Avidin and streptavidin.

Publisher Summary This chapter discusses the fundamental molecular properties of avidin and streptavidin. Carbohydrate-free avidin can be obtained by use of deglycosylating enzymes and it has been shown to be present in significant amounts in some commercial preparations from which it may be separated by use of lectin columns. Improvement on the original use of biotinyl cellulose came with the introduction of iminobiotinyl derivatives of Sepharose that utilized the pH dependence of the binding 24 to achieve efficient elution. In iminobiotin, the ureido group becomes a guanidinium group; the form in which this is uncharged is strongly bound. The gene for streptavidin has been cloned and sequenced with the ultimate objective of using it in general expression systems for detecting and isolating fusion proteins. The stability is greatly enhanced by biotin binding, because the total free energy of binding is about 330 kJ/mol of tetramer. The dissociation constant for biotin is so low that it can be estimated only from the ratio of the rate constants for binding and exchange. The binding is accompanied by a red shift of the tryptophan spectrum and by a decrease in fluorescence, either of which can be used as the basis for quantitative assays.

[1]  E. Titchener,et al.  Evidence for the participation of biotin in the enzymic synthesis of fatty acids. , 1958, Biochimica et biophysica acta.

[2]  R. Williams,et al.  Raman spectroscopy of avidin: secondary structure, disulfide conformation, and the environment of tyrosine. , 1982, Biochemistry.

[3]  P. Kraulis,et al.  The structure of β-lactoglobulin and its similarity to plasma retinol-binding protein , 1986, Nature.

[4]  M. Lane,et al.  Homogeneous functional insulin receptor from 3T3-L1 adipocytes. Purification using N alpha B1-(biotinyl-epsilon-aminocaproyl)insulin and avidin-sepharose. , 1985, The Journal of biological chemistry.

[5]  R. Raff,et al.  A sea urchin gene encodes a polypeptide homologous to epidermal growth factor. , 1987, Science.

[6]  N. Green,et al.  The use of bifunctional biotinyl compounds to determine the arrangement of subunits in avidin. , 1971, The Biochemical journal.

[7]  M. Wilchek,et al.  The avidin-biotin complex in bioanalytical applications. , 1988, Analytical biochemistry.

[8]  H. Fraenkel-conrat,et al.  Avidin. II. Composition and mode of action of avidin A. , 1952, Archives of biochemistry and biophysics.

[9]  J. Gershoni,et al.  Biotin binding to avidin. Oligosaccharide side chain not required for ligand association. , 1987, The Biochemical journal.

[10]  C. Cantor,et al.  Molecular cloning and nucleotide sequence of the streptavidin gene. , 1986, Nucleic acids research.

[11]  M. Wilchek,et al.  Studies on the biotin-binding site of avidin. Lysine residues involved in the active site. , 1988, The Biochemical journal.

[12]  S. Camper,et al.  Biotin-binding protein from egg yolk. A protein distinct from egg white avidin. , 1978, The Journal of biological chemistry.

[13]  G. Nicolson,et al.  Immunoaffinity isolation of membrane antigens with biotinylated monoclonal antibodies and immobilized streptavidin matrices. , 1984, Journal of immunological methods.

[14]  K. Hofmann,et al.  Avidin binding of carboxyl-substituted biotin and analogues. , 1982, Biochemistry.

[15]  D. B. Mccormick,et al.  Specific purification of avidin by column chromatography on biotin-cellulose. , 1965, Analytical biochemistry.

[16]  M. Wilchek,et al.  p-Diazobenzoyl-biocytin: a new biotinylating reagent for DNA. , 1988, Nucleic acids research.

[17]  F. J. Wolf,et al.  THE PROPERTIES OF STREPTAVIDIN, A BIOTIN-BINDING PROTEIN PRODUCED BY STREPTOMYCETES. , 1964, Archives of biochemistry and biophysics.

[18]  M. Kulomaa,et al.  Kinetics of avidin induction by tissue injury and inflammation in chicks and the dependence of induction on protein and RNA synthesis , 1981 .

[19]  N M Green,et al.  Thermodynamics of the binding of biotin and some analogues by avidin. , 1966, The Biochemical journal.

[20]  K. Hofmann,et al.  Hormone-receptor studies with avidin and biotinylinsulin-avidin complexes. , 1980, The Journal of biological chemistry.

[21]  P. Adiga,et al.  Purification of biotin-binding protein from chicken egg yolk and comparison with avidin. , 1984, Biochimica et biophysica acta.

[22]  P. A. Peterson,et al.  The three‐dimensional structure of retinol‐binding protein. , 1984, The EMBO journal.

[23]  R. C. Bruch,et al.  Compositional and structural heterogeneity of avidin glycopeptides. , 1982, Biochemistry.

[24]  J. Wallace,et al.  Pyruvate carboxylase from Saccharomyces cerevisiae. Quaternary structure, effects of allosteric ligands and binding of avidin. , 1986, European journal of biochemistry.

[25]  M. Wilchek,et al.  An improved method for the single-step purification of streptavidin. , 1986, Journal of biochemical and biophysical methods.

[26]  K. Yamamoto,et al.  Effect of avidin binding to SH1 on the interface between subfragment-1 and F-actin. , 1987, Journal of biochemistry.

[27]  N. Green,et al.  Optical rotatory dispersion, circular dichroism and far-ultraviolet spectra of avidin and streptavidin. , 1966, The Biochemical journal.

[28]  B. Maliwal,et al.  Effect of ligand binding and conformational changes in proteins on oxygen quenching and fluorescence depolarization of tryptophan residues. , 1984, Biophysical Chemistry.

[29]  Molecular cloning of the chicken avidin cDNA. , 1987, Nucleic acids research.

[30]  N. Green,et al.  Transcarboxylase. XI. Electron microscopy and subunit structure. , 1972, The Journal of biological chemistry.

[31]  J. Wallace,et al.  Localisation of the active site of pyruvate carboxylase by electron microscopic examination of avidin-enzyme complexes. , 1983, European journal of biochemistry.

[32]  J. Gordon,et al.  The structure of crystalline Escherichia coli-derived rat intestinal fatty acid-binding protein at 2.5-A resolution. , 1988, The Journal of biological chemistry.

[33]  K. Hofmann,et al.  Avidin binding of biotinylated corticotropins. , 1983, Biochemistry.

[34]  J Godovac-Zimmermann,et al.  The structural motif of beta-lactoglobulin and retinol-binding protein: a basic framework for binding and transport of small hydrophobic molecules? , 1988, Trends in biochemical sciences.

[35]  R. Huber,et al.  Crystallization, crystal structure analysis and preliminary molecular model of the bilin binding protein from the insect Pieris brassicae. , 1987, Journal of molecular biology.

[36]  P. A. Peterson,et al.  The primary structure of bovine cellular retinoic acid-binding protein. , 1985, The Journal of biological chemistry.

[37]  K. Hofmann,et al.  Ligands for insulin receptor isolation. , 1984, Biochemistry.

[38]  M. Wilchek,et al.  The use of the avidin-biotin complex as a tool in molecular biology. , 2006, Methods of biochemical analysis.

[39]  R. Giese,et al.  Avidin binding of radiolabeled biotin derivatives. , 1988, Journal of Biological Chemistry.

[40]  P. Dimroth.  Purification of the sodium transport enzyme oxaloacetate decarboxylase by affinity chromatography on avidin sepharose , 1982, FEBS letters.

[41]  S. Lavielle,et al.  Avidin binding of biotinylated analogues of substance P. , 1983, Biochimica et Biophysica Acta.

[42]  W. Maloy,et al.  An avidin monomer affinity column for the purification of biotin-containing enzymes. , 1979, Analytical biochemistry.

[43]  N. Green,et al.  The properties of subunits of avidin coupled to sepharose. , 1973, The Biochemical journal.

[44]  J. Wendoloski,et al.  Structural origins of high-affinity biotin binding to streptavidin. , 1989, Science.