度高于2微克/毫升时能明显抑制ODC,但聚-L-赖氨酸的效果较差。抑制ODC的能力似乎与碱性多肽的精氨酸残基含量相关。增加底物浓度和离子强度可降低抑制作用。