EFFECTS OF NONENZYMATIC GLYCOSYLATION AND FATTY-ACIDS ON TRYPTOPHAN BINDING TO HUMAN SERUM-ALBUMIN
EFFECTS OF NONENZYMATIC GLYCOSYLATION AND FATTY-ACIDS ON TRYPTOPHAN BINDING TO HUMAN SERUM-ALBUMIN
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DOI：
10.1016/0006-2952(92)90717-w
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发表时间：
1992-04-15
影响因子：
5.8
通讯作者：
FELDHOFF, RC
中科院分区：
文献类型：
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作者：
BOHNEY, JP;FELDHOFF, RC
利用透析速率技术检查了结合脂肪酸和非酶糖基化 (NEG) 对色氨酸与人血清白蛋白 (HSA) 结合的影响。每摩尔 HSA 结合 0、1、2、3 或 5 摩尔棕榈酸酯的 HSA 在体外糖基化至超过糖尿病中所见的水平。 NEG 不受脂肪酸抑制，表明 NEG 的主要位点 Lys-525 不是长链脂肪酸与 HSA 结合的主要位点的重要组成部分。结合数据的斯卡查德分析表明，可用色氨酸结合位点数量出现预期的脂肪酸依赖性减少，但表明脂肪酸不影响色氨酸亲和力。结合数据未能显示 NEG 对色氨酸结合的影响。 NEG 对色氨酸结合缺乏抑制表明药物结合位点 II（吲哚/苯二氮卓位点）对 NEG 以及 NEG 可能发生的 HSA 中的任何构象变化具有抵抗力。这些数据表明，糖尿病患者血浆游离色氨酸升高以及由此导致的血清素代谢改变与 NEG 升高无关，并且可能是糖尿病性高脂血症的结果。
The effects of bound fatty acids and nonenzymatic glycosylation (NEG) on tryptophan binding to human serum albumin (HSA) were examined utilizing a rate of dialysis technique. HSA with 0, 1, 2, 3, or 5 mol of palmitate bound per mol of HSA was glycosylated in vitro to a level exceeding that seen in diabetes. NEG was not inhibited by fatty acids, suggesting that Lys-525, the primary site for NEG, is not an essential component of the principal sites for long-chain fatty acid binding to HSA. Scatchard analysis of binding data showed an expected fatty acid dependent decrease in the number of available tryptophan binding sites, but showed that fatty acids did not affect tryptophan affinity. The binding data failed to show an effect of NEG on tryptophan binding. The lack of inhibition of tryptophan binding by NEG suggests that drug-binding Site II, the indole/benzodiazepine site, is resistant to both NEG and to any conformational changes in HSA which may occur with NEG. These data suggest that elevated plasma free tryptophan and the resulting altered serotonin metabolism seen in diabetes are independent of increased NEG and likely result from diabetic hyperlipidemia.