- 作者: Krishna Harohalli, Charles E. Petersen, Chung-Eun Ha, Jimmy B. Feix, Nadhipuram V. Bhagavan
- 作者服務機構: Department of Biochemistry and Biophysics, John A . Burns School of Medicine, University of Hawaii, Honolulu, Hawaii, Biophysics Research Institute, Medical College of Wisconsin, Milwaukee, Wisc., USA
- 中文摘要: --
- 英文摘要: petition between these two residues for reaction withN 0 , the reactive nitrosating species formed in aqueousacidified NO solutions.The patterns of nitric oxide (NO) release from nitrosatedbovine serum albumin (BSA), human serum albumin(HSA) and a number of recombinant HSA mutants werecompared.All albumin species were nitrosated by incu-bation with acidified NO . The pattern of NO release fromBSA nitrosated with acidified NO was in agreement withprevious reports which indicated that Cys-34 is the pri-mary target for nitrosation in BSA. In contrast, the pat-tern of NO release from HSA nitrosated with acidifiedNO indicated that the primary nitrosation target was anamino acid residue other than Cys-34. Based on our ini-tial findings and a previous report that tryptophan is apotential target for nitrosation by acidified NO , severalrecombinant HSA mutants were synthesized in the yeastspecies Pichia pastoris. The following recombinant HSAspecies were produced: wild-type, C34S, W214L, W214Eand W214L/Y411W HSA. Nitrosation of these mutantsusing acidified NO showed that Trp-214 is the primarynitrosation target in HSA. Mutation of Trp-214 led to anincrease in Cys-34 nitrosation, indicating possible com-
- 中文關鍵字: --
- 英文關鍵字: Nitric Oxide, Human seruma, bumin, Site-directed mutagenesis, Cardiovascular disease