Site-directed mutagenesis study of the role of histidine residues in the neutral-to-basic transition of human serum albumin
| Autor: | Nadhipuram V. Bhagavan, Chung-Eun Ha, Jinsheng Yang |
|---|---|
| Rok vydání: | 2005 |
| Předmět: |
Biophysics
Biochemistry Pichia law.invention Pichia pastoris law medicine Humans Histidine Protein Structure Quaternary Site-directed mutagenesis Molecular Biology Serum Albumin biology Chemistry Mutagenesis Wild type Hydrogen-Ion Concentration Human serum albumin biology.organism_classification Recombinant Proteins Yeast Mutation Mutagenesis Site-Directed Recombinant DNA medicine.drug |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - General Subjects. 1724:37-48 |
| ISSN: | 0304-4165 |
| DOI: | 10.1016/j.bbagen.2005.03.020 |
| Popis: | Site-directed mutagenesis was used to study the role of histidine residues located in domain I in the neutral-to-basic (N-B) transition of human serum albumin (HSA). Based on a previous study of the N-B transition by means of proton NMR, the following recombinant HSA species were synthesized in the yeast species, Pichia pastoris: H9F, H9S, H39F, H39S, H67F, H67S, H105F, H105S, H128F, H128S, H146F, H146S, and wild type HSA. By monitoring the fluorescent intensity of warfarin bound to the above recombinant human serum albumin species as a function of pH, the mutational effect of individual histidine residues on the N-B transition was examined. While H9, H67, H105, H128 and H146 contribute to the transition significantly, H39 appears to have virtually no contribution to the transition. Based on the X-ray crystallographic structure, it is suggested that electrostatic interactions are the principal factor in determining the histidine pK shifts. |
| Databáze: | OpenAIRE |
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