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Journal ArticleDOI

Specificity, stereochemistry, and mechanism of the color reaction between p-dimethylaminocinnamalhyde and biotin analogs.

Donald B. McCormick, +1 more
- 01 Mar 1970 - 
- Vol. 34, Iss: 1, pp 226-236
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TLDR
Biotin and other cyclic ureido compounds monoalkylated on each nitrogen have been shown to react with p-dimethylaminocinamaldehyde in anhydrous solution or on dry chromatograms in a classic way for formation of the conjugate imine.
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This article is published in Analytical Biochemistry.The article was published on 1970-03-01. It has received 83 citations till now. The article focuses on the topics: Imine & Biotin.

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Citations
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Journal ArticleDOI

Enzymatic synthesis of biotin-labeled polynucleotides: novel nucleic acid affinity probes

TL;DR: Biotin-labeled polynucleotides, both single and double-stranded, are selectively and quantitatively retained on avidin-Sepharose, even after extensive washing with 8 M urea, 6 M guanidine hydrochloride, or 99% formamide.
Journal ArticleDOI

Non-radioactive hybridization probes prepared by the chemical labelling of DNA and RNA with a novel reagent, photobiotin

TL;DR: The sensitivity of detection of target RNA in dot-blots and Northern blots was equivalent to that obtained with 32p-labelled DNA probes, and photobiotin was also used for the labelling of proteins with biotin.
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Polyacrylamides Bearing Pendant α-Sialoside Groups Strongly Inhibit Agglutination of Erythrocytes by Influenza Virus: The Strong Inhibition Reflects Enhanced Binding through Cooperative Polyvalent Interactions

TL;DR: An ELISA assay is described for measuring the binding of influenza virus A-X31 to α-sialoside groups that are linked to biotin-labeled polyacrylamides, and the role of steric stabilization in the mechanism is shown to be directly related to the binding affinity of the polymers for the viral surface.
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Acetyl Coenzyme A Carboxylase System of Escherichia coli PURIFICATION AND PROPERTIES OF THE BIOTIN CARBOXYLASE, CARBOXYLTRANSFERASE, AND CARBOXYL CARRIER PROTEIN COMPONENTS

TL;DR: The two catalytic components of the E. coli acetyl-CoA carboxylase system are devoid of free or covalently bound biotin yet have the ability to carry out their respective model half-reactions utilizing free d-biotin derivatives in place of carboxy carrier protein.
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Cleavable biotin probes for labeling of biomolecules via azide-alkyne cycloaddition.

TL;DR: Five cleavable biotin probes are described for use in labeling of proteins and other biomolecules via azide-alkyne cycloaddition and a probe constructed around a dialkoxydiphenylsilane (DADPS) linker was found to be cleaved efficiently when treated with 10% HCO(2)H for 0.5 h.
References
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Journal ArticleDOI

Bacterial degradation of biotin. Catabolism of 14C-biotin and its sulfoxides.

TL;DR: A biotin-degrading particulate system has been obtained by sonic rupture of a soil pseudomonad which grows on d-biotin as sole source of carbon, nitrogen, and sulfur and is efficiently catabolized by the particulate preparations and exhibit mutual competition as substrates.
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Bacterial Degradation of Biotin III. METABOLISM OF 14C-CARBONYL-LABELED BIOTIN

TL;DR: These findings establish that the side chain of biotin is degraded by β-oxidation with loss of 2 acetate units, and that after the complete degradation of the side Chain, oxidation of both carbons bridging the ureido to thiophane rings occurs, producing urea which is degraded to CO2 and NH3 by urease.
Journal ArticleDOI

Possible Biochemical Implications of the Crystal Structure of Biotin

TL;DR: An examination of the molecular architecture of biotin, as determined by x-ray crystallographic analysis, has indicated that biotin may be capable of forming an intramolecular hydrogen bond in solution.
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Bacterial Degradation of Biotin II. CATABOLISM OF 14C-HOMOBIOTIN AND 14C-NORBIOTIN

TL;DR: Findings indicate the presence of a β oxidative system which catalyzes the degradation of the side chain of biotin as well as of several biotin analogues.
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