01693naa a2200277 a 450000100080000000500110000800800410001902400510006010000230011124501560013426000090029052008790029965000110117865000160118965000160120565000110122165000190123265000180125165000180126965000100128765000100129770000140130770000150132170000140133677300650135021643742024-05-21       1993    bl uuuu     u00u1 u    #d7 ahttps://doi.org/10.1017/S00220299000273452DOI1 aDOLORES PÉREZ, M.  aComparison of the ability to bind lipids of beta-lactoglobulin and serum albumin of milk from ruminant and non-ruminant species.h[electronic resource]  c1993  aThe interaction of sheep, horse, pig, human and guinea-pig whey proteins with fatty acids has been studied. Using gel filtration and autoradiography, it was found that sheep β-lactoglobulin and serum albumin from all species had the ability to bind fatty acids in vitro. Sheep β-lactoglobulin, isolated from milk, had ˜ 0·5 mol fatty acids bound per mol monomer protein, and albumin from sheep, horse and pig contained ˜ 4·5, 2·9 and 4·7 mol fatty acids/mol protein respectively. However, β-lactoglobulin from horse and pig milk had neither fatty acids physiologically bound nor the ability to bind them in vitro. Albumin was the only whey protein detected with bound fatty acids in these species as well as in human and guinea pig. This suggests that the ability of ruminant β-lactoglobulin to bind fatty acids was not shared by the same protein of non-ruminants.  aCattle  aFatty acids  aGuinea pigs  aHorses  aLactoglobulins  aMilk proteins  aSerum albumin  aSheep  aSwine1 aPUYOL, P.1 aENA, J. M.1 aCALVO, C.  tJournal of Dairy Researchgv. 60, n. 1, p. 55-63, Feb. 1993.