The milk-fat globule membrane

Anderson, M.; Cawston, Tim E.

doi:10.1017/s0022029900015508

Cited by 96 publications

(18 citation statements)

References 146 publications

(232 reference statements)

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“…La distribution de la LPL du lait de chèvre dans la phase aqueuse est encore très mal connue. La proportion de LPL dans les micelles de caséines semble être beaucoup plus faible (8 Des mélanges de laits présentant une forte lipolyse (laits susceptibles thermisés, LST) avec des laits « normaux}) frais (LNF) n'ont toutefois pas permis de mettre en évidence la présence dans les LS d'activateurs éventuels de la lipolyse des LN ( fig. 11).…”

Section: °Localisation De La Lipase Du Laitunclassified

Variations physiologiques des activités lipasiques et de la lipolyse spontanée dans les laits de vache, de chèvre et de femme : revue bibliographique (suite)

Chilliard

1982

Lait

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Section: °Localisation De La Lipase Du Laitunclassified

Variations physiologiques des activités lipasiques et de la lipolyse spontanée dans les laits de vache, de chèvre et de femme : revue bibliographique (suite)

Chilliard

1982

Lait

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“…The membrane surrounding fat droplets in milk has received increasing attention in recent years as a source of antigens derived from the actively secreting epithelial cells of mammary tissue (Ceriani et al, 1980;Freudenstein et al, 1979;Mather et al, 1980; for reviews, see Anderson & Cawston, 1975;Patton & Keenan, 1975). A major reason for this interest is the convenience with which large amounts of apically derived membrane-bound protein can be isolated, purified and characterized.…”

mentioning

confidence: 99%

Detection of xanthine oxidase and immunologically related proteins in fractions from bovine mammary tissue and milk after electrophoresis in polyacrylamide gels containing sodium dodecyl sulphate

Mather¹,

Sullivan²,

Madara³

1982

Biochemical Journal

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A solid-phase immunoassay was used to detect xanthine oxidase in fractions from bovine mammary glands after electrophoresis in polyacrylamide gels containing sodium dodecyl sulphate. Under these conditions the major proportion of xanthine oxidase in either mammary tissue or mild could be recovered as a protein of mol.wt. 150 000. In mammary tissue approx. 80% of the enzyme was in a soluble form and the remainder was accounted for in either 'mitochondrial' or microsomal fractions after tissue homogenization and fractionation. Affinity chromatography of either detergent-solubilized microsomal membranes or postmicrosomal supernatants on immobilized antibody to xanthine oxidase yielded a single protein that cross-reacted with antibody to the enzyme. In milk presumptive degradation products of the enzyme were detected in minor quantities with mol.wts. of 43 000 in the whey fraction and 90 000 in fat-globule membrane. Only the undegraded enzyme was present in the skim-milk membrane fraction. Xanthine oxidase is therefore synthesized and secreted as a protein with a monomeric mol.wt. of 150 000 and is not subjected to extensive proteolytic degradation during the storage of milk in mammary alveoli. The significance of the results is discussed in relation to the overall protein composition of the membranes of milk-fat globules and skim milk.

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“…Variations between values reported for the chemical composition and enzymic activities of the bovine milk-fat globule membrane (MFGM) (Anderson & Cawston, 1975;Patton & Keenan, 1975) result in part from the different methods used in the breed, nutrition, stage of lactation and perhaps other factors. Very little is known concerning the influence of the last 3 factors, especially the influence of stage of lactation (Anderson & Cawston, 1975).…”

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confidence: 99%

“…Very little is known concerning the influence of the last 3 factors, especially the influence of stage of lactation (Anderson & Cawston, 1975). studied the variations in protein, phospholipid and neutral lipid composition of a deoxycholate soluble fraction from MFGM during lactation.…”

mentioning

confidence: 99%

Milk-fat globule membranes: chemical composition and phosphoesterase activities during lactation

Dı́az-Mauriño¹,

Nieto

1977

Journal of Dairy Research

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The morphology, protein and glycoprotein composition, amino-acid analysis, phospholipid and carbohydrate contents and 3 phosphoesterase activities of the milk-fat globule membranes were studied in 4 cows during their whole period of lactation. No differences were found in the morphology and the overall chemical composition. However, glycoprotein composition varied with the cow and, for each cow, with the stage of lactation. The differences were more marked for membranes obtained from colostrum. Acid phosphomonoesterase was practically unchanged during the whole period of lactation, while alkaline phosphomonoesterase and phosphodiesterase increased as lactation proceeded.

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The milk-fat globule membrane

Cited by 96 publications

References 146 publications

Variations physiologiques des activités lipasiques et de la lipolyse spontanée dans les laits de vache, de chèvre et de femme : revue bibliographique (suite)

Variations physiologiques des activités lipasiques et de la lipolyse spontanée dans les laits de vache, de chèvre et de femme : revue bibliographique (suite)

Detection of xanthine oxidase and immunologically related proteins in fractions from bovine mammary tissue and milk after electrophoresis in polyacrylamide gels containing sodium dodecyl sulphate

Milk-fat globule membranes: chemical composition and phosphoesterase activities during lactation

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