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Rose J. Randall

Bio: Rose J. Randall is an academic researcher from Washington University in St. Louis. The author has contributed to research in topics: Folin–Ciocalteu reagent & Protein iodination. The author has an hindex of 1, co-authored 1 publications receiving 285427 citations.

Papers
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Journal Article
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.

289,852 citations


Cited by
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Journal ArticleDOI
TL;DR: This assay is very reproducible and rapid with the dye binding process virtually complete in approximately 2 min with good color stability for 1 hr with little or no interference from cations such as sodium or potassium nor from carbohydrates such as sucrose.

225,085 citations

PatentDOI
TL;DR: This new method maintains the high sensitivity and low protein-to-protein variation associated with the Lowry technique and demonstrates a greater tolerance of the bicinchoninate reagent toward such commonly encountered interferences as nonionic detergents and simple buffer salts.

20,907 citations

Journal ArticleDOI
TL;DR: The purification of homogeneous glutathione S-transferases B and C from rat liver is described, and only transferases A and C are immunologically related.

16,953 citations

Journal ArticleDOI
Tsuneo Omura1, Ryo Sato1
TL;DR: The present paper gives a detailed account of the investigations on rabbit liver microsomes and crude microsomal digests, which have led to postulate the hemoprotein nature of the pigment.

11,895 citations

Journal ArticleDOI
TL;DR: The loss of immunological reactivity at high specific radioactivities or at high levels of chemical substitution with STAI/sup 127/!iodine is demonstrated.
Abstract: A simple and rapid method is presented for the preparation of I/sup 131/- labeled human growth hormone of high specific radioactivity (240-300 mu C/ mu g). Low amounts of carrierfree I/sup 131/ iodide (2 mC) are allowed to react, without prior treatment, with small quantities of protein (5 mu g) in a highyield reaction (approx. 70% transfer of I/sup 131/ to protein). The degree of chemical substitution is minimized (0.5- 1.0 atom of iodine/molecule of protein) by the use of carrier-free I/sup 131/ iodide. The I/sup 131/-labeled hormone (up to 300 mu C/ mu g) contains no detectable degradation products and is immunologically identical with the unlabeled hormone. The loss of immunological reactivity at high specific radioactivities or at high levels of chemical substitution with STAI/sup 127/!iodine is demonstrated. (auth)

10,047 citations