메뉴 건너뛰기




Volumn 49, Issue 1, 2006, Pages 32-38

Partial purification of human parathyroid hormone 1-84 as a thioredoxin fusion form in recombinant Escherichia coli by thermoosmotic shock

Author keywords

Affinity chromatography; Human parathyroid hormone 1 84; Purification; Recombinant Escherichia coli; Thermoosmotic shock

Indexed keywords

CYCLIC AMP; EDETIC ACID; HYBRID PROTEIN; PARATHYROID HORMONE; PTH PROTEIN, HUMAN; THIOREDOXIN;

EID: 33747788707     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2006.03.004     Document Type: Article
Times cited : (5)

References (17)
  • 1
    • 0020430921 scopus 로고
    • Parathyroid hormone: chemistry, biosynthesis, and mode of action
    • Potts J.T., Kronenberg H.M., and Rosenblatt M. Parathyroid hormone: chemistry, biosynthesis, and mode of action. Adv. Protein. Chem. 35 (1982) 323-396
    • (1982) Adv. Protein. Chem. , vol.35 , pp. 323-396
    • Potts, J.T.1    Kronenberg, H.M.2    Rosenblatt, M.3
  • 2
    • 33747767736 scopus 로고
    • Characteristics of the vasodilator action of PTH (1-34) in porcine coronary artery segments and perfused rat thoracic aorta
    • Crass M.F., Neufeld M.D., Hulsey S.M., and Bulkley T.J. Characteristics of the vasodilator action of PTH (1-34) in porcine coronary artery segments and perfused rat thoracic aorta. J. Mol. Cell Cardiol. 20 supplement III (1988) 34
    • (1988) J. Mol. Cell Cardiol. , vol.20 , Issue.SUPPL. III , pp. 34
    • Crass, M.F.1    Neufeld, M.D.2    Hulsey, S.M.3    Bulkley, T.J.4
  • 4
    • 0027673618 scopus 로고
    • Affinity purification of histidine-tagged proteins
    • Schmitt J., Hess H., and Stunnenberg H.J. Affinity purification of histidine-tagged proteins. Mol. Biol. Rep. 18 (1993) 223-230
    • (1993) Mol. Biol. Rep. , vol.18 , pp. 223-230
    • Schmitt, J.1    Hess, H.2    Stunnenberg, H.J.3
  • 5
    • 0014010845 scopus 로고
    • The release of enzymes by osmotic shock from Escherichia coli in exponential phase
    • Nossal N.G., and Heppel L.A. The release of enzymes by osmotic shock from Escherichia coli in exponential phase. J. Biol. Chem. 241 (1966) 3055-3062
    • (1966) J. Biol. Chem. , vol.241 , pp. 3055-3062
    • Nossal, N.G.1    Heppel, L.A.2
  • 6
    • 0030875484 scopus 로고    scopus 로고
    • Effects of salt and osmotic shocks on unadapted and adapted callus lines of tobacco
    • Gangopadhyay G., Basu S., Mukherjee B.B., and Gupta S. Effects of salt and osmotic shocks on unadapted and adapted callus lines of tobacco. Plant. Cell Tiss. Org. 49 (1997) 45-52
    • (1997) Plant. Cell Tiss. Org. , vol.49 , pp. 45-52
    • Gangopadhyay, G.1    Basu, S.2    Mukherjee, B.B.3    Gupta, S.4
  • 7
    • 0030269967 scopus 로고    scopus 로고
    • Development of a simple method for the recovery of recombinant proteins from the Escherichia coli periplasm
    • French C., Keshavarz-Moore E., and Ward J.M. Development of a simple method for the recovery of recombinant proteins from the Escherichia coli periplasm. Enzyme Microb. Technol. 19 (1996) 332-338
    • (1996) Enzyme Microb. Technol. , vol.19 , pp. 332-338
    • French, C.1    Keshavarz-Moore, E.2    Ward, J.M.3
  • 8
    • 0036279657 scopus 로고    scopus 로고
    • Lysozyme-osmotic shock methods for localization of periplasmic redox proteins in bacteria
    • Davidson V.L., and Sun D.P. Lysozyme-osmotic shock methods for localization of periplasmic redox proteins in bacteria. Meth. Enzymol. 353 (2002) 121-130
    • (2002) Meth. Enzymol. , vol.353 , pp. 121-130
    • Davidson, V.L.1    Sun, D.P.2
  • 9
    • 0031029293 scopus 로고    scopus 로고
    • Effect of heat treatment on chemically modified proteins of legume seeds
    • Klepacka M., Porzucek H., and Kluczyńska M. Effect of heat treatment on chemically modified proteins of legume seeds. Food Chem. 58 (1997) 219-222
    • (1997) Food Chem. , vol.58 , pp. 219-222
    • Klepacka, M.1    Porzucek, H.2    Kluczyńska, M.3
  • 10
    • 2042537516 scopus 로고
    • Thioredoxin and ferredoxin-thioredoxin reductase activity occur in a fermentative bacterium
    • Hammel K.E., and Buchanan B.B. Thioredoxin and ferredoxin-thioredoxin reductase activity occur in a fermentative bacterium. FEBS Lett. 130 (1981) 88-92
    • (1981) FEBS Lett. , vol.130 , pp. 88-92
    • Hammel, K.E.1    Buchanan, B.B.2
  • 12
    • 0021306856 scopus 로고
    • System for polyacrylamide gel electrophoresis
    • Blackshear P.J. System for polyacrylamide gel electrophoresis. Meth. Enzymol. 104 (1984) 237-255
    • (1984) Meth. Enzymol. , vol.104 , pp. 237-255
    • Blackshear, P.J.1
  • 13
    • 0036074194 scopus 로고    scopus 로고
    • CAMP binding protein assay for widespread use in cell signaling studies
    • Chen H.L., McCauley L.K., and D'Silva N.J. CAMP binding protein assay for widespread use in cell signaling studies. Biotechniques 33 (2002) 1-5
    • (2002) Biotechniques , vol.33 , pp. 1-5
    • Chen, H.L.1    McCauley, L.K.2    D'Silva, N.J.3
  • 14
    • 2542459428 scopus 로고    scopus 로고
    • A modified osmotic shock for periplasmic release of a recombinant creatinase from Escherichia coli
    • Chen Y.C., Chen L.A., Chen S.J., Chang M.C., and Chen T.L. A modified osmotic shock for periplasmic release of a recombinant creatinase from Escherichia coli. Biochem. Eng. J. 19 (2004) 211-215
    • (2004) Biochem. Eng. J. , vol.19 , pp. 211-215
    • Chen, Y.C.1    Chen, L.A.2    Chen, S.J.3    Chang, M.C.4    Chen, T.L.5
  • 15
    • 0031549641 scopus 로고    scopus 로고
    • Factors determining more efficient large-scale release of a periplasm enzyme from E. coli using lysozyme
    • Pierce J.J., Turner C., Keshavarz-Moore E., and Dunnill P. Factors determining more efficient large-scale release of a periplasm enzyme from E. coli using lysozyme. J. Biotechnol. 58 (1997) 1-11
    • (1997) J. Biotechnol. , vol.58 , pp. 1-11
    • Pierce, J.J.1    Turner, C.2    Keshavarz-Moore, E.3    Dunnill, P.4
  • 16
    • 0026070766 scopus 로고
    • Protein fusions: bioseparation and application
    • Sherwood R. Protein fusions: bioseparation and application. Trends Biotechnol. 9 (1991) 1-3
    • (1991) Trends Biotechnol. , vol.9 , pp. 1-3
    • Sherwood, R.1
  • 17
    • 76549170704 scopus 로고
    • The release of enzymes from Escherichia coli by osmotic shock and during the formation of spheroplasts
    • Neu H.C., and Heppel L.A. The release of enzymes from Escherichia coli by osmotic shock and during the formation of spheroplasts. J. Biol. Chem. 240 (1965) 3685-3692
    • (1965) J. Biol. Chem. , vol.240 , pp. 3685-3692
    • Neu, H.C.1    Heppel, L.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.