Structural proteome of human colostral fat globule membrane proteins
Autor: | Maria Cavaletto, Alessandra Coscia, Claudio Fabris, Lorenza Perono Garoffo, Lorenzo Napolitano, Maria Gabriella Giuffrida, Carlo Giunta, Enrico Bertino, Amedeo Conti, Donatella Fortunato, Giuseppina Dellavalle |
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Rok vydání: | 2003 |
Předmět: |
Internet
Spectrometry Mass Electrospray Ionization Milk Human Proteome Edman degradation Chemistry Membrane Proteins Apical membrane Milk Proteins Mass spectrometry Biochemistry Membrane protein Spectrometry Mass Matrix-Assisted Laser Desorption-Ionization Humans Colostrum Female Globules of fat Time-of-flight mass spectrometry Databases Protein Molecular Biology Software |
Zdroj: | PROTEOMICS. 3:897-905 |
ISSN: | 1615-9861 1615-9853 |
DOI: | 10.1002/pmic.200300367 |
Popis: | Milk fat globule membrane (MFGM) contains proteins derived from the apical membrane of secreting epithelial cells of the mammary gland. Between 2-4% of total human milk protein content is associated with the fat globule fraction, as MFGM proteins. While MFGM proteins have very low classical nutritional value, they play important roles in various cell processes and defence mechanisms for the newborn. To date, fewer than 30 human MFGM proteins have been identified and characterized, either by immunological methods or by Edman sequencing and mass spectrometry. This study aimed to update the structural proteome of human colostral MFGM proteins and to create an annotated two-dimensional electrophoresis (2-DE) MFGM protein database available on-line. More than one hundred 2-DE spots derived from human colostral MFGM proteins were investigated by matrix-assisted laser desorption/ionization-time of flight mass spectrometry and proteins were identified by three different software packages available on the web (PeptIdent, MS-Fit and ProFound); uncertain identifications were solved by nanoelectrospray ionization-ion trap mass spectrometry using SEQUEST software. |
Databáze: | OpenAIRE |
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