Limited proteolysis of beta-lactoglobulin using thermolysin. Effects of calcium on the outcome of proteolysis.

[1]  H. Mantsch,et al.  Salt bridge induced changes in the secondary structure of ionic polypeptides , 1992, Biopolymers.

[2]  P E Wright,et al.  Folding of peptide fragments comprising the complete sequence of proteins. Models for initiation of protein folding. I. Myohemerythrin. , 1992, Journal of molecular biology.

[3]  J. Chobert,et al.  Limited Proteolysis of Solvent-Induced Folding Changes of β-Lactoglobulin , 1991 .

[4]  J. Chobert,et al.  Influence of pH on the structural changes of beta-lactoglobulin studied by tryptic hydrolysis. , 1991, Biochimica et biophysica acta.

[5]  M. Marden,et al.  β‐Lactoglobulin binds retinol and protoporphyrin IX at two different binding sites , 1990, FEBS letters.

[6]  G. Dodin,et al.  Binding of ellipticine to beta-lactoglobulin. A physico-chemical study of the specific interaction of an antitumor drug with a transport protein. , 1990, European journal of biochemistry.

[7]  J. Kinsella,et al.  Structural and conformational basis of the resistance of .beta.-lactoglobulin to peptic and chymotryptic digestion , 1988 .

[8]  B. Ribadeau-Dumas,et al.  Preparation of β‐Lactoglobulin and p‐Lactoglobulin‐Free Proteins from Whey Retentate by NaCI Salting Out at Low pH , 1988 .

[9]  G. Brûlé,et al.  Binding of bivalent cations to α-lactalbumin and β-lactoglobulin: effect of pH and ionic strength , 1988 .

[10]  M. Bolognesi,et al.  Crystal structure of the trigonal form of bovine beta-lactoglobulin and of its complex with retinol at 2.5 A resolution. , 1987, Journal of molecular biology.

[11]  R. Huber,et al.  Crystallization, crystal structure analysis and preliminary molecular model of the bilin binding protein from the insect Pieris brassicae. , 1987, Journal of molecular biology.

[12]  Miguel Calvo Rebollar,et al.  Lipid binding by β-lactoglobulin of cow milk , 1987 .

[13]  P. Kraulis,et al.  The structure of β-lactoglobulin and its similarity to plasma retinol-binding protein , 1986, Nature.

[14]  D. I. Stuart,et al.  α-Lactalbumin possesses a novel calcium binding loop , 1986, Nature.

[15]  M. Zamai,et al.  Correlation between sites of limited proteolysis and segmental mobility in thermolysin. , 1986, Biochemistry.

[16]  B. Bidlingmeyer,et al.  Rapid analysis of amino acids using pre-column derivatization. , 1984, Journal of chromatography.

[17]  P. A. Peterson,et al.  The three‐dimensional structure of retinol‐binding protein. , 1984, The EMBO journal.

[18]  E. M. Brown.  Interactions of -Lactoglobulin and a-Lactalbumin with Lipids: A Review1 , 1984 .

[19]  J. Andrew McCammon,et al.  The dynamic picture of protein structure , 1983 .

[20]  K. Brew,et al.  Characteristics of the binding of Ca2+ and other divalent metal ions to bovine alpha-lactalbumin. , 1981, The Journal of biological chemistry.

[21]  P. Song,et al.  Spectroscopic characterization of β-lactoglobulin-retinol complex , 1980 .

[22]  B. Matthews,et al.  The conformation of thermolysin. , 1974, The Journal of biological chemistry.

[23]  A. Stangl,et al.  Die Sequenzanalyse des β-Lactoglobulins , 1973 .

[24]  J. Heller,et al.  The enhancement of fluorescence and the decreased susceptibility to enzymatic oxidation of retinol complexed with bovine serum albumin, -lactoglobulin, and the retinol-binding protein of human plasma. , 1972, The Journal of biological chemistry.

[25]  A. Berger,et al.  On the size of the active site in proteases. I. Papain. , 1967, Biochemical and biophysical research communications.