NMR Studies of the Structure and Environment of the Milk Protein α-Lactalbumin

  • Lawrence J. Berliner
  • Robert Kaptein
  • Keiko Koga
  • Giovanni Musci
Part of the Basic Life Sciences book series (BLSC, volume 56)


α-Lactalbumin (o-LA) plays a unique role in milk biochemistry. That is, its function appears to be only as a modifier protein in lactose biosynthesis by directing the specificity of galactosyl transferase from the acceptor substrate N-acetylglucosamine (GlcNAc) to glucose (Glc). Specifically, α-lactalbumin lowers the KM for Glc from 1.4 M to 5.0 mM, while the reaction involving GlcNAc as an acceptor becomes inhibited in the presence of α-lactalbumin (Hill and Brew, 1975). Actually, it was not known until very recently that α-LA was a calcium-binding protein. It had been studied extensively in the past by Kronman and colleagues (Kronman et al., 1964; Kronman and Andreotti, 1972) yet it was never realized that the protein existed in several conformations due to multiple states of cation binding. In fact, much of the published data on the physical or structural properties of this protein previous to 1978 are ambiguous since workers were not aware that their α-LA samples contained calcium and/or other strongly bound cations.


Dynamic Nuclear Polarization Chemically Induce Dynamic Nuclear Polarization Calcium Site Nuclear Spin Relaxation Nuclear Spin State 
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Copyright information

© Plenum Press, New York 1990

Authors and Affiliations

  • Lawrence J. Berliner
    • 1
  • Robert Kaptein
    • 2
  • Keiko Koga
    • 3
  • Giovanni Musci
    • 4
  1. 1.Department of ChemistryOhio State UniversityColumbusUSA
  2. 2.Department of Organic ChemistryUniversity of UtrechtUtrechtThe Netherlands
  3. 3.Bioenergetics Research Center, Tokushima Research InstituteOtsuka Pharmaceutical Co., Ltd.Kawauchi-cho, Tokushima 771Japan
  4. 4.Centro di Biologia Molecolare del C.N.R. Dipartimento di Scienze BiochimicheUniversita’ „La Sapienza“RomeItaly

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