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

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.

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

Nuclear Medicine and Biology ◽

10.1016/0969-8051(93)90106-5 ◽

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

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Immunohistochemical Reaction of Three Monoclonal Antibodies to Human Milk Fat Globule Membrane with Human Normal and Tumoral Tissues

Protides of the Biological Fluids ◽

10.1016/b978-0-08-031739-7.50139-7 ◽

1985 ◽

pp. 553-556 ◽

Cited By ~ 5

Author(s):

J. ABARCA ◽

E. ABOUD-PIRAK ◽

C. OTTE-SLACHMUYLDER ◽

Y-J. SCHNEIDER ◽

A. TROUET

Keyword(s):

Monoclonal Antibodies ◽

Human Milk ◽

Milk Fat ◽

Milk Fat Globule Membrane ◽

Immunohistochemical Reaction ◽

Milk Fat Globule ◽

Fat Globule ◽

Human Milk Fat

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

Biochemical Journal ◽

10.1042/bj2240581 ◽

1984 ◽

Vol 224 (2) ◽

pp. 581-589 ◽

Cited By ~ 13

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.

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