The primary structure of a low-Mr multiphosphorylated variant ofβ-casein in equine milk

PROTEOMICS ◽  
2007 ◽  
Vol 7 (8) ◽  
pp. 1327-1335 ◽  
Author(s):  
Laurent Miclo ◽  
Jean-Michel Girardet ◽  
Antonio S. Egito ◽  
Daniel Mollé ◽  
Patrice Martin ◽  
...  
2001 ◽  
Vol 68 (1) ◽  
pp. 53-61 ◽  
Author(s):  
STEFANIA IAMETTI ◽  
GABRIELLA TEDESCHI ◽  
EMANUELA OUNGRE ◽  
FRANCESCO BONOMI

In this work the purification and the complete primary structure of κ-casein from equine milk are reported for the first time. Mares' milk casein was separated by RP-HPLC into four fractions. Complete primary sequence was obtained by sequence analysis of the protein in the fastest eluting peak isolated by chromatography. This sequence was 95% identical to that reported for the C-terminal portion of the zebras' κ-casein and showed high similarity with κ-caseins from sources other than Equidae, confirming that this protein was indeed κ-casein in equine milk. The presence of post-translational modifications in equine κ-casein was investigated by mass spectroscopy, after enzymic dephosphorylation. Two main components were found, the smaller component being more abundant. Equine κ-casein was recognized by a lectin specific for one of the glucosidic bonds in the saccharide moiety of bovine κ-casein. Sequence comparison with prevision studies showed that the distribution of charged and hydrophobic regions in equine κ-casein was similar, but not identical, to that found in the bovine protein; these regions are associated with the role of κ-casein in the formation and stabilization of the micellar structure of casein in milk.


1985 ◽  
Vol 260 (4) ◽  
pp. 2301-2306
Author(s):  
H Pande ◽  
J Calaycay ◽  
D Hawke ◽  
C M Ben-Avram ◽  
J E Shively

1991 ◽  
Vol 266 (29) ◽  
pp. 19480-19483 ◽  
Author(s):  
K. Takahashi ◽  
H. Inoue ◽  
K. Sakai ◽  
T. Kohama ◽  
S. Kitahara ◽  
...  

1972 ◽  
Vol 247 (23) ◽  
pp. 7612-7621 ◽  
Author(s):  
C. Richard Savage ◽  
Tadashi Inagami ◽  
Stanley Cohen

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