Interaction of Mercury with Human and Bovine Milk Proteins

スポンサーリンク

概要

• 論文の詳細を見る

• The interaction of inorganic mercury with human and bovine milk proteins was studied. Gel filtration chromatography of skimmed milk and whey incubated with mercury showed that, in human milk, mercury was mainly bound to caseins, while a low proportion was bound to albumin. In bovine milk, mercury was associated with two protein fractions, caseins and β-lactoglobulin. Furthermore, it was shown by electrophoresis that mercury induced the formation of dimers of β-lactoglobulin. Thus, in both human and bovine milk, mercury prossessed greater ability to interact with milk proteins than to the low-molecular-weight substances. However, the pattern of mercury distribution was different between the milk of these two species.

• 社団法人日本農芸化学会の論文
• 1997-10-23

著者

• Calvo Miguel

  Food Technology And Biochemistry Department Faculty Of Veterinary Science University Of Zaragoza

• Mata Luis

  Food Technology And Biochemistry Department Faculty Of Veterinary Science University Of Zaragoza

• SANCHEZ Lourdes

  Food Technology and Biochemistry Department, Faculty of Veterinary Science, University of Zaragoza

• Sanchez Lourdes

  Dep. Of Animal Production And Food Sci. Food Technol. Unit Veterinary Fac. Univ. Of Zaragoza

関連論文

• Interaction of Mercury with Human and Bovine Milk Proteins
• Transport of Iron Bound to Recombinant Human Lactoferrin from Rice and Iron Citrate Across Caco-2 Cell Monolayers
• Antibacterial Activity of Recombinant Human Lactoferrin from Rice : Effect of Heat Treatment
• Effects of Hydrostatic High Pressure on the Structure and Antibacterial Activity of Recombinant Human Lactoferrin from Transgenic Rice

スポンサーリンク