New genetic variants identified in donkey's milk whey proteins

Novel genetic variants for donkey milk lysozyme and beta-lactoglobulins I and II have been identified by the combined use of peptide mass mapping and sequencing by tandem mass spectrometry in association with database searching. The novel donkey lysozyme variant designated as lysozyme B (Mr 14,631 D...

Full description

Saved in:
Bibliographic Details
Published in:Journal of Protein Chemistry 2000-02, Vol.19 (2), p.105-116
Main Authors: Herrouin, M, Mollé, D, Fauquant, J, Ballestra, F, Maubois, J L, Léonil, J
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Amino acids
Animals
Chromatography, High Pressure Liquid
Chymotrypsin - metabolism
Cysteine - chemistry
Database searching
Electrophoresis, Polyacrylamide Gel
Gene mapping
Genetic diversity
Genetic variance
Genetic Variation
Lactoglobulin
Lactoglobulins - chemistry
Lactoglobulins - genetics
Life Sciences
Lysozyme
Mammals
Mass spectrometry
Mass spectroscopy
Milk
Milk - chemistry
Molecular Sequence Data
Muramidase - chemistry
Muramidase - genetics
Peptide mapping
Peptides
Perissodactyla
Population genetics
Proteins
Sequence Analysis, Protein
Sequence Homology, Amino Acid
Spectrometry, Mass, Electrospray Ionization
Trypsin - metabolism
Whey protein
β-Lactoglobulin
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Novel genetic variants for donkey milk lysozyme and beta-lactoglobulins I and II have been identified by the combined use of peptide mass mapping and sequencing by tandem mass spectrometry in association with database searching. The novel donkey lysozyme variant designated as lysozyme B (Mr 14,631 Da) differed in three amino acid exchanges, N49 --> D, Y52 --> S, and S61 --> N, from the previously published sequence. Three novel genetic variants for donkey beta-lactoglobulins were identified. One of them is a type beta-lactoglobulin I with three amino acid exchanges at E36 --> S, S97 --> T, and V150 --> I (beta-lactoglobulin I B, Mr 18,510 Da). The two others are type beta-lactoglobulins II with two amino acid exchanges at C110 --> P and M118--> T (beta-lactoglobulin II B, Mr 18,227 Da) and with three amino acid exchanges at D96 --> E, C110 --> P, and M118 -->T (beta-lactoglobulin II C, Mr 18,241 Da). All these primary structures are closely related to those of homologous proteins in horse milk (percent identity >96%).
ISSN:0277-8033
1572-3887
1573-4943
DOI:10.1023/A:1007078415595