Molecular mass analysis of aggregation of jack bean urease by Static light scattering (SLS) (CAT#: STEM-MB-0575-WXH)

Introduction

Jack bean urease is a metalloenzyme, which catalyzes the hydrolysis of urea to produce ammonia and carbon dioxide. The heavy metal ions are common inhibitors to control the rate of the enzymatic urea hydrolysis, which take the Hg2+ as the representative. Aggregation of jack bean urease (JBU) is involved in many alterations of its biological properties, notably the ureolytic and entomotoxic activities.

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Principle Applications Procedure Materials Notes Related Products

Principle

Static light scattering is a technique in physical chemistry that measures the intensity of the scattered light to obtain the average molecular weight Mw of a macromolecule like a polymer or a protein in solution. Measurement of the scattering intensity at many angles allows calculation of the root mean square radius, also called the radius of gyration Rg. By measuring the scattering intensity for many samples of various concentrations, the second virial coefficient, A2, can be calculated.

Applications

The main applications of static light scattering is molecular mass determination of macromolecules, such as proteins and polymers, as it is possible to measure the molecular mass of proteins without any assumption about their shape.

Procedure

1. Sample preparation
2. Measurement by SLS instrument
3. Data analysis

Materials

• Right-Angle Light Scattering (RALS) Detector
• Low-Angle Light Scattering (LALS) Detector
• Hybrid RALS/LALS Detector
• Multi-Angle Light Scattering (MALS) Detector

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