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Alpha -Lactalbumin
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Authors: Permyakov, Eugene A. (Institute for Biological Instrumentation) 
Editors: Vladimir N. Uversky (Indiana University of Medicine)
Book Description:
Small acidic protein á-lactalbumin, one of the major protein components of milk, is one of the most extensively investigated Ca2+-binding proteins, which does not belong to the EF-hand family of calcium-binding proteins. It serves as a model for studies of the mechanisms of protein stability, folding and unfolding. á-Lactalbumin acts as a regulatory subunit of galactosyltransferase in lactose synthase, which catalyzes the synthesis of lactose from UDP-galactose and glucose. It represents a classical example of molten globule state at acidic pH and in its apo-form at elevated temperatures. Three-dimensional structures of several -lactalbumins are determined. The protein possesses a single strong Ca2+-binding site, which binds Mg2+, Mn2+, Na+, and K+ as well, and several distinct Zn2+-binding sites. The binding of cations to the Ca2+-site increases protein stability against action of heat, various denaturing agents and proteases, while the binding of Zn2+ to the Ca2+-saturated protein decreases its stability and causes its aggregation. -Lactalbumin interacts with membranes, proteins, peptides and low molecular weight substrates and products. These interactions are modulated by the binding of metal cations to á-lactalbumin. á-Lactalbumin forms amyloid fibrils at low pH values and some folding variants of á-lactalbumin demonstrate bactericidal activity and some of them cause apoptosis of tumor cells. Thus, -lactalbumin is a metal binding protein, the function of which depends on its environment: it takes part in lactose synthesis in the mammary gland and could be important for lowering the incidence of cancer and various infections in breast-fed children.

Table of Contents:
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Preface; Chapter 1. Introduction; Chapter 2. Anatomy of -Lactalbumin, 2.2. Isolation and Purification of -Lactalbumin, 2.3. Amino Acid Sequence and Gene Structure of -Lactalbumin, 2.4. Secondary and Tertiary Structure at Neutral pH, 2.5. Location and Structure of Cation Binding Sites, 2.6. Structure and Properties of the Molten Globule State; Chapter 3. “Psychology” of -Lactalbumin, 3.1. The Binding of Calcium and Other Divalent and Monovalent Cation to the Strong Binding Site, 3.2. Thermal Stability of -Lactalbumin, 3.3. Unfolding of -Lactalbumin Causes by Various Denaturants, 3.4. Unfolding of -Lactalbumin Causes by Pressure, 3.5. Effects of N-terminus Mutation on Protein Properties, 3.6. Acid transition, 3.7. Fibrillation of -Lactalbumin, 3.8. Effects of UV-illumination, 3.9. Interactions of -Lactalbumin with Organic Substances, Peptides and Proteins, 3.10. Interactions with Membrane Systems and Hydrophobic Interfaces; Chapter 4. Functions of -Lactalbumin, 4.1. -Lactalbumin as a Component of Lactose Synthase, 4.2. Bactericidal and Antiviral Activity of -Lactalbumin, 4.3. Cytotoxic Activity of -Lactalbumin; Chapter 5. Concluding Remarks; Index.

   Series:
      Molecular Anatomy and Physiology of Proteins - Vladimir N. Uversky (Indiana University of Medicine, USA), Series Editor
   Binding: Hardcover
   Pub. Date: 2005
   ISBN: 1-59454-107-8
   Status: AV
  
Status Code Description
AN Announcing
FM Formatting
PP Page Proofs
FP Final Production
EP Editorial Production
PR At Prepress
AP At Press
AV Available
  
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