Purification and Characterization of Novel Whey Glycoprotein WGP-88 Which Binds to a Monoclonal Antibody to PAS-4 Glycoprotein in the Bovine Milk Fat Globule Membrane

1997 ◽  
Vol 61 (9) ◽  
pp. 1568-1574 ◽  
Author(s):  
Sik Hwangbo ◽  
Norihiro Azuma ◽  
Jun-ichi Kurisaki ◽  
Choemon Kanno
Keyword(s):  
Monoclonal Antibody ◽  
Milk Fat ◽  
Bovine Milk ◽  
Purification And Characterization ◽  
Milk Fat Globule Membrane ◽  
Milk Fat Globule ◽  
Fat Globule

Production and characterization of monoclonal antibodies directed against bovine milk fat globule membrane (MFGM)

1994 ◽  
Vol 1199 (1) ◽  
pp. 87-95 ◽  
Author(s):  
Naohito Aoki ◽  
Hidenori Kuroda ◽  
Miho Urabe ◽  
Yoshimi Taniguchi ◽  
Takahiro Adachi ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Milk Fat ◽  
Bovine Milk ◽  
Milk Fat Globule Membrane ◽  
Milk Fat Globule ◽  
Fat Globule

scholarly journals Isolation and structural characterization of alkali-labile oligosaccharides from bovine milk-fat-globule membrane

1978 ◽  
Vol 171 (3) ◽  
pp. 549-557 ◽  
Author(s):  
G H Farrar ◽  
R Harrison
Keyword(s):  
Mass Spectrometry ◽  
Structural Characterization ◽  
Milk Fat ◽  
Bovine Milk ◽  
Periodate Oxidation ◽  
Methylation Analysis ◽  
Milk Fat Globule Membrane ◽  
Milk Fat Globule ◽  
Fat Globule

Treatment of sialoglycopeptides derived from bovine milk-fat-globule membrane with alkaline borohydride released a reduced oligosaccharide fraction from which a tetrasaccharide and two trisaccharides were isolated. Periodate-oxidation studies coupled with methylation analysis and g.l.c.-mass spectrometry established their structures as: N-acetylneuraminyl-(2 leads to 3)-beta-D-galactopyranosyl-(1 leads to 3)-[N-acetylneuraminyl-(2 leads to 6)]-N-acetyl-D-galactosaminitol, N-acetylneuraminyl-(2 leads to 3)-D-glactopyranosyl-(1 leads to 3)-N-acetyl-D-galactosaminitol and beta-D-galactopyranosyl-(1 leads to 3)-[N-acteylneuraminyl-(2 leads to 6)]-N-acetyl-D-galactosaminitol respectively.

scholarly journals Preparation of monoclonal antibodies to xanthine oxidase and other proteins of bovine milk-fat-globule membrane

1980 ◽  
Vol 188 (3) ◽  
pp. 925-928 ◽  
Author(s):  
I H Mather ◽  
C S Nace ◽  
V G Johnson ◽  
R A Goldsby
Keyword(s):  
Monoclonal Antibody ◽  
Monoclonal Antibodies ◽  
Xanthine Oxidase ◽  
Cell Lines ◽  
Milk Fat ◽  
Bovine Milk ◽  
Serial Transfer ◽  
Milk Fat Globule Membrane ◽  
Milk Fat Globule ◽  
Fat Globule

Nine hybridomas secreting monoclonal antibody to proteins of bovine milk-fat-globule membrane were isolated. All nine cell lines continued to secrete monoclonal antibody after serial transfer in culture and after passage as solid tumours in Balb/cJ mice. Four of the cell lines secreted monoclonal antibody specific for xanthine oxidase, one of the major proteins of milk-fat-globule membrane.

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.

scholarly journals Safety and Tolerance Evaluation of Milk Fat Globule Membrane-Enriched Infant Formulas: A Randomized Controlled Multicenter Non-Inferiority Trial in Healthy Term Infants

2014 ◽  
Vol 8 ◽  
pp. CMPed.S16962 ◽  
Author(s):  
Claude Billeaud ◽  
Giuseppe Puccio ◽  
Elie Saliba ◽  
Bernard Guillois ◽  
Carole Vaysse ◽  
...  
Keyword(s):  
Weight Gain ◽  
Milk Fat ◽  
Bovine Milk ◽  
Control Group ◽  
Infant Formulas ◽  
Term Infants ◽  
Milk Fat Globule Membrane ◽  
Standard Formula ◽  
Milk Fat Globule ◽  
Fat Globule

Objective This multicenter non-inferiority study evaluated the safety of infant formulas enriched with bovine milk fat globule membrane (MFGM) fractions. Methods Healthy, full-term infants ( n = 119) age ≤14 days were randomized to standard infant formula (control), standard formula enriched with a lipid-rich MFGM fraction (MFGM-L), or standard formula enriched with a protein-rich MFGM fraction (MFGM-P). Primary outcome was mean weight gain per day from enrollment to age 4 months (non-inferiority margin: –3.0 g/day). Secondary (length, head circumference, tolerability, morbidity, adverse events) and exploratory (phospholipids, metabolic markers, immune markers) outcomes were also evaluated. Results Weight gain was non-inferior in the MFGM-L and MFGM-P groups compared with the control group. Among secondary and exploratory outcomes, few between-group differences were observed. Formula tolerance rates were high (>94%) in all groups. Adverse event and morbidity rates were similar across groups except for a higher rate of eczema in the MFGM-P group (13.9% vs control [3.5%], MFGM-L [1.4%]). Conclusion Both MFGM-enriched formulas met the primary safety endpoint of non-inferiority in weight gain and were generally well tolerated, although a higher rate of eczema was observed in the MFGM-P group.

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