Porcine pancreatic alpha amylase and its isoforms--effect of deglycosylation by peptide-N-glycosidase F
| Autor: | Sridevi Annapurna Singh, G. Muralikrishna, B. Anitha Gopal |
|---|---|
| Rok vydání: | 2008 |
| Předmět: |
PNGase F
Spectrometry Mass Electrospray Ionization Sus scrofa Peptide Biochemistry Structural Biology Animals Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase Glycoside hydrolase Molecular Biology Pancreas chemistry.chemical_classification biology Tryptophan Temperature General Medicine respiratory system Carbohydrate Fluorescence Isoenzymes chemistry biology.protein Electrophoresis Polyacrylamide Gel Spectrophotometry Ultraviolet alpha-Amylases Glycoprotein Alpha-amylase |
| Zdroj: | International journal of biological macromolecules. 43(2) |
| ISSN: | 0141-8130 |
| Popis: | Porcine pancreatic α-amylase (PPA) and its isoforms (PPA-I and PPA-II) were deglycosylated by peptide- N -glycosidase F (PNGase F) to investigate the role of bound carbohydrate. On deglycosylation, the effect on thermal stability was less pronounced. Deglycosylation resulted in a shift of the mid-point of thermal transition by 1–2 °C towards lower temperature. The fluorescence emission maxima of PPA, PPA-I and PPA-II were found to be 340 nm indicating the presence of tryptophan residues in a fairly hydrophilic environment. A red shift in emission spectra accompanied by an increase in fluorescence intensity was observed upon deglycosylation. |
| Databáze: | OpenAIRE |
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