Front cover: N -glycosylation proteomic characterization and cross-species comparison of milk fat globule membrane proteins from mammals

PROTEOMICS ◽  
2016 ◽  
Vol 16 (21) ◽  
pp. NA-NA
Author(s):  
Yongxin Yang ◽  
Nan Zheng ◽  
Weiyu Wang ◽  
Xiaowei Zhao ◽  
Yangdong Zhang ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Milk Fat ◽  
Species Comparison ◽  
Milk Fat Globule Membrane ◽  
Front Cover ◽  
Milk Fat Globule ◽  
Fat Globule ◽  
Cross Species Comparison

N-glycosylation proteomic characterization and cross-species comparison of milk fat globule membrane proteins from mammals

PROTEOMICS ◽  
2016 ◽  
Vol 16 (21) ◽  
pp. 2792-2800 ◽  
Author(s):  
Yongxin Yang ◽  
Nan Zheng ◽  
Weiyu Wang ◽  
Xiaowei Zhao ◽  
Yangdong Zhang ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Milk Fat ◽  
Species Comparison ◽  
Milk Fat Globule Membrane ◽  
Milk Fat Globule ◽  
Fat Globule ◽  
Cross Species Comparison

Chemical changes in bovine milk fat globule membrane caused by heat treatment and homogenization of whole milk

2002 ◽  
Vol 69 (4) ◽  
pp. 555-567 ◽  
Author(s):  
SUNG JE LEE ◽  
JOHN W. SHERBON
Keyword(s):  
Heat Treatment ◽  
Membrane Proteins ◽  
Milk Fat ◽  
Whey Proteins ◽  
Bovine Milk ◽  
Chemical Changes ◽  
Milk Fat Globule Membrane ◽  
Whole Milk ◽  
Milk Fat Globule ◽  
Fat Globule

The effects of heat treatment and homogenization of whole milk on chemical changes in the milk fat globule membrane (MFGM) were investigated. Heating at 80 °C for 3–18 min caused an incorporation of whey proteins, especially β-lactoglobulin (β-lg), into MFGM, thus increasing the protein content of the membrane and decreasing the lipid. SDS-PAGE showed that membrane glycoproteins, such as PAS-6 and PAS-7, had disappeared or were weakly stained in the gel due to heating of the milk. Heating also decreased free sulphydryl (SH) groups in the MFGM and increased disulphide (SS) groups, suggesting that incorporation of β-lg might be due to association with membrane proteins via disulphide bonds. In contrast, homogenization caused an adsorption of caseins to the MFGM but no binding of whey proteins to the MFGM without heating. Binding of caseins and whey proteins and loss of membrane proteins were not significantly different between milk samples that were homogenized before and after heating. Viscosity of whole milk was increased when milk was treated with both homogenization and heating.

Compositional and electrophoretic changes in buffalo milk-fat globule membrane proteins during lactation

1976 ◽  
Vol 43 (3) ◽  
pp. 381-388 ◽  
Author(s):  
Sukhminder Singh ◽  
N. C. Ganguli
Keyword(s):  
Membrane Proteins ◽  
Isoelectric Focusing ◽  
Gel Electrophoresis ◽  
Milk Fat ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Polyacrylamide Gel ◽  
Milk Fat Globule Membrane ◽  
Milk Fat Globule ◽  
Fat Globule

SummaryChemical analyses, polyacrylamide-gel electrophoresis and isoelectric focusing of milk-fat globule membrane proteins (FGMP) obtained from the milk of 2 Murrah buffaloes were done to determine if any change in composition occurred during lactation. Changes in the levels of sialic acid, hexose, hexosamine, N and P were found in the FGMP obtained at different stages of lactation. On the day of parturition, 8 major proteins in FGMP were determined by sodium dodecyl sulphate polyacrylamide-gel electrophoresis whereas 6 major proteins were obtained in FGMP of middle and late lactation milks. Isoelectric focusing of FGMP showed 8–9, 9–13 and 13–16 proteins from colostrum, middle and late lactation milks, respectively and the isoelectric pH of the proteins varied from 5·25 to 7·80, 5·85 to 8·30 and 5·75 to 8·61 respectively.

Identification of the milk fat globule membrane proteins

1976 ◽  
Vol 448 (4) ◽  
pp. 589-598 ◽  
Author(s):  
Jay J. Basch ◽  
Harold M. Farrell ◽  
Rae Greenberg
Keyword(s):  
Membrane Proteins ◽  
Milk Fat ◽  
Milk Fat Globule Membrane ◽  
Milk Fat Globule ◽  
Fat Globule
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