A proteomic approach to evaluate the butyrophilin gene family expression in human milk fat globule membrane
| Autor: | Lorenzo Napolitano, Giuseppina Dellavalle, Enrico Bertino, Amedeo Conti, Laura Gardano, Carlo Giunta, Maria Cavaletto, Donatella Fortunato, Maria Gabriella Giuffrida, Claudio Fabris |
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| Rok vydání: | 2002 |
| Předmět: |
Proteomics
Globuli di grasso Molecular Sequence Data Biology Biochemistry Mass Spectrometry Fats Butyrophilin Lactation Peptide mass medicine Animals Humans Gene family Electrophoresis Gel Two-Dimensional proteoma Amino Acid Sequence Molecular Biology Milk fat globule Membrane Glycoproteins Butyrophilins Milk Human Cytoplasmic Vesicles Membrane Intracellular Membranes Butirofillina medicine.anatomical_structure Multigene Family Proteome Immunoglobulin superfamily Female Sequence Alignment Latte umano |
| Zdroj: | 2 (2002): 850–856. info:cnr-pdr/source/autori:Cavaletto M.1, Giuffrida M.G.2, Fortunato D.2, Gardano L.3, Dellavalle G.2, Napolitano L.2, Giunta C.3, Bertino E.4, Fabris C.4, Conti A.2/titolo:A proteomic approach to evaluate the butyrophilin gene family expression in human milk fat globule membrane/doi:/rivista:/anno:2002/pagina_da:850/pagina_a:856/intervallo_pagine:850–856/volume:2 |
| Popis: | Milk fat globule membrane (MFGM) contains proteins derived from the apical membrane of secreting epithelial cells of the mammary gland. Between 2 and 4% of tota 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 mechanism 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 2-DE MFGM protein database available on line. More than one hundred 2DE spots derived from human colostral MFGM proteins were investigated by MALDI-TOF 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 nanoESI-ion trap mass spectrometry using Sequest software. |
| Databáze: | OpenAIRE |
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