메뉴 건너뛰기




Volumn 16, Issue 10, 2006, Pages 1157-1167

Proteolysis of bovine α-lactalbumin by thermolysin during thermal denaturation

Author keywords

Lactalbumin; Bovine milk; Molten globule; Thermal unfolding; Thermolysin

Indexed keywords

AMINO ACIDS; BACTERIA; DAIRY PRODUCTS; HYDROLYSIS; MASS SPECTROMETRY;

EID: 33745020692     PISSN: 09586946     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.idairyj.2005.10.004     Document Type: Article
Times cited : (17)

References (32)
  • 3
    • 0001744217 scopus 로고    scopus 로고
    • Use of differential scanning calorimetry and infrared spectroscopy in the study of the thermal and structural stability of α-lactalbumin
    • Boye J.I., Alli I., and Ismail A.A. Use of differential scanning calorimetry and infrared spectroscopy in the study of the thermal and structural stability of α-lactalbumin. Journal of Agricultural and Food Chemistry 45 (1997) 1116-1125
    • (1997) Journal of Agricultural and Food Chemistry , vol.45 , pp. 1116-1125
    • Boye, J.I.1    Alli, I.2    Ismail, A.A.3
  • 4
    • 0001447396 scopus 로고
    • α-Lactalbumin
    • Fox P.F. (Ed), Elsevier Science Publishers Ltd, New York, NY, USA
    • Brew K., and Grobler J.A. α-Lactalbumin. In: Fox P.F. (Ed). Advanced dairy chemistry, Vol. 1: Proteins (1992), Elsevier Science Publishers Ltd, New York, NY, USA 191-230
    • (1992) Advanced dairy chemistry, Vol. 1: Proteins , pp. 191-230
    • Brew, K.1    Grobler, J.A.2
  • 5
    • 0034711229 scopus 로고    scopus 로고
    • Crystal structures of apo- and holo-bovine α-lactalbumin at 2.2-Å resolution reveal an effect of calcium on inter-lobe interactions
    • Chrysina E.D., Brew K., and Acharya K.R. Crystal structures of apo- and holo-bovine α-lactalbumin at 2.2-Å resolution reveal an effect of calcium on inter-lobe interactions. Journal of Biological Chemistry 275 (2000) 37021-37029
    • (2000) Journal of Biological Chemistry , vol.275 , pp. 37021-37029
    • Chrysina, E.D.1    Brew, K.2    Acharya, K.R.3
  • 6
    • 0033565832 scopus 로고    scopus 로고
    • Clauser, K. R., Baker, P. R., & Burlingame, A. L. (1999). Role of accurate mass measurement (+/-10 ppm) in protein identification strategies employing MS or MS/MS and database searching. Analytical Chemistry, 71, 2871-2882. Software available at htpp://prospector.ucsf.edu/ucsfhtml4.0/msbridge.htm.
  • 7
    • 8844240048 scopus 로고    scopus 로고
    • Peptic hydrolysis of ovine β-lactoglobulin and α-lactalbumin. Exceptional susceptibility of native ovine β-lactoglobulin to pepsinolysis
    • El-Zahar K., Sitohy M., Choiset Y., Métro F., Haertlé T., and Chobert J.-M. Peptic hydrolysis of ovine β-lactoglobulin and α-lactalbumin. Exceptional susceptibility of native ovine β-lactoglobulin to pepsinolysis. International Dairy Journal 15 (2005) 17-27
    • (2005) International Dairy Journal , vol.15 , pp. 17-27
    • El-Zahar, K.1    Sitohy, M.2    Choiset, Y.3    Métro, F.4    Haertlé, T.5    Chobert, J.-M.6
  • 10
    • 0030207403 scopus 로고    scopus 로고
    • Phosphopeptides interacting with colloidal calcium phosphate isolated by tryptic hydrolysis of bovine casein micelles
    • Gagnaire V., Pierre A., Mollé D., and Léonil J. Phosphopeptides interacting with colloidal calcium phosphate isolated by tryptic hydrolysis of bovine casein micelles. Journal of Dairy Research 63 (1996) 405-422
    • (1996) Journal of Dairy Research , vol.63 , pp. 405-422
    • Gagnaire, V.1    Pierre, A.2    Mollé, D.3    Léonil, J.4
  • 11
  • 12
    • 0030993346 scopus 로고    scopus 로고
    • Calcium binding peptides from α-lactalbumin: Implications for protein folding and stability
    • Kuhlman B., Boice J.A., Wu W.J., Fairman R., and Raleigh D.P. Calcium binding peptides from α-lactalbumin: Implications for protein folding and stability. Biochemistry 36 (1997) 4607-4615
    • (1997) Biochemistry , vol.36 , pp. 4607-4615
    • Kuhlman, B.1    Boice, J.A.2    Wu, W.J.3    Fairman, R.4    Raleigh, D.P.5
  • 13
    • 72449130043 scopus 로고
    • Chromatographic determination of amino acids by the use of automatic recording equipment
    • Colowick S.P., and Kaplan N.O. (Eds), Academic Press, New York, NY, USA
    • Moore S., and Stein W.H. Chromatographic determination of amino acids by the use of automatic recording equipment. In: Colowick S.P., and Kaplan N.O. (Eds). Methods in enzymology Vol. 6 (1963), Academic Press, New York, NY, USA 819-831
    • (1963) Methods in enzymology , vol.6 , pp. 819-831
    • Moore, S.1    Stein, W.H.2
  • 15
    • 0014028211 scopus 로고
    • Thermostable protease from thermophilic bacteria. I. Thermostability, physicochemical properties, and amino acid composition
    • Ohta Y., Ogura Y., and Wada A. Thermostable protease from thermophilic bacteria. I. Thermostability, physicochemical properties, and amino acid composition. Journal of Biological Chemistry 241 (1966) 5919-5925
    • (1966) Journal of Biological Chemistry , vol.241 , pp. 5919-5925
    • Ohta, Y.1    Ogura, Y.2    Wada, A.3
  • 16
    • 0034685838 scopus 로고    scopus 로고
    • α-Lactalbumin: Structure and function
    • Permyakov E.A., and Berliner L.J. α-Lactalbumin: Structure and function. FEBS Letters 473 (2000) 269-274
    • (2000) FEBS Letters , vol.473 , pp. 269-274
    • Permyakov, E.A.1    Berliner, L.J.2
  • 18
    • 0028876581 scopus 로고
    • Rapid determination of the ratios of three aromatic residues in peptides by reversed-phase high-performance liquid chromatography with a high-resolution photodiode-array detector
    • Perrin E., Miclo L., Driou A., and Linden G. Rapid determination of the ratios of three aromatic residues in peptides by reversed-phase high-performance liquid chromatography with a high-resolution photodiode-array detector. Journal of Chromatography 664 (1995) 267-276
    • (1995) Journal of Chromatography , vol.664 , pp. 267-276
    • Perrin, E.1    Miclo, L.2    Driou, A.3    Linden, G.4
  • 19
    • 0030585408 scopus 로고    scopus 로고
    • Crystal structures of guinea-pig, goat and bovine α-lactalbumin: Highlight the enhanced conformational flexibility of regions that are significant for its action in lactose synthase
    • Pike A.C., Brew K., and Acharya K.R. Crystal structures of guinea-pig, goat and bovine α-lactalbumin: Highlight the enhanced conformational flexibility of regions that are significant for its action in lactose synthase. Structure 4 (1996) 691-703
    • (1996) Structure , vol.4 , pp. 691-703
    • Pike, A.C.1    Brew, K.2    Acharya, K.R.3
  • 21
    • 0037110569 scopus 로고    scopus 로고
    • Molten globule of bovine α-lactalbumin at neutral pH induced by heat, trifluoroethanol, and oleic acid: A comparative analysis by circular dichroism spectroscopy and limited proteolysis
    • Polverino de Laureto P., Frare E., Gottardo R., and Fontana A. Molten globule of bovine α-lactalbumin at neutral pH induced by heat, trifluoroethanol, and oleic acid: A comparative analysis by circular dichroism spectroscopy and limited proteolysis. Proteins: Structure, Function, and Genetics 49 (2002) 385-397
    • (2002) Proteins: Structure, Function, and Genetics , vol.49 , pp. 385-397
    • Polverino de Laureto, P.1    Frare, E.2    Gottardo, R.3    Fontana, A.4
  • 22
    • 0036891687 scopus 로고    scopus 로고
    • Partly folded states of members of the lysozyme/lactalbumin superfamily: A comparative study by circular dichroism spectroscopy and limited proteolysis
    • Polverino de Laureto P., Frare E., Gottardo R., Van Dael H., and Fontana A. Partly folded states of members of the lysozyme/lactalbumin superfamily: A comparative study by circular dichroism spectroscopy and limited proteolysis. Protein Science 11 (2002) 2932-2946
    • (2002) Protein Science , vol.11 , pp. 2932-2946
    • Polverino de Laureto, P.1    Frare, E.2    Gottardo, R.3    Van Dael, H.4    Fontana, A.5
  • 24
  • 25
    • 84907035182 scopus 로고
    • The structural and functional roles of metal ions in thermolysin
    • Roche R.S., and Voordouw G. The structural and functional roles of metal ions in thermolysin. CRC Critical Reviews in Biochemistry 5 (1978) 1-23
    • (1978) CRC Critical Reviews in Biochemistry , vol.5 , pp. 1-23
    • Roche, R.S.1    Voordouw, G.2
  • 26
    • 0001900355 scopus 로고
    • Enzymatic hydrolysis of whey proteins. Hydrolysis of α-lactalbumin and β-lactoglobulin in buffer solutions by proteolytic enzymes
    • Schmidt D.G., and Poll J.K. Enzymatic hydrolysis of whey proteins. Hydrolysis of α-lactalbumin and β-lactoglobulin in buffer solutions by proteolytic enzymes. Netherlands Milk and Dairy Journal 45 (1991) 225-240
    • (1991) Netherlands Milk and Dairy Journal , vol.45 , pp. 225-240
    • Schmidt, D.G.1    Poll, J.K.2
  • 27
    • 0001769758 scopus 로고
    • Enzymatic hydrolysis of whey proteins. Influence of heat treatment of α-lactalbumin and β-lactoglobulin on their proteolysis by pepsin and papain
    • Schmidt D.G., and Van Markwijk B.W. Enzymatic hydrolysis of whey proteins. Influence of heat treatment of α-lactalbumin and β-lactoglobulin on their proteolysis by pepsin and papain. Netherlands Milk and Dairy Journal 47 (1993) 15-22
    • (1993) Netherlands Milk and Dairy Journal , vol.47 , pp. 15-22
    • Schmidt, D.G.1    Van Markwijk, B.W.2
  • 29
    • 0036084260 scopus 로고    scopus 로고
    • Comparison of protein fragments identified by limited proteolysis and by computational cutting of proteins
    • Tsai C.J., Polverino de Laureto P., Fontana A., and Nussinov R. Comparison of protein fragments identified by limited proteolysis and by computational cutting of proteins. Protein Science 11 (2002) 1753-1770
    • (2002) Protein Science , vol.11 , pp. 1753-1770
    • Tsai, C.J.1    Polverino de Laureto, P.2    Fontana, A.3    Nussinov, R.4
  • 32
    • 0026679847 scopus 로고
    • Absence of the thermal transition in apo-α-lactalbumin in the molten globule state: A study by differential scanning microcalorimetry
    • Yutani K., Ogasahara K., and Kuwajima K. Absence of the thermal transition in apo-α-lactalbumin in the molten globule state: A study by differential scanning microcalorimetry. Journal of Molecular Biology 228 (1992) 347-350
    • (1992) Journal of Molecular Biology , vol.228 , pp. 347-350
    • Yutani, K.1    Ogasahara, K.2    Kuwajima, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.