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Characterization of an alkaline subtilopeptidase type Pfizer
International Journal of Peptide and Protein Research
|January 1, 1976
Summary
This study characterizes alkaline subtilopeptidase from Pfizer, detailing its stability, amino acid profile, and molecular weight. The enzyme exhibits optimal activity at high pH and moderate temperatures, with a specific amino acid composition and structure.
Area of Science:
- Enzymology
- Protein Chemistry
- Biochemistry
Background:
- Alkaline subtilopeptidase is a versatile enzyme with industrial applications.
- Understanding its physiochemical properties is crucial for optimizing its use.
Purpose of the Study:
- To determine the physiochemical properties of alkaline subtilopeptidase type Pfizer.
- To analyze its amino acid composition and the profile of its tryptic peptides.
Main Methods:
- Electrophoretic techniques for homogeneity and isoelectric point determination.
- Gel filtration for molecular weight estimation.
- Amino acid analysis and tryptic peptide mapping using Dowex 50-X2 chromatography.
Main Results:
- The enzyme is stable between pH 5-10, with an optimum pH of 9.5-10.
- It shows stability up to 50°C for 2 hours, with a molecular weight of 25,000 Da.
- The amino acid composition revealed 247 residues, lacking disulfide bonds, cysteine, and tryptophan. Alanine is the N-terminal and arginine is the C-terminal residue.
- Tryptic hydrolysis yielded 15 peptides with established compositions.
Conclusions:
- Alkaline subtilopeptidase type Pfizer possesses distinct physiochemical and structural characteristics.
- Its stability profile suggests suitability for applications in alkaline environments and moderate temperatures.
- Detailed peptide mapping provides a foundation for further structural and functional investigations.