Glycosyl transferases in mouse and human milk fat globule membranes

1984 ◽  
Vol 58 (1-2) ◽  
pp. 157-163 ◽  
Author(s):  
Armando J. Parodi ◽  
Edward W. Blank ◽  
Jerry Peterson ◽  
Roberto Ceriani
Keyword(s):  
Human Milk ◽  
Milk Fat ◽  
Glycosyl Transferases ◽  
Milk Fat Globule ◽  
Fat Globule ◽  
Milk Fat Globule Membranes ◽  
Human Milk Fat

Glycosyl transferases in mouse and human milk fat globule membranes

1984 ◽  
pp. 157-163
Author(s):  
Armando J. Parodi ◽  
Edward W. Blank ◽  
Jerry Peterson ◽  
Roberto Ceriani
Keyword(s):  
Human Milk ◽  
Milk Fat ◽  
Glycosyl Transferases ◽  
Milk Fat Globule ◽  
Fat Globule ◽  
Milk Fat Globule Membranes ◽  
Human Milk Fat

scholarly journals Isolation and characterization of two individual glycoprotein components from human milk-fat-globule membranes

1982 ◽  
Vol 207 (1) ◽  
pp. 37-41 ◽  
Author(s):  
A Imam ◽  
D J Laurence ◽  
A M Neville
Keyword(s):  
Human Milk ◽  
Milk Fat ◽  
Sodium Dodecyl ◽  
Membrane Glycoproteins ◽  
Lectin Affinity Chromatography ◽  
Isolation And Characterization ◽  
Milk Fat Globule ◽  
Fat Globule ◽  
Milk Fat Globule Membranes ◽  
Human Milk Fat

Two individual glycoprotein components from human milk-fat-globule membranes (MFGM) has been purified by selectively extracting the membrane glycoproteins followed by lectin affinity chromatography and gel filtration on Sephadex G-200 in the presence of protein-disaggregating agents. The purified glycoprotein components, termed ‘epithelial-membrane glycoprotein’ (EMGP-155 and EMGP-39) have estimated molecular weights of 155 000 and 39 000 respectively, and yield a single band under reducing conditions on sodium dodecyl sulphate/polyacrylamide gel. EMGP-155 and EMGP-39 contain 21.0% and 7.0% carbohydrate by weight, with fucose (13.5%, 12.4%), mannose (3.7%, 6.2%), galactose (28.5%, 22.6%), N-acetylglucosamine (17.8%, 7.4%) and sialic acid (36.4%, 51.4%) of the carbohydrate moiety respectively. For both the glycoprotein components, aspartic and glutamic acid and serine are the major amino acid residues.

Reactions of Monoclonal Antibodies against Human Milk Fat Globule Membranes with Embryonal Tissue

1984 ◽  
pp. 1021-1024 ◽  
Author(s):  
U. KOLDOVSKY ◽  
U. WARGALLA ◽  
J. HILKENS ◽  
J. TAYLOR-PAPADIMITRIOU ◽  
PH. HAGEMANN ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Human Milk ◽  
Milk Fat ◽  
Milk Fat Globule ◽  
Fat Globule ◽  
Milk Fat Globule Membranes ◽  
Human Milk Fat

scholarly journals Isolation and chemical and immunochemical characterization of the peanut-lectin-binding glycoprotein from human milk-fat-globule membranes

1984 ◽  
Vol 224 (2) ◽  
pp. 581-589 ◽  
Author(s):  
J Fischer ◽  
P J Klein ◽  
G H Farrar ◽  
F G Hanisch ◽  
G Uhlenbruck
Keyword(s):  
Human Milk ◽  
Binding Sites ◽  
Milk Fat ◽  
Lectin Binding ◽  
Functional Characterization ◽  
Milk Fat Globule ◽  
Fat Globule ◽  
Milk Fat Globule Membranes ◽  
Human Milk Fat

Membrane glycoprotein with high Mr (HMr-MGP) was purified from neuraminidase-treated Triton X-100-solubilized human milk-fat-globule membranes by peanut-agglutinin (PNA) affinity chromatography. The high carbohydrate content (75%), blood-group-A activity and typical monosaccharide composition (L-fucose, D-galactose, N-acetyl-D-glucosamine and N-acetyl-D-galactosamine in the proportions 0.26:1.00:1.85:1.30) indicate that the isolated HMr-MGP is a mucinous substance. Fractionation of the oligosaccharides from alkaline-borohydride-treated HMr-MGP on Bio-Gel P-2 suggest that the PNA-binding sites are located mainly on longer (tetra- to deca-saccharide) alkali-labile bound oligosaccharide chains. Polyclonal antibodies raised against the HMr-MGP showed an antigenic distribution in histological sections that was comparable with the distribution of peroxidase-labelled-PNA-binding sites in both normal and malignant breast tissues. The positive immunohistological staining of some other tissue components with this antibody indicates that HMr-MGP is not strictly breast-associated. The functional role of HMr-MGP is unknown, but, since its expression is dependent on the differentiation state of secretory epithelial cells, it serves as a differentiation antigen that can be used for better functional characterization of breast cancers.

Structure of the human milk fat globule

2013 ◽  
Vol 25 (10) ◽  
pp. 223-226 ◽  
Author(s):  
Cyrielle Garcia ◽  
Sheila Innis
Keyword(s):  
Human Milk ◽  
Milk Fat ◽  
Milk Fat Globule ◽  
Fat Globule ◽  
Human Milk Fat

Radiation doses obtained from 99mTc-labelled human milk fat globule monoclonal antibodies

1993 ◽  
Vol 20 (2) ◽  
pp. 145-148
Author(s):  
M.M. Calitz ◽  
A. Van Aswegen ◽  
M.M.J. Van Der Merwe ◽  
M.G. Lötter
Keyword(s):  
Monoclonal Antibodies ◽  
Human Milk ◽  
Milk Fat ◽  
Radiation Doses ◽  
Milk Fat Globule ◽  
Fat Globule ◽  
Human Milk Fat

scholarly journals A novel FADS2 isoform identified in human milk fat globule suppresses FADS2 mediated Δ6-desaturation of omega-3 fatty acids

2018 ◽  
Vol 138 ◽  
pp. 52-59 ◽  
Author(s):  
Kumar S.D. Kothapalli ◽  
Hui Gyu Park ◽  
Xiaoxian Guo ◽  
Xuepeng Sun ◽  
James Zou ◽  
...  
Keyword(s):  
Fatty Acids ◽  
Human Milk ◽  
Milk Fat ◽  
Omega 3 Fatty Acids ◽  
Omega 3 ◽  
Milk Fat Globule ◽  
Fat Globule ◽  
Human Milk Fat
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