本文用紫外光谱研究了等离子点附近HSA或BSA (?)Cu(Ⅱ)或Ni(Ⅱ)金属中心的结构。结果表明:在pH4.0～5.3时,Cu(Ⅱ)—HSA配合物在低浓度时独具五配位的四方锥构型,高浓度时(>10~(-4)mol·1~(-1))为四配位的四方平面构型,Cu(Ⅱ)—BSA、Ni(Ⅱ)—BSA在上述pH范围内均只存在四方平面构型。Cu(Ⅱ)、Ni(Ⅱ)结合位置与生理pH下的相同,均在白蛋白的N端三肽段上,与Asp~1的α-NH_2、His~3的咪唑基N及两个去质子肽氮配位,Cu(Ⅱ)在HSA中的第五结合基团为Asp~1的羧基。本文还对上述pH效应进行了讨论。 In this paper, the structure of HSA or BSA (?) Cu (II) or Ni (II) metal near the plasma has been studied by UV spectroscopy. The results showed that the Cu (Ⅱ) -HSA complex has a unique pentagonal tetragonuclear conformation at low concentration (pH4.0 ~ 5.3) -1)) was tetragonal. The Cu (Ⅱ) -BSA and Ni (Ⅱ) -BSA only existed in the tetragonal plane in the above pH range. The binding sites of Cu (Ⅱ) and Ni (Ⅱ) are the same as those at physiological pH. They are all located on the N-terminal tripeptide of albumin, which interacts with α-NH_2 of Asp ~ 1, imidazole N of His ~ 3, Proton peptide nitrogen coordination, Cu (Ⅱ) in HSA in the fifth binding group is Asp ~ 1 carboxyl. This article also discussed the pH effect.