Protein methylase II was purified from human placenta approx. 8700-fold with a yield of 14%. 2. Unlike protein methylase II from other sources, the activity of human placenta enzyme was completely inhibited by 2 mM Cu2+. Other divalent ions were without effect. 3. Human chorionic gonadotropin (HCG), immunoglobulin A and calf thymus histones served as good in vitro substrates for the enzyme, particularly HCG. 4. The Km for S-adenosyl-L-methionine and Ki for S-adenosyl-L-homocysteine were 2.08 x 10(-6) and 5.8 x 10(-7) M, respectively. 5. The protein methylase II activity in human placenta changed with gestational age, the activity at 1st and 2nd trimester being approximately twice that of term placenta.
摘要
从人胎盘中纯化出蛋白甲基化酶II,纯化倍数约为8700倍,产率为14%。2. 与其他来源的蛋白甲基化酶II不同,人胎盘酶的活性可被2 mM Cu2+完全抑制。其他二价离子则无此作用。3. 人绒毛膜促性腺激素(HCG)、免疫球蛋白A和小牛胸腺组蛋白是该酶良好的体外底物,尤其是HCG。4. S-腺苷-L-甲硫氨酸的Km值和S-腺苷-L-高半胱氨酸的Ki值分别为2.08×10(-6)和5.8×10(-7) M。5. 人胎盘中蛋白甲基化酶II的活性随胎龄而变化,孕早期和中期的活性约为足月胎盘的两倍。