메뉴 건너뛰기




Volumn 18, Issue 1, 1997, Pages 111-123

A procedure for the detection of free thiol-containing proteins on a polyvinylidene difluoride membrane

Author keywords

BSA; membrane biotinylation; PVDF; thiol

Indexed keywords

BIOTIN DERIVATIVE; BOVINE SERUM ALBUMIN; POLYVINYLIDENE FLUORIDE; PROTEIN; THIOL DERIVATIVE;

EID: 0031046246     PISSN: 01971522     EISSN: None     Source Type: Journal    
DOI: 10.1080/01971529708005807     Document Type: Article
Times cited : (1)

References (18)
  • 1
    • 0026487591 scopus 로고
    • A Brief Survey of Methods for Preparing Protein Conjugates with Dyes, Haptens, and Cross-Linking Reagents
    • Brinkley, M. A Brief Survey of Methods for Preparing Protein Conjugates with Dyes, Haptens, and Cross-Linking Reagents. Bioconjug. Chem. 1992; 3: 2-13.
    • (1992) Bioconjug. Chem. , vol.3 , pp. 2-13
    • Brinkley, M.1
  • 2
    • 0029087071 scopus 로고
    • Influence of the Antibody-Peroxidase Coupling Methods on the Conjugates Stability and on the Methodologies for the Preservation of the Activity in Time
    • Presentini, R. and Terrana, B. Influence of the Antibody-Peroxidase Coupling Methods on the Conjugates Stability and on the Methodologies for the Preservation of the Activity in Time. J. Immunoassay 1995; 16: 309-24.
    • (1995) J. Immunoassay , vol.16 , pp. 309-324
    • Presentini, R.1    Terrana, B.2
  • 3
    • 0029560307 scopus 로고
    • P-Azidoiodoacetanilide, a New Short Photocrosslinker that Has Greater Cysteine Specificity than p-Azidophenacyl Bromide and p-Azidobromcaceuanilide
    • Zhang, J., Lee, M.H. and Walker, G.C. p-Azidoiodoacetanilide, a New Short Photocrosslinker that Has Greater Cysteine Specificity than p-Azidophenacyl Bromide and p-Azidobromcaceuanilide. Biochem. Biophys. Res. Commun. 1995; 217: 1177-84.
    • (1995) Biochem. Biophys. Res. Commun. , vol.217 , pp. 1177-1184
    • Zhang, J.1    Lee, M.H.2    Walker, G.C.3
  • 4
    • 0028973541 scopus 로고
    • Control of Protein-Ligand Recognition Using a Stimuli-Responsive Polymer
    • Stayton, P.S., Shimoboji, T., Long, C. et al. Control of Protein-Ligand Recognition Using a Stimuli-Responsive Polymer. Nature 1995; 378: 472-4.
    • (1995) Nature , vol.378 , pp. 472-474
    • Stayton, P.S.1    Shimoboji, T.2    Long, C.3
  • 5
    • 0029130715 scopus 로고
    • The Agonist Binding Site on the Bovine Bradykinin B2 Receptor is Adjacent to a Sulfhydryl and is Differentiated from the Antagonist Binding Site by Chemical Cross-Linking
    • Herzig, M.C.S. and Leeb-Lundberg, L.M.F. The Agonist Binding Site on the Bovine Bradykinin B2 Receptor Is Adjacent to a Sulfhydryl and Is Differentiated from the Antagonist Binding Site by Chemical Cross-Linking. J. Biol. Chem. 1995; 270: 20591-8.
    • (1995) J. Biol. Chem. , vol.270 , pp. 20591-20598
    • Herzig, M.C.S.1    Leeb-Lundberg, L.M.F.2
  • 6
    • 0028846457 scopus 로고
    • The Erbstatin Analogue Methyl 2,5-Dihydroxycinnamate Cross-Links Proteins and is Cytotoxic to Normal and Neoplastic Epithelial Cells by a Mechanism Independent of Tyrosine Kinase Inhibition
    • Stanwell, C., Burke, Jr., T.R. and Yuspa, S.H. The Erbstatin Analogue Methyl 2,5-Dihydroxycinnamate Cross-Links Proteins and Is Cytotoxic to Normal and Neoplastic Epithelial Cells by a Mechanism Independent of Tyrosine Kinase Inhibition. Cancer Res. 1995; 55: 4950-6.
    • (1995) Cancer Res. , vol.55 , pp. 4950-4956
    • Stanwell, C.1    Burke T.R., Jr.2    Yuspa, S.H.3
  • 7
    • 0028923790 scopus 로고
    • Conjugation to Preactivated Proteins Using Divinylsulfone and lodoacetic Acid
    • Houen, G. and Jensen, O.M. Conjugation to Preactivated Proteins Using Divinylsulfone and lodoacetic Acid. J. Immunol. Methods 1995; 181: 187-200.
    • (1995) J. Immunol. Methods , vol.181 , pp. 187-200
    • Houen, G.1    Jensen, O.M.2
  • 8
    • 0028845475 scopus 로고
    • A Method for Preparing Chelate-Cytokine Conjugates with Retention of Protein Structure, Biological Activity, and Pharmacokinetic Properties
    • Litzinger, D.C., Ransone, C.M., Ralph, L.D. et al. A Method for Preparing Chelate-Cytokine Conjugates with Retention of Protein Structure, Biological Activity, and Pharmacokinetic Properties. J. Immunol. Methods 1995; 187: 151-61.
    • (1995) J. Immunol. Methods , vol.187 , pp. 151-161
    • Litzinger, D.C.1    Ransone, C.M.2    Ralph, L.D.3
  • 9
    • 0022556066 scopus 로고
    • Coating of Liposomes with Subunits of Monoclonal IgM Antibody and Targeting of the Liposomes
    • Hashimoto, Y., Sugawara, M., Kamiya, T. and Suzuki, S. Coating of Liposomes with Subunits of Monoclonal IgM Antibody and Targeting of the Liposomes. Methods Enzymol. 1986; 121: 817-28.
    • (1986) Methods Enzymol. , vol.121 , pp. 817-828
    • Hashimoto, Y.1    Sugawara, M.2    Kamiya, T.3    Suzuki, S.4
  • 11
    • 0025281379 scopus 로고
    • Introduction to Avidin-Biotin Technology
    • Wilchek, M. and Bayer, E.A. Introduction to Avidin-Biotin Technology. Methods Enzymol. 1990; 184: 5-13.
    • (1990) Methods Enzymol. , vol.184 , pp. 5-13
    • Wilchek, M.1    Bayer, E.A.2
  • 12
    • 0028797277 scopus 로고
    • A One-Step Procedure for Biotinylation and Chemical Cross-Linking of Lymphocyte Surface and Intracellular Membrane-Associated Molecules
    • Altin, J.G. and Pagler, E.B. A One-Step Procedure for Biotinylation and Chemical Cross-Linking of Lymphocyte Surface and Intracellular Membrane-Associated Molecules. Anal. Biochem. 1995; 224: 382-9.
    • (1995) Anal. Biochem. , vol.224 , pp. 382-389
    • Altin, J.G.1    Pagler, E.B.2
  • 13
    • 0005345696 scopus 로고
    • Biothiols: Monothiols and Dithiols, Protein Thiols, and Thiyl Radicals
    • Packer, L., ed. Biothiols: Monothiols and Dithiols, Protein Thiols, and Thiyl Radicals. Methods Enzymol. 1995; 251.
    • (1995) Methods Enzymol. , vol.251
    • Packer, L.1
  • 15
    • 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: 680-5.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 16
    • 0009482260 scopus 로고
    • Electrophoretic Transfer of Proteins from Polyacrylamide Gels to Nitrocellulose Sheets: Procedure and some Applications
    • Towbin, H., Staehelin, T. and Gordon, J. Electrophoretic Transfer of Proteins from Polyacrylamide Gels to Nitrocellulose Sheets: Procedure and some Applications. Proc. Natl. Acad. Sci. U.S.A. 1979: 76: 4350-4.
    • (1979) Proc. Natl. Acad. Sci. U.S.A. , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 17
    • 0029006929 scopus 로고
    • An Assay for Detecting Nanogram Levels of Proteolytic Enzymes
    • Koritsas, V.M. and Atkinson, H.J. An Assay for Detecting Nanogram Levels of Proteolytic Enzymes. Anal. Biochem. 1995; 227: 22-6.
    • (1995) Anal. Biochem. , vol.227 , pp. 22-26
    • Koritsas, V.M.1    Atkinson, H.J.2
  • 18
    • 0027303654 scopus 로고
    • A Solid-Phase Protein Assay: Quantitation of Protein in the Nanogram Range
    • Sulter, M.W., Kloosterhuis, G.J., Coenraads, P-J. and Pas, H.H. A Solid-Phase Protein Assay: Quantitation of Protein in the Nanogram Range. Anal. Biochem. 1993; 211: 301-4.
    • (1993) Anal. Biochem. , vol.211 , pp. 301-304
    • Sulter, M.W.1    Kloosterhuis, G.J.2    Coenraads, P.-J.3    Pas, H.H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.