Journal ArticleDOI
Assay of proteins in the presence of interfering materials.
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TLDR
The Lowry protein assay is a sensitive but highly nonspecific procedure that has been modified so that protein can be assayed in the presence of interfering chemicals.About:
This article is published in Analytical Biochemistry.The article was published on 1976-01-01. It has received 3135 citations till now. The article focuses on the topics: Lowry protein assay & Bicinchoninic acid assay.read more
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Ubiquitin Stress Response in Postischemic Hippocampal Neurons under Nontolerant and Tolerant Conditions
Takafumi Ide,Koji Takada,Jian Hua Qiu,Nobuhito Saito,Nobutaka Kawahara,Akio Asai,Takaaki Kirino +6 more
TL;DR: Under tolerant conditions, subsequent ischemia in the CA1 region induces the stress response of ubiquitin up to the translational level, leading to the rapid restoration of protein synthesis and to eventual neuronal survival.
Journal ArticleDOI
A new approach for the detection of multiple protein kinases using monoclonal antibodies directed to the highly conserved region of protein kinases.
Isamu Kameshita,Toshiyuki Tsuge,Tomoko Kinashi,Shun Kinoshita,Noriyuki Sueyoshi,Atsuhiko Ishida,Shigeru Taketani,Yasushi Shigeri,Yoshiro Tatsu,Noboru Yumoto,Katsuichiro Okazaki +10 more
TL;DR: Results indicate that the present monoclonal antibodies directed to multiple protein kinases will be a powerful tool for the detection of a variety of known and novel protein Kinase family enzymes expressed in cells.
Journal ArticleDOI
An endogenous factor from soybean (Glycine max L.) cell cultures activates phosphorylation of a protein which is dephosphorylated in vivo in elicitor-challenged cells.
Dorit Grab,M. Feger,Jürgen Ebel +2 more
TL;DR: The effect of the elicitor on protein phosphorylation was tested after labeling of the cells with [32P]orthophosphate and a number of proteins which were radioactively labeled in vivo were also phosphorylated in vitro by endogenous protein-kinase activity in the presence of Ca2+.
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Subcellular localization of a membrane-associated transglutaminase activity in rat liver.
Charles W. Slife,M.Diane Dorsett,Gregory T. Bouquett,Ashley Register,Eldred B Taylor,Scott Conroy +5 more
TL;DR: Fractionation of rat liver by homogenization and differential centrifugation revealed that only about 83% of the transglutaminase activity in the tissue is in a soluble form, and that the remainder is associated with the particulate fraction.
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Hemopexin-mediated heme transport to the liver. Evidence for a heme-binding protein in liver plasma membranes.
A Smith,W T Morgan +1 more
TL;DR: Solubilized HBC was shown to be distinct from hemopexin itself, free heme, ligandin, globin, heme oxygenase, cytochrome P-450, and albumin, and to bind heme that is presented to it in a nonprotein bound form, showing true heme-binding activity.
References
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Journal Article
Protein Measurement with the Folin Phenol Reagent
TL;DR: Procedures are described for measuring protein in solution or after precipitation with acids or other agents, and for the determination of as little as 0.2 gamma of protein.
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Influence of sucrose on protein determination by the Lowry procedure
B. P. Gerhardt,Harry Beevers +1 more
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Interference by detergents, chelating agents, and buffers with the Lowry protein determination.
TL;DR: The effect of succinic acid, sodium citrate, and Bicine on the Lowry method changes depending on the concentration of the chemicals, but the changes were not as significant as in the case of the chemical mentioned above.
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Interferences by sulfhydryl, disulfide reagents and potassium ions on protein determination by Lowry's method.
TL;DR: The concentrations ofulfhydryl, disulfide reagents, and also potassium ions interfere with the protein determination by Lowry's method, but at moderate concentrations this interference can be overcome by running appropriate blanks.