메뉴 건너뛰기




Volumn 23, Issue 2, 2012, Pages 86-90

Separation of a milk acid phosphatase from a purified lactoferrin fraction and identification as a member of the mammalian purple acid phosphatase family

Author keywords

[No Author keywords available]

Indexed keywords

ACID PHOSPHATASE; ACTIVE MOLECULES; BOVINE MILK; LACTOFERRIN; N-TERMINAL AMINO ACID SEQUENCE; OPTIMUM PH; OPTIMUM TEMPERATURE; PURPLE ACID PHOSPHATASE; TARTRATE-RESISTANT ACID PHOSPHATASE; TIME-DEPENDENT; TRYPTIC DIGESTION;

EID: 84856281709     PISSN: 09586946     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.idairyj.2011.10.003     Document Type: Article
Times cited : (2)

References (20)
  • 1
    • 0032439914 scopus 로고    scopus 로고
    • Purification and characterization of an acid phosphatase from cell membrane fraction of Lactococcus lactis ssp lactis 303
    • Akuzawa R., Fox P.F. Purification and characterization of an acid phosphatase from cell membrane fraction of Lactococcus lactis ssp lactis 303. Food Research International 1998, 31:157-165.
    • (1998) Food Research International , vol.31 , pp. 157-165
    • Akuzawa, R.1    Fox, P.F.2
  • 3
    • 0021329978 scopus 로고
    • Purification and characterization of a vanadate-sensitive nucleotide tri- and diphosphatase with acid pH optimum from rat bone
    • Andersson G., Ek-Rylander B., Hammarström L. Purification and characterization of a vanadate-sensitive nucleotide tri- and diphosphatase with acid pH optimum from rat bone. Archives of Biochemistry and Biophysics 1984, 228:431-438.
    • (1984) Archives of Biochemistry and Biophysics , vol.228 , pp. 431-438
    • Andersson, G.1    Ek-Rylander, B.2    Hammarström, L.3
  • 4
    • 33644915633 scopus 로고    scopus 로고
    • Biochemical characterization of lactoferrin (LF)-binding proteins involved in the multiple physiological functions of LF invitro
    • Fujihara M., Tanigawa K., Kawakami H., Ohtsuki K. Biochemical characterization of lactoferrin (LF)-binding proteins involved in the multiple physiological functions of LF invitro. Milk Science 2004, 53:320-322.
    • (2004) Milk Science , vol.53 , pp. 320-322
    • Fujihara, M.1    Tanigawa, K.2    Kawakami, H.3    Ohtsuki, K.4
  • 5
    • 0035805651 scopus 로고    scopus 로고
    • The highly exposed loop region in mammalian purple acid phosphatase controls the catalytic activity
    • Funhoff E.G., Klaassen C.H.W., Samyn B., Van Beeumen J., Averill B.A. The highly exposed loop region in mammalian purple acid phosphatase controls the catalytic activity. Chembiochem 2001, 2:355-363.
    • (2001) Chembiochem , vol.2 , pp. 355-363
    • Funhoff, E.G.1    Klaassen, C.H.W.2    Samyn, B.3    Van Beeumen, J.4    Averill, B.A.5
  • 7
    • 33644897325 scopus 로고    scopus 로고
    • Purification and biochemical characterization of a fibroblast growth factor-binding protein (FGF-BP) from the lactoferrin fraction of bovine milk
    • Kawakami A., Hirayama K., Kawakami F., Kawakami H., Fujihara M., Ohtsuki K. Purification and biochemical characterization of a fibroblast growth factor-binding protein (FGF-BP) from the lactoferrin fraction of bovine milk. Biochimica et Biophysica Acta 2006, 1760:421-431.
    • (2006) Biochimica et Biophysica Acta , vol.1760 , pp. 421-431
    • Kawakami, A.1    Hirayama, K.2    Kawakami, F.3    Kawakami, H.4    Fujihara, M.5    Ohtsuki, K.6
  • 8
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 9
    • 0033214081 scopus 로고    scopus 로고
    • Tartrate-resistant purple acid phosphatase is synthesized as a latent proenzyme and activated by cysteine proteinases
    • Ljusberg J., Ek-Rylander B., Andersson G. Tartrate-resistant purple acid phosphatase is synthesized as a latent proenzyme and activated by cysteine proteinases. Biochemical Journal 1999, 343:63-69.
    • (1999) Biochemical Journal , vol.343 , pp. 63-69
    • Ljusberg, J.1    Ek-Rylander, B.2    Andersson, G.3
  • 11
    • 0023664635 scopus 로고
    • Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes
    • Matsudaira P. Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes. Journal of Biological Chemistry 1987, 262:10035-10038.
    • (1987) Journal of Biological Chemistry , vol.262 , pp. 10035-10038
    • Matsudaira, P.1
  • 12
    • 0019153180 scopus 로고
    • Comparative study of the iron-binding properties of human transferring. I. Complete sequential iron saturation and desaturation of the lactotransferrin
    • Mazurier J., Spik G. Comparative study of the iron-binding properties of human transferring. I. Complete sequential iron saturation and desaturation of the lactotransferrin. Biochimica et Biophysica Acta 1980, 629:399-408.
    • (1980) Biochimica et Biophysica Acta , vol.629 , pp. 399-408
    • Mazurier, J.1    Spik, G.2
  • 13
    • 0019492995 scopus 로고
    • Ultrasensitive stain for proteins in polyacrylamide gels shows regional variation in cerebrospinal fluid proteins
    • Merril C.R., Goldman D., Sedman S.A., Ebert M.H. Ultrasensitive stain for proteins in polyacrylamide gels shows regional variation in cerebrospinal fluid proteins. Science 1981, 211:1437-1438.
    • (1981) Science , vol.211 , pp. 1437-1438
    • Merril, C.R.1    Goldman, D.2    Sedman, S.A.3    Ebert, M.H.4
  • 14
    • 71649083204 scopus 로고    scopus 로고
    • Presence of lactoferrin in a bovine skim milk fraction with acid phosphatase activity
    • Miura T., Ono K., Izumi T., Akuzawa R. Presence of lactoferrin in a bovine skim milk fraction with acid phosphatase activity. International Dairy Journal 2010, 20:67-71.
    • (2010) International Dairy Journal , vol.20 , pp. 67-71
    • Miura, T.1    Ono, K.2    Izumi, T.3    Akuzawa, R.4
  • 15
    • 0025010656 scopus 로고
    • Intracellular regulation of enzyme secretion from rat osteoclasts and evidence for a functional role in bone resorption
    • Moonga B.S., Moss D.W., Patchell A., Zaidi M. Intracellular regulation of enzyme secretion from rat osteoclasts and evidence for a functional role in bone resorption. Journal of Physiology 1990, 429:29-45.
    • (1990) Journal of Physiology , vol.429 , pp. 29-45
    • Moonga, B.S.1    Moss, D.W.2    Patchell, A.3    Zaidi, M.4
  • 16
    • 0027715897 scopus 로고
    • Transient expression of tartrate-resistant acid phosphatase (TRAP) gene in hamster cells: a pilot study
    • Nuthmann V., Dirks W., Drexler H.G. Transient expression of tartrate-resistant acid phosphatase (TRAP) gene in hamster cells: a pilot study. Leukemia 1993, 7:1960-1964.
    • (1993) Leukemia , vol.7 , pp. 1960-1964
    • Nuthmann, V.1    Dirks, W.2    Drexler, H.G.3
  • 17
    • 0023086945 scopus 로고
    • Histochemical investigations on the localization of the purple acid phosphatase in the bovine spleen
    • Schindelmeiser J., Münstermann D., Witzel H. Histochemical investigations on the localization of the purple acid phosphatase in the bovine spleen. Histochemistry 1987, 87:13-19.
    • (1987) Histochemistry , vol.87 , pp. 13-19
    • Schindelmeiser, J.1    Münstermann, D.2    Witzel, H.3
  • 18
    • 0027585645 scopus 로고
    • Separation and characterization of the C-terminal half molecule of bovine lactoferrin
    • Shimazaki K., Tanaka T., Kon H., Oota K., Kawaguchi A., Maki Y., et al. Separation and characterization of the C-terminal half molecule of bovine lactoferrin. Journal of Dairy Science 1993, 76:946-955.
    • (1993) Journal of Dairy Science , vol.76 , pp. 946-955
    • Shimazaki, K.1    Tanaka, T.2    Kon, H.3    Oota, K.4    Kawaguchi, A.5    Maki, Y.6
  • 19
    • 0034980338 scopus 로고    scopus 로고
    • Characterization of bovine Angiogenin-1 and lactogenin-like protein as a Glycyrrhizin-binding protein and their invitro phosphorylation by C-kinase
    • Tanigawa K., Fujihara M., Sakamoto R., Yanahira S., Ohtsuki K. Characterization of bovine Angiogenin-1 and lactogenin-like protein as a Glycyrrhizin-binding protein and their invitro phosphorylation by C-kinase. Biological and Pharmaceutical Bulletin 2001, 24:443-447.
    • (2001) Biological and Pharmaceutical Bulletin , vol.24 , pp. 443-447
    • Tanigawa, K.1    Fujihara, M.2    Sakamoto, R.3    Yanahira, S.4    Ohtsuki, K.5
  • 20
    • 0000282102 scopus 로고
    • Isolation of lactoperoxidase and lactoferrins from bovine milk acid whey by carboxymethyl cation exchange chromatography
    • Yoshida S., Ye X.-Y. Isolation of lactoperoxidase and lactoferrins from bovine milk acid whey by carboxymethyl cation exchange chromatography. Journal of Dairy Science 1991, 74:1439-1444.
    • (1991) Journal of Dairy Science , vol.74 , pp. 1439-1444
    • Yoshida, S.1    Ye, X.-Y.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.