๐”– Bobbio Scriptorium
โœฆ   LIBER   โœฆ

A sensitive fluorometric assay for avidin and biotin

โœ Scribed by Henry J. Lin; Jack F. Kirsch


Publisher
Elsevier Science
Year
1977
Tongue
English
Weight
252 KB
Volume
81
Category
Article
ISSN
0003-2697

No coin nor oath required. For personal study only.

โœฆ Synopsis


The quenching of the tryptophan fluorescence of avidin by biotin forms the basis for a rapid, sensitive assay for biotin and avidin in solutions free of fluorescent contaminants. Avidin solutions are assayed by titration with a standard biotin solution until no further decrease in fluorescence at 350 nm, with excitation at 290 nm. is observed. Unknown quantities of biotin in solution may be determined by titration with aliquots of standard avidin until the change in fluorescence observed following each addition undergoes a sharp increase. As little as 20 ng of biotin may be measured in this way.


๐Ÿ“œ SIMILAR VOLUMES


Sensitive fluorometric assay for leghemo
โœ T.A. LaRue; J.J. Child ๐Ÿ“‚ Article ๐Ÿ“… 1979 ๐Ÿ› Elsevier Science ๐ŸŒ English โš– 371 KB

A sensitive spectrofluorometric assay for leghemoglobin is based upon the action of hot saturated oxalic acid on heme proteins. The assay will detect 200 ng of leghemoglobin per milliliter I National Research Council of Canada No. 17110.

A Sensitive Fluorometric Assay for Tissu
โœ Thomas M. Jeitner; Hans-Lothar Fuchsbauer; John P. Blass; Arthur J.L. Cooper ๐Ÿ“‚ Article ๐Ÿ“… 2001 ๐Ÿ› Elsevier Science ๐ŸŒ English โš– 104 KB

We have devised a highly sensitive fluorometric well plate assay for tissue transglutaminase that is suitable for multiple kinetic analyses/high-throughput screening of chemical inventories for inhibitors of this enzyme. The procedure measures the rate of fluorescence enhancement ( exc 260 nm, em 53

A simple and sensitive fluorometric assa
โœ Takashi Yamauchi; Hitoshi Fujisawa ๐Ÿ“‚ Article ๐Ÿ“… 1978 ๐Ÿ› Elsevier Science ๐ŸŒ English โš– 419 KB

A simple, rapid, and sensitive fluorometric assay for measuring the activity of tyrosine hydroxylase is described. The enzyme activity is detected by converting tyrosine to 3,4-dihydroxyphenylalanine (dopa), which is then subjected to conversion to the highly fluorescent product by the trihydroxyind