Milk Proteins

1. Front Matter

   Pages I-XI

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2. Introductory Remarks

   1. Research Funding by the EEC

      • J. Gay

      Pages 1-4

   2. The Industry’s Interest in Protein Research

      • A. Nienhaus

      Pages 5-6

3. Milk Protein and Nitrogen Equilibrium

   1. How to Evaluate Dietary Protein

      • V. R. Young, P. L. Pellett

      Pages 7-36

   2. Milk Proteins and Tissue Nitrogen Equilibrium

      • P. J. Reeds

      Pages 37-48

   3. The Endocrine Response to Dietary Protein: the Anabolic Drive on Growth

      • D. J. Millward

      Pages 49-61

   4. Endocrine Response to Animal and Vegetable Protein

      • C. A. Barth, K. E. Scholz-Ahrens, M. Pfeuffer, M. de Vrese

      Pages 62-67

   5. Reliability and Limitations of the Homoarginine Method for Evaluation of Protein Digestibility in the Pig

      • H. Hagemeister, M. Schmitz, H. Erbersdobler

      Pages 68-71

   6. Lactoferrin Content in Feces in Ileostomy-operated Children Fed Human Milk

      • L. Hambraeus, G. Hjorth, B. Kristiansson, H. Hedlund, H. Andersson, B. Lönnerdal et al.

      Pages 72-75

   7. Specificity of the Intestinal Lactoferrin Receptor

      • L. A. Davidson, B. Lönnerdal

      Pages 76-82

   8. The Effects of Quantity and Type of Dietary Protein on the Rehabilitation after a Period of Energetic Undernourishment

      • H. de Waard, P. L. M. Reyven

      Pages 83-83

4. Milk Proteins and Ligands

   1. Milk Proteins and Metabolic Requirements of Trace Elements, Minerals, and Vitamins

      • B. Lönnerdal

      Pages 87-96

   2. Manganese Absorption from Human Milk, Cow Milk, and Infant Formulas

      • L. Davidsson, Å. Cederblad, B. Lönnerdal, B. Sandström

      Pages 97-99

   3. Intrinsic Labelling of Iron in Milk

      • J. Gislason, B. Jones, B. Lönnerdal, L. Hambraeus

      Pages 100-102

   4. Does Bovine Lactoferrin Resist Absorption in the Small Intestine of Neonatal and Adult Pigs?

      • M. Schmitz, H. Hagemeister, Iris Görtler, J. G. Bindels, C. A. Barth

      Pages 103-104

   5. Can Lactoferrin Supplementation Improve the Availability of Iron from Milk?

      • G. Schulz-Lell, H.-D. Oldigs, K. Dörner, J. Schaub

      Pages 105-107

   6. The Nutritive Value of Bovine Lactoferrin

      • I. Schoppe, C. A. Barth, H. Hagemeister

      Pages 108-109

5. Milk Proteins: Structural and Genetic Aspects

   1. Structure and Variability of Milk Proteins

      • B. Ribadeau-Dumas

      Pages 112-123

   2. Modification of Milk by Gene Transfer

      • J. Paul Simons

      Pages 124-132

   3. Analysis of Protein Structure in Solution by Two-Dimensional NMR Spectroscopy: 2D-1H NMR Investigation of Ribonuclease T1 and Its Complexes with 2′- and 3′-Guanosine Monophosphates

      • H. Rüterjans, E. Hoffmann, J. Schmidt, J. Simon

      Pages 133-142

This book reviews the state of knowledge and progress of research on food proteins, and in particular, milk proteins. Its basis is the Symposium on Milk Proteins that was held at the Federal Dairy Research Centre in Kiel, FRG, in June, 1988. Scien­ tists from around the world attended and addressed pure, as well as applied fields of protein research and technology. This book is divided into five sections, each adapted from the symposium's invited lectures, short communications, and poster presentations. New criteria for the "bio­ logical value" of dietary proteins and their relationships are considered according to: - Milk Proteins and Nitrogen Equilibrium - Milk Proteins and Ligands - Milk Proteins: Structural and Genetic Aspects - Milk Proteins: Technological and Functional Aspects - Milk Proteins and Clinical Nutrition Generally, different dietary proteins are classified according to their "biological value," i.e., their capacity to cause different retention of nitrogen in the body. But we think there are other intriguing leads worth studying that may help to identify which dietary proteins are best recommended for specific dietary situations or clini­ cal conditions. In addition, we have taken into consideration new fields such as attempts to determine the three-dimensional structure of proteins using two-dimensional NMR spectroscopy, and the application of genetic engineering to the lactating cell. In other words, we are on the way to the transgenic cow with customized milk constituents and composition.

• Alanin
• Lipid
• NMR
• biological
• cell
• fields
• food
• genetic engineering
• metabolism
• nitrogen
• nuclear magnetic resonance (NMR)
• nutrition
• protein
• proteins
• receptor

• Institut für Physiologie und Biochemie der Ernährung, Bundesanstalt für Milchforschung, Kiel 1, Germany

  C. A. Barth

• Institut für Chemie und Physik, Bundesanstalt für Milchforschung, Kiel 1, Germany

  E. Schlimme

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