𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Bioluminescent enzyme immunoassay for estriol. Use of reversibly inactivated bacterial luciferase as label

✍ Scribed by Fredrick S. Yein; Charles K. Marschke; Philip C. Deming; Thomas F. Holzman; Paul S. Satoh

Publisher
Elsevier Science
Year
1985
Tongue
English
Weight
562 KB
Volume
149
Category
Article
ISSN
0003-2697

No coin nor oath required. For personal study only.

✦ Synopsis

A bioluminescent enzyme immunoassay using estriol labeled with reversibly inactivated bacterial luciferase is described. An estriol derivative bearing an alkylthiolsulfonate is linked to the cysteinyl thiols of Iuciferase by formation of mixed disuhide linkages; thus, luciferase becomes inactive. After immunoassay, the inactive luciferase of the label bound to the immunoprecipitate is reactivated by incubation with dithiothreitol and the luciferase activity then is quantitated by a 20-s reaction performed with an automated luminometer (LKB 125 I). Under the defined conditions, the labels are stable for at least 14 days as tested at 4Β°C. A standard curve with a wide linear range from 50 to 6000 pg is demonstrated. This unique technology discussed here, therefore, offers exciting possibilities as a sensitive and rapid enzyme immunoassay for estriol. o 1985 Academic Press, Inc.

πŸ“œ SIMILAR VOLUMES

Development of ultra-high sensitivity bi
Development of ultra-high sensitivity bioluminescent enzyme immunoassay for hepatitis B virus surface antigen using firefly luciferase
✍ Takayuki Minekawa; Hiroshi Ohkuma; Katsushi Abe; Hiroaki Maekawa; Hidetoshi Arak πŸ“‚ Article πŸ“… 2009 πŸ› John Wiley and Sons 🌐 English βš– 447 KB πŸ‘ 1 views

## Abstract Hepatitis B virus (HBV) infection continues to be a global public health concern. Efficient diagnosis of HBV surface antigen (HBsAg) is useful for identification of infection, treatment and prevention of transfusion‐transmitted viral infections. Seronegative window reduction afforded by

Selective Inactivation of Eukaryotic Ξ²-G
Selective Inactivation of Eukaryotic Ξ²-Galactosidase in Assays for Inhibitors of HIV-1 TAT Using Bacterial Ξ²-Galactosidase as a Reporter Enzyme
✍ D.C. Young; S.D. Kingsley; K.A. Ryan; F.J. Dutko πŸ“‚ Article πŸ“… 1993 πŸ› Elsevier Science 🌐 English βš– 614 KB

Bacterial \(\beta\)-galactosidase is one of several reporter enzymes used in studying the transcriptional activity of eukaryotic promoters. Although it is one of the easiest and least expensive enzymes to assay, its use has been limited because of its low sensitivity, which is due in part to endogen

Optimal conditions of immune complex tra
Optimal conditions of immune complex transfer enzyme immunoassays for antibody IgGs to HIV-1 using recombinant p17, p24, and reverse transcriptase as antigens
✍ Seiichi Hashida; Setsuko Ishikawa; Kazuya Hashinaka; Ichiro Nishikata; Shinichi πŸ“‚ Article πŸ“… 1998 πŸ› John Wiley and Sons 🌐 English βš– 113 KB πŸ‘ 2 views

The immune complex transfer enzyme immunoassays for antibody IgGs to p17, p24, and reverse transcriptase (RT) of HIV-1 were tested under various conditions. Antibody IgGs to HIV-1 were reacted for up to 20 hr with 2,4dinitrophenyl-bovine serum albumin-recombinant HIV-1 protein conjugates and recombi

Use of inactive Ξ²-d-galactosidase for el
Use of inactive Ξ²-d-galactosidase for elimination of interference by anti-Ξ²-d-galactosidase antibodies in immune complex transfer enzyme immunoassay for anti-thyroglobulin igg in serum using Ξ²-d-galactosidase from escherichia coli as label
✍ Takeyuki Kohno; Dr. Eiji Ishikawa; Hiroyuki Katsumaru; Hidetaka Nakamoto; Taeko πŸ“‚ Article πŸ“… 1991 πŸ› John Wiley and Sons 🌐 English βš– 757 KB

A novel enzyme immunoassay (immune complex transfer enzyme immunoassay) for anti-thyroglobulin IgG using beta-D-galactosidase from Escherichia coli as label was reported previously. This immunoassay was highly sensitive in demonstrating anti-thyroglobulin IgG not only in all patients with Graves' di