메뉴 건너뛰기




Volumn , Issue , 2003, Pages 1-302

Calculations for Molecular Biology and Biotechnology: A Guide to Mathematics in the Laboratory

(1)  Stephenson, Frank H a  

a NONE

Author keywords

[No Author keywords available]

Indexed keywords


EID: 84902390579     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-0-12-665751-7.X5041-0     Document Type: Book
Times cited : (17)

References (29)
  • 1
    • 0001641514 scopus 로고
    • Mutations of bacteria from virus sensitivity to virus resistance
    • S.E. Luria and M. Delbrück (1943) Mutations of bacteria from virus sensitivity to virus resistance. Genetics 28 491-511.
    • (1943) Genetics , vol.28 , pp. 491-511
    • Luria, S.E.1    Delbrück, M.2
  • 3
    • 0025355882 scopus 로고
    • Analysis of cytokine mRNA and DNA: detection and quantitation by competitive polymerase chain reaction
    • G. Gilliland Gary, S. Perrin Steven, K. Blanchard Kerry and H.F. Bunn H. Franklin (1990) Analysis of cytokine mRNA and DNA: detection and quantitation by competitive polymerase chain reaction. Proc. Natl. Acad. Sci. USA 87 2725-2729.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 2725-2729
    • Gilliland, G.1    Perrin, S.2    Blanchard, K.3    Bunn, H.F.4
  • 4
    • 0003056398 scopus 로고
    • Manipulation of DNA by PCR
    • K. Mullis, F. Ferré, R.A. Gibbs (Eds), Birkhäuser
    • K. Hayashi Kenshi (1994) Manipulation of DNA by PCR. K. Mullis, F. Ferré, R.A. Gibbs (Eds) The Polymerase Chain Reaction Birkhäuser 3-13.
    • (1994) The Polymerase Chain Reaction , pp. 3-13
    • Hayashi, K.1
  • 5
    • 0027518417 scopus 로고
    • Quantitative competitive polymerase chain reaction for accurate quantitation of HIV DNA and RNA species
    • M. Piatak Jr., K.-C. Luk Ka-Cheung, B. Williams Bill and J.D. Lifson Jeffrey D. (1993) Quantitative competitive polymerase chain reaction for accurate quantitation of HIV DNA and RNA species. BioTechniques 14 70-80.
    • (1993) BioTechniques , vol.14 , pp. 70-80
    • Piatak, M.1    Luk, K.-C.2    Williams, B.3    Lifson, J.D.4
  • 6
    • 0024578843 scopus 로고
    • Effect of ionic strength on the hybridization of oligodeoxynucleotides with reduced charge due to methylphosphonate linkages to unmodified oligodeoxynucleotides containing the complementary sequence
    • R.S. Quartin Robin S. and J.G. Wetmur James G. (1989) Effect of ionic strength on the hybridization of oligodeoxynucleotides with reduced charge due to methylphosphonate linkages to unmodified oligodeoxynucleotides containing the complementary sequence. Biochemistry 28 1040-1047.
    • (1989) Biochemistry , vol.28 , pp. 1040-1047
    • Quartin, R.S.1    Wetmur, J.G.2
  • 7
    • 0003899358 scopus 로고
    • Nucleic acid hybridization and unconventional bases
    • M.A. Innis, D.H. Gelfand, J.J. Sninsky (Eds), Boston: Academic Press
    • J.G. Wetmur James G. and J.J. Sninsky John J. (1995) Nucleic acid hybridization and unconventional bases. M.A. Innis, D.H. Gelfand, J.J. Sninsky (Eds) PCR Strategies Boston: Academic Press 69-83.
    • (1995) PCR Strategies , pp. 69-83
    • Wetmur, J.G.1    Sninsky, J.J.2
  • 8
    • 0017085802 scopus 로고
    • A colony bank containing synthetic ColE1 hybrid plasmids representative of the entire E. coli genome
    • L. Clark and J. Carbon (1976) A colony bank containing synthetic ColE1 hybrid plasmids representative of the entire E. coli genome. Cell 9 91.
    • (1976) Cell , vol.9 , pp. 91
    • Clark, L.1    Carbon, J.2
  • 10
    • 0016837953 scopus 로고
    • Ligation of EcoR I endonuclease-generated DNA fragments into linear and circular structures
    • A. Dugaiczyk, H.W. Boyer and H.M. Goodman (1975) Ligation of EcoR I endonuclease-generated DNA fragments into linear and circular structures. J. Mol. Biol. 96 174-184.
    • (1975) J. Mol. Biol. , vol.96 , pp. 174-184
    • Dugaiczyk, A.1    Boyer, H.W.2    Goodman, H.M.3
  • 11
    • 0015228646 scopus 로고
    • Chromatid structure: relationship between DNA content and nucleotide sequence diversity
    • C.D. Laird (1971) Chromatid structure: relationship between DNA content and nucleotide sequence diversity. Chromosoma 32 378.
    • (1971) Chromosoma , vol.32 , pp. 378
    • Laird, C.D.1
  • 12
    • 0017848516 scopus 로고
    • Extracellular nucleases of pseudomonad Bal31 III. Use of the double-strand deoxyriboexonuclease activity as the basis of a convenient method for mapping fragments of DNA produced by cleavage with restriction enzymes
    • R.J. Legersky, J.L. Hodnett and H.B. Gray Jr. (1978) Extracellular nucleases of pseudomonad Bal31 III. Use of the double-strand deoxyriboexonuclease activity as the basis of a convenient method for mapping fragments of DNA produced by cleavage with restriction enzymes. Nucl. Acids Res. 5 1445.
    • (1978) Nucl. Acids Res. , vol.5 , pp. 1445
    • Legersky, R.J.1    Hodnett, J.L.2    Gray, H.B.3
  • 14
    • 0023552653 scopus 로고
    • Oligonucleotide probes for the screening of recombinant DNA libraries
    • B.R. Wallace and C.G. Miyada (1987) Oligonucleotide probes for the screening of recombinant DNA libraries. Meth. Enzymol. 152 432.
    • (1987) Meth. Enzymol. , vol.152 , pp. 432
    • Wallace, B.R.1    Miyada, C.G.2
  • 15
    • 0018787038 scopus 로고
    • Hybridization of synthetic oligodeoxyribonucleotides to X174 DNA: the effect of single base pair mismatch
    • B.R. Wallace, J. Shaffer, R.C. Murphy, J. Bonner, T. Hirose and K. Itakura (1979) Hybridization of synthetic oligodeoxyribonucleotides to X174 DNA: the effect of single base pair mismatch. Nucl. Acids Res. 6 3543.
    • (1979) Nucl. Acids Res. , vol.6 , pp. 3543
    • Wallace, B.R.1    Shaffer, J.2    Murphy, R.C.3    Bonner, J.4    Hirose, T.5    Itakura, K.6
  • 16
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M.M. Bradford (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analyt. Biochem. 72 248.
    • (1976) Analyt. Biochem. , vol.72 , pp. 248
    • Bradford, M.M.1
  • 18
    • 0020435972 scopus 로고
    • Recombinant genomes which express chloramphenicol acetyltransferase in mammalian cells
    • C.M. Gorman, L.F. Moffat and B.H. Howard (1982) Recombinant genomes which express chloramphenicol acetyltransferase in mammalian cells. Molec. Cell. Biol. 2 1044-1051.
    • (1982) Molec. Cell. Biol. , vol.2 , pp. 1044-1051
    • Gorman, C.M.1    Moffat, L.F.2    Howard, B.H.3
  • 19
    • 84882122333 scopus 로고
    • Uses of fusion genes in mammalian transfection: harvest and assay for chloramphenicol acetyltransferase
    • F.M. Ausubel, R. Brent, R.E. Kingston, D.D. Moore, J.G. Seidman, J.A. Smith, K. Struhl, P. Wang-Iverson, S.G. Bonitz (Eds), Cold Spring Harbor, N.Y.: Wiley
    • R.E. Kingston (1989) Uses of fusion genes in mammalian transfection: harvest and assay for chloramphenicol acetyltransferase. F.M. Ausubel, R. Brent, R.E. Kingston, D.D. Moore, J.G. Seidman, J.A. Smith, K. Struhl, P. Wang-Iverson, S.G. Bonitz (Eds) Short Protocols in Molecular Biology: A Compendium of Methods from Current Protocols in Molecular Biology Cold Spring Harbor, N.Y.: Wiley 268-270.
    • (1989) Short Protocols in Molecular Biology: A Compendium of Methods from Current Protocols in Molecular Biology , pp. 268-270
    • Kingston, R.E.1
  • 21
    • 77957012032 scopus 로고
    • Spectrophotometric and turbidimetric methods for measuring proteins
    • E. Layne (1957) Spectrophotometric and turbidimetric methods for measuring proteins. Meth. Enzymol. 3 447-454.
    • (1957) Meth. Enzymol. , vol.3 , pp. 447-454
    • Layne, E.1
  • 22
    • 0003785155 scopus 로고
    • Boca Raton, FL: Cold Spring Harbor Laboratory
    • J.H. Miller (1972) Experiments in Molecular Genetics. Boca Raton, FL: Cold Spring Harbor Laboratory 352-355.
    • (1972) Experiments in Molecular Genetics , pp. 352-355
    • Miller, J.H.1
  • 23
    • 0020669405 scopus 로고
    • Determination of total protein
    • G.L. Peterson (1983) Determination of total protein. Meth. Enzymol. 91 95-119.
    • (1983) Meth. Enzymol. , vol.91 , pp. 95-119
    • Peterson, G.L.1
  • 25
    • 0016160429 scopus 로고
    • Measurement of protein by spectrophotometry at 205 nm
    • R.K. Scopes (1974) Measurement of protein by spectrophotometry at 205 nm. Analyt. Biochem. 59 277-282.
    • (1974) Analyt. Biochem. , vol.59 , pp. 277-282
    • Scopes, R.K.1
  • 26
    • 0014239874 scopus 로고
    • Characterization of chloramphenicol acetyltransferase from chloramphenicol-resistant Staphylococcus aureus
    • W.V. Shaw and R.F. Brodsky (1968) Characterization of chloramphenicol acetyltransferase from chloramphenicol-resistant Staphylococcus aureus. J. Bacteriol. 95 28-36.
    • (1968) J. Bacteriol. , vol.95 , pp. 28-36
    • Shaw, W.V.1    Brodsky, R.F.2
  • 27
    • 0018611787 scopus 로고
    • Primary structure of a chloramphenicol acetyltransferase specified by R plasmids
    • W.V. Shaw, L.C. Packman, B.D. Burleigh, A. Dell, H.R. Morris and B.S. Hartley (1979) Primary structure of a chloramphenicol acetyltransferase specified by R plasmids. Nature 282 870-872.
    • (1979) Nature , vol.282 , pp. 870-872
    • Shaw, W.V.1    Packman, L.C.2    Burleigh, B.D.3    Dell, A.4    Morris, H.R.5    Hartley, B.S.6
  • 28
    • 0024297305 scopus 로고
    • A continuous cell-free translation system capable of producing polypeptides in high yield
    • A.S. Spirin, V.I. Baranov, L.A. Ryabova, S.Y. Ovodov and Y.B. Alakhov (1988) A continuous cell-free translation system capable of producing polypeptides in high yield. Science 242 1162.
    • (1988) Science , vol.242 , pp. 1162
    • Spirin, A.S.1    Baranov, V.I.2    Ryabova, L.A.3    Ovodov, S.Y.4    Alakhov, Y.B.5
  • 29
    • 0025211779 scopus 로고
    • Quantitation of protein
    • C.M. Stoscheck (1990) Quantitation of protein. Meth. Enzymol. 182 50-68.
    • (1990) Meth. Enzymol. , vol.182 , pp. 50-68
    • Stoscheck, C.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.