Effect of the Ph in the Conformation and Activity of the Acid Protease From Aspergillus saitoi

Salvador   R.   Tello-sois

doi:10.2174/0929866013409599

Abstract

The circular dichroism spectrum in the far UV-region (190-240 nm) indicates that the acid protease from Aspergillus saitoi contains appreciable amounts of beta-sheet. The structure-activity relationship of the protein is studied as a function of the pH.

Keywords: acid protease, aspergillus saitoi, pepsin, gastricsin, cathepsins d e, renin, pepsinlilke acid proteases

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Protein & Peptide Letters

Title: Effect of the Ph in the Conformation and Activity of the Acid Protease From Aspergillus saitoi

Volume: 8 Issue: 2

Author(s): Salvador R. Tello-sois

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Keywords: acid protease, aspergillus saitoi, pepsin, gastricsin, cathepsins d e, renin, pepsinlilke acid proteases

Abstract: The circular dichroism spectrum in the far UV-region (190-240 nm) indicates that the acid protease from Aspergillus saitoi contains appreciable amounts of beta-sheet. The structure-activity relationship of the protein is studied as a function of the pH.

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Tello-sois R. Salvador, Effect of the Ph in the Conformation and Activity of the Acid Protease From Aspergillus saitoi, Protein & Peptide Letters 2001; 8 (2) . https://dx.doi.org/10.2174/0929866013409599