메뉴 건너뛰기




Volumn 24, Issue 2, 1996, Pages 253-258

Large-scale purification and preliminary X-ray diffraction studies of human aspartylglucosaminidase

Author keywords

crystallization; glycosylasparaginase; lysosomes; protein purification

Indexed keywords

COMPLEMENTARY DNA; LYSOSOME ENZYME; N4 (BETA N ACETYLGLUCOSAMINYL)ASPARAGINASE; RECOMBINANT PROTEIN;

EID: 0029968087     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(199602)24:2<253::AID-PROT12>3.0.CO;2-M     Document Type: Article
Times cited : (12)

References (20)
  • 1
    • 0024850749 scopus 로고
    • Lysosomal degradation of Asn-linked glycoproteins
    • Aronson, N. N., Kuranda, J. K. Lysosomal degradation of Asn-linked glycoproteins. FASEB J. 3:2615-2622, 1989.
    • (1989) FASEB J. , vol.3 , pp. 2615-2622
    • Aronson, N.N.1    Kuranda, J.K.2
  • 2
    • 0027389271 scopus 로고
    • Lysosomal aspartylglucosaminidase is processed to the active subunit complex in the endoplasmic reticulum
    • Ikonen, E., Julkunen, I., Tollersrud, O-K., Kalkkinen, N., Peltonen, L. Lysosomal aspartylglucosaminidase is processed to the active subunit complex in the endoplasmic reticulum. EMBO J. 12:295-302, 1993.
    • (1993) EMBO J. , vol.12 , pp. 295-302
    • Ikonen, E.1    Julkunen, I.2    Tollersrud, O.-K.3    Kalkkinen, N.4    Peltonen, L.5
  • 3
    • 0024410435 scopus 로고
    • Purification and characterization of rat liver glycosylasparaginase
    • Tollersrud, O-K., Aronson, N. N. Purification and characterization of rat liver glycosylasparaginase. Biochem. J. 260:101-108, 1989.
    • (1989) Biochem. J. , vol.260 , pp. 101-108
    • Tollersrud, O.-K.1    Aronson, N.N.2
  • 4
    • 0025730688 scopus 로고
    • Human leucocyte aspartylglucosaminidase. Evidence for two different subunits in a more complex native structure
    • Halila, R., Baumann, M., Ikonen, E., Enomaa, N., Peltonen, L. Human leucocyte aspartylglucosaminidase. Evidence for two different subunits in a more complex native structure. Biochem. J. 276.251-2562, 1991.
    • (1991) Biochem. J. , vol.276 , pp. 251-2562
    • Halila, R.1    Baumann, M.2    Ikonen, E.3    Enomaa, N.4    Peltonen, L.5
  • 5
    • 0024468076 scopus 로고
    • Isolation of a human hepatic 60 kDa aspartylglucosaminidase consisting of three non-identical polypeptides
    • Baumann, M., Peltonen, L., Aula, P., Kalkkinen, N. Isolation of a human hepatic 60 kDa aspartylglucosaminidase consisting of three non-identical polypeptides. Biochem. J. 262:189-194, 1989.
    • (1989) Biochem. J. , vol.262 , pp. 189-194
    • Baumann, M.1    Peltonen, L.2    Aula, P.3    Kalkkinen, N.4
  • 6
    • 0028407361 scopus 로고
    • Large-scale purification of human aspartylglucosaminidase: Utilization of exceptional sodium dodecyl sulfate resistance
    • Heiskanen, T., Tollersrud, O. K., Zhao, M., Peltonen, L. Large-scale purification of human aspartylglucosaminidase: Utilization of exceptional sodium dodecyl sulfate resistance. Protein Expression Purification 5:205-210, 1994.
    • (1994) Protein Expression Purification , vol.5 , pp. 205-210
    • Heiskanen, T.1    Tollersrud, O.K.2    Zhao, M.3    Peltonen, L.4
  • 8
    • 0027070454 scopus 로고
    • Purification and structure of human liver aspartylglucosaminidase
    • Rip, J. W., Coulter-Mackie, M. B., Rupar, C. A., Gordon, B. A. Purification and structure of human liver aspartylglucosaminidase. Biochem. J. 288:1005-1010, 1992.
    • (1992) Biochem. J. , vol.288 , pp. 1005-1010
    • Rip, J.W.1    Coulter-Mackie, M.B.2    Rupar, C.A.3    Gordon, B.A.4
  • 9
    • 0026874436 scopus 로고
    • A highspeed data collection system for large-unit-cell crystals using an imaging plate as a detector
    • Sato, M., Yamamoto, M., Imada, K., Katsube, Y. A highspeed data collection system for large-unit-cell crystals using an imaging plate as a detector. J. Appl. Crystallogr. 25:348-357, 1992.
    • (1992) J. Appl. Crystallogr. , vol.25 , pp. 348-357
    • Sato, M.1    Yamamoto, M.2    Imada, K.3    Katsube, Y.4
  • 11
    • 0028964044 scopus 로고
    • Intracellular sorting of aspartylglucosaminidase: The role of N-linked oligosaccharides and evidence of Man-6-P independent lysosomal targeting
    • Tikkanen, R., Enomaa, N., Riikonen, A., Ikonen, E., Peltonen, L. intracellular sorting of aspartylglucosaminidase: The role of N-linked oligosaccharides and evidence of Man-6-P independent lysosomal targeting. DNA Cell Biol. 14: 305-312, 1995.
    • (1995) DNA Cell Biol. , vol.14 , pp. 305-312
    • Tikkanen, R.1    Enomaa, N.2    Riikonen, A.3    Ikonen, E.4    Peltonen, L.5
  • 12
    • 0026788005 scopus 로고
    • Human aspartylglucosaminidase. A biochemical and immunocytochemical characterization of the enzyme in normal and aspartylglucosaminuria fibroblasts
    • Enomaa, N., Heiskanen, T., Halila, R., Sormunen, R., Seppälä, R., Vihinen, M., Peltonen, L. Human aspartylglucosaminidase. A biochemical and immunocytochemical characterization of the enzyme in normal and aspartylglucosaminuria fibroblasts. Biochem. J. 286:613-618, 1992.
    • (1992) Biochem. J. , vol.286 , pp. 613-618
    • Enomaa, N.1    Heiskanen, T.2    Halila, R.3    Sormunen, R.4    Seppälä, R.5    Vihinen, M.6    Peltonen, L.7
  • 13
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews, B. W. Solvent content of protein crystals. J. Mol. Biol. 33:491-497, 1968.
    • (1968) J. Mol. Biol. , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 14
    • 0026095291 scopus 로고
    • Glycoasparaginase from human leukocytes. Inactivation and covalent modification with diazo-oxonorvaline
    • Kaartinen, V., Williams, J. C., Tomich, J., Yates, J. R., Hood, L. E., Mononen, I. Glycoasparaginase from human leukocytes. Inactivation and covalent modification with diazo-oxonorvaline. J. Biol. Chem. 266:5860-5869, 1991.
    • (1991) J. Biol. Chem. , vol.266 , pp. 5860-5869
    • Kaartinen, V.1    Williams, J.C.2    Tomich, J.3    Yates, J.R.4    Hood, L.E.5    Mononen, I.6
  • 16
    • 0027124132 scopus 로고
    • Purification and crystallization of human cathepsin D
    • Fusek, M., Baudys, M., Metcalf, P. Purification and crystallization of human cathepsin D. J. Mol. Biol. 226:555-557, 1992.
    • (1992) J. Mol. Biol. , vol.226 , pp. 555-557
    • Fusek, M.1    Baudys, M.2    Metcalf, P.3
  • 17
    • 0026656187 scopus 로고
    • Human liver cathepsin D. Purification, crystallization and preliminary X-ray diffraction analysis of a lysosomal enzyme
    • Gulnik, S., Baldwin, E. T., Tarasova, N., Erickson, J. Human liver cathepsin D. Purification, crystallization and preliminary X-ray diffraction analysis of a lysosomal enzyme. J. Mol. Biol. 227:265-270, 1992.
    • (1992) J. Mol. Biol. , vol.227 , pp. 265-270
    • Gulnik, S.1    Baldwin, E.T.2    Tarasova, N.3    Erickson, J.4
  • 19
    • 0026089364 scopus 로고
    • Aspartylglucosaminuria: cDNA encoding human aspartylglucosaminidase and the missense mutation causing the disease
    • Ikonen, E., Baumann, M., Grön, K., Syvänen, A-c., Enomaa, N., Halila, R., Aula, P., Peltonen, L. Aspartylglucosaminuria: cDNA encoding human aspartylglucosaminidase and the missense mutation causing the disease. EMBO J. 10:51-58, 1991.
    • (1991) EMBO J. , vol.10 , pp. 51-58
    • Ikonen, E.1    Baumann, M.2    Grön, K.3    Syvänen, A.-C.4    Enomaa, N.5    Halila, R.6    Aula, P.7    Peltonen, L.8
  • 20
    • 0014401981 scopus 로고
    • Aspartylglucosaminuria. An inborn error of metabolism associated with mental defect
    • Pollitt, R. J., Jenner, F. A., Merskey, H. Aspartylglucosaminuria. An inborn error of metabolism associated with mental defect. Lancet 2:253-255, 1968.
    • (1968) Lancet , vol.2 , pp. 253-255
    • Pollitt, R.J.1    Jenner, F.A.2    Merskey, H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.