Schuessler H, Schilling K
Int J Radiat Biol Relat Stud Phys Chem Med. 1984 Mar;45(3):267-81. doi: 10.1080/09553008414550381.
Radiolysis of bovine serum albumin under aerobic and anaerobic conditions was studied by SDS-polyacrylamide gel electrophoresis. After Coomassie Blue or Fast Green staining quantitative evaluations give information about the degradation processes of the protein. Under nitrogen the main reaction is the aggregation caused by covalent cross-links, which includes only a small portion of intermolecular S-S bridges. Under air the radiolysis leads to peptide chain scission, which is not a random process, but yields specific protein fragments. A mechanism for this fragmentation reaction is suggested. The radiation-induced broadening of the serum albumin peak is interpreted as being a result of intramolecular disulfide exchange. In contrast to lactate dehydrogenase the degradation of serum albumin is enhanced by oxygen, probably because of its low tryptophan content.
通过十二烷基硫酸钠-聚丙烯酰胺凝胶电泳研究了有氧和无氧条件下牛血清白蛋白的辐射分解。经考马斯亮蓝或固绿染色后，定量评估可提供有关蛋白质降解过程的信息。在氮气氛围下，主要反应是由共价交联引起的聚集，其中仅包含一小部分分子间的S-S桥。在空气中，辐射分解导致肽链断裂，这不是一个随机过程，而是产生特定的蛋白质片段。提出了这种断裂反应的机制。血清白蛋白峰的辐射诱导展宽被解释为分子内二硫键交换的结果。与乳酸脱氢酶不同，血清白蛋白的降解因氧气而增强，这可能是由于其色氨酸含量较低。
