Human serum and milk albumins are metal-dependent DNases.

It is known that that human serum albumin (HSA) and alpha-lactalbumin (LA) possess DNA-binding sites. Electrophoretically homogeneous HSA and LA containing no canonical enzymes were isolated from human sera and milk. Here we have analyzed for the first time the possibility of DNA hydrolysis by these proteins. It was shown that HSA possesses metal-dependent DNase activity, while LA cannot hydrolyze DNA. Several rigid criteria have been applied to show that DNase activity is an intrinsic property of HSA from human sera and milk. HSA preparations were inactive after their dialysis against EDTA or in the presence of EDTA, but were activated after addition of several external metal ions: Mn  > Mg  > Ca . The best activation of HSA preparations was observed in the presence of two metal ions: Mg +Ca  > Mn  + Ca  ≥ Mn  + Mg . In contrast to DNases having only one pH optimum, HSA preparations demonstrated two well-pronounced optima at pH 5.7-5.9 and 6.9-7.1 as well as a weak optimum at pH 8.4-8.6. These results demonstrate the diversity of HSA in the DNA hydrolysis at various pHs and in activation by various metal cofactors. Possible reasons for the diversity of HSA preparations are discussed. © 2018 IUBMB Life, 70(6):501-510, 2018.