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Analysis of Trypsin inhibitor (TIP) by Raman Spectroscopy (CAT#: STEM-ST-0020-WXH)

Introduction

Natural trypsin Inhibitors also known as serine protease inhibitors (serpins) are the largest and most diverse family of protease inhibitors. Serpins control the activation and catabolism of proteins by the inhibition of serine proteases in vivo.
There are four natural sources of trypsin inhibitors: bovine pancreas, ovomucoid, soybean, and lima bean. Each inhibitor acts as a competitive substrate analog and binds with its serine protease to form an inactive complex, therefore rendering the protease inactive.




Principle

Raman Spectroscopy is a non-destructive chemical analysis technique which provides detailed information about chemical structure, phase and polymorphy, crystallinity and molecular interactions.
The principle behind Raman spectroscopy is that the monochromatic radiation is passed through the sample such that the radiation may get reflected, absorbed, or scattered. The scattered photons have a different frequency from the incident photon as the vibration and rotational property vary.

Applications

• Analysis of biocompatibility of a material.
• Analysis of nucleic acids.
• Study of interactions between drugs and cells.
• Photodynamic therapy (PDT).
• Analyzing metabolic accumulations of a substance or compounds.
• Diagnosis of disease.
• Analysis of individual cells.
• Cell sorting applications.
• Analyzing the features of biomolecules.
• Study of bone structure.

Procedure

1. Preparation of samples
2. Determine instrument parameters
3. Perform background scan
4. Test the sample
5. Data analysis

Materials

• Raman Spectrometer
• Raman Imaging Microscope
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