๐”– Bobbio Scriptorium
โœฆ   LIBER   โœฆ

Measurement of protein in cell suspensions using the Commassie brilliant blue dye-binding assay

โœ Scribed by Geir O. Gogstad; May-Britt Krutnes


Publisher
Elsevier Science
Year
1982
Tongue
English
Weight
381 KB
Volume
126
Category
Article
ISSN
0003-2697

No coin nor oath required. For personal study only.

โœฆ Synopsis


The direct measurement of protein in cell suspensions using the Coomassie brilliant blue dyebinding assay demonstrated markedly lower values compared to those obtained with the Lowry assay. It is shown that the addition of small amounts of Triton X-100 or NaOH to the cell suspensions prior to addition of the dye reagent corrected this discrepancy. Standards of soluble proteins may be used for the quantitation of protein in cell suspensions with the dyebinding assay provided that the same amounts of Triton X-100 or NaOH are added to both the standards and the samples.


๐Ÿ“œ SIMILAR VOLUMES


Mechanism of Dye Binding in the Protein
โœ A.A. Waheed; K.Sridhar Rao; P.D. Gupta ๐Ÿ“‚ Article ๐Ÿ“… 2000 ๐Ÿ› Elsevier Science ๐ŸŒ English โš– 97 KB

Eosin B and eosin Y have been used to estimate micro- and submicrogram quantities of proteins respectively as shown in our previous reports. In the present study we describe the mechanism of eosin binding to proteins. At pH lower than 3.0 the absorbance of unbound dye is greatly reduced. After the d

Plasma (1โ†’3)-ฮฒ-D-glucan assay and immuno
โœ Hiroshi Tamura; Shigenori Tanaka; Teruo Ikeda; Taminori Obayashi; Yohichi Hashim ๐Ÿ“‚ Article ๐Ÿ“… 1997 ๐Ÿ› John Wiley and Sons ๐ŸŒ English โš– 95 KB ๐Ÿ‘ 1 views

A highly sensitive enzyme-linked immunosorbent assay specific to (1โ†’3)-ฮฒ-Dglucans (GBP-ELISA) has been developed using a novel (1โ†’3)-ฮฒ-D-glucan-binding protein (T-GBP), which was purified from the amebocyte lysate of the Japanese horseshoe crab, Tachypleus tridentatus. This method allowed quantitati