Identification of Collagen-Binding Proteins in Lactobacillus spp. with Surface-Enhanced Laser Desorption/Ionization–Time of Flight ProteinChip Technology
Autor: | Gregor Reid, Jeffrey C. Howard, Bradley J. Thatcher, Bing Siang Gan, Brian Martin, Christine Heinemann |
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Rok vydání: | 2000 |
Předmět: |
Integrins
Lactobacillus casei Receptors Collagen Lactobacillus fermentum Mass spectrometry Applied Microbiology and Biotechnology Peptide Library Lactobacillus Methods Peptide library Chromatography Ecology biology Chemistry food and beverages biology.organism_classification Surface-enhanced laser desorption/ionization Lacticaseibacillus casei Matrix-assisted laser desorption/ionization Biochemistry Spectrometry Mass Matrix-Assisted Laser Desorption-Ionization Collagen Carrier Proteins Bacteria Food Science Biotechnology |
Zdroj: | Applied and Environmental Microbiology. 66:4396-4400 |
ISSN: | 1098-5336 0099-2240 |
DOI: | 10.1128/aem.66.10.4396-4400.2000 |
Popis: | 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. |
Databáze: | OpenAIRE |
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