Identification of collagen-binding proteins in Lactobacillus spp by surface-enhanced laser desorption and ionization technology (CAT#: STEM-ST-0367-LJX)

Introduction

Biosurfactants produced by Lactobacillus fermentum RC-14, L. rhamnosus GR-1 and 36, and L. casei Shirota were found to contain proteins that bind to both collagen types III and VI, as determined by surface-enhanced laser desorption/ionization (SELDI)-time of flight mass spectrometry. Both collagen types III and VI immobilized on SELDI preactivated ProteinChip arrays detected several different sizes (2 to 48 kDa) of collagen-binding proteins. Overall, the RC-14-produced biosurfactant contained the greatest number of collagen-binding proteins (RC-14 > GR-1 > 36 > Shirota), including the mature form of a previously cloned 29-kDa collagen-binding protein (referred to in its mature 26-kDa form). Although biosurfactants isolated from L. casei Shirota and L. rhamnosus 36 and GR-1 also contain several collagen-binding proteins, they do not contain the 26-kDa collagen-binding protein. Together, these results demonstrate the utility of the SELDI system as a means of rapidly characterizing clinically important but complex biosurfactant solutions.

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Principle Applications Procedure Materials Notes Related Products

Principle

The surface enhanced laser desorption ionization technique belongs to laser desorption mass spectrometry (LDMS). It is different from ordinary LDMS in that the laser is not directly hit on the sample to desorption, but the sample is suspended in the matrix, the laser is hit on the matrix, the matrix absorbs and transmits the laser energy, so that the sample in the matrix desorption out. After desorption and ionization, the samples were examined in a time-flight mass spectrometer.

Applications

For protein analysis and measurement of molecular weight of complete proteins
For the diagnosis of a variety of diseases, especially cancer

Procedure

1. The surface of the protein chip is treated in a certain chemical or biochemical way (surface enhancement), so that it has the ability to bind specifically to a certain type of protein
2. The serum or protein extract is directly added to the surface of the chip, and the chip is washed after incubation. Specific proteins bind to the chip and are thus separated from the protein mixture
3. The chip then uses a "chip reader" (a kind of SELDI-TOF-MS) to obtain a mass spectrum of the protein bound to the chip
4. The SELDI protein chip system can be used to compare changes in the protein profile of any set of control samples or different disease states to identify biomarkers or disease-related targets

Materials

• Sample Type:
Lactobacillus spp

Notes

When operating, strictly follow the experimental steps.

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