Journal ArticleDOI
A rapid method for removal of [125I]iodide following iodination of protein solutions.
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TLDR
A simple, highly effective, and rapid method for the removal of iodide following iodination of protein solutions is described, with an advantage of the confinement of radioactive waste to small easily disposable tubes.About:
This article is published in Analytical Biochemistry.The article was published on 1980-07-15. It has received 137 citations till now. The article focuses on the topics: Iodide.read more
Citations
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Journal ArticleDOI
A new solid-state reagent to iodinate proteins. I. Conditions for the efficient labeling of antiserum.
TL;DR: A new solid-state reagent for iodinating polypeptides and proteins was used to radiolabel antiporcine insulin antiserum which retained its immunological ability to recognize insulin.
Journal ArticleDOI
The transforming growth factor-β system, a complex pattern of cross-reactive ligands and receptors
Sela Cheifetz,James A. Weatherbee,Monica L.-S. Tsang,Jacqueline K. Anderson,John E. Mole,Roger C. Lucas,Joan Massagué +6 more
TL;DR: A new homodimer form of transforming growth factor-beta, TGF-beta 2, has been identified in porcine blood platelets and could provide flexibility to the regulation of tissue growth and differentiation by the T GF-beta system.
Journal ArticleDOI
Protein-resistant surfaces prepared by PEO-containing block copolymer surfactants.
TL;DR: The data presented indicate that adsorption of the surfactants on LDPE is dependent on the molecular geometry of theSurfactants suitable for the preparation of PEO-rich surfaces and possible mechanisms for their protein resistance are discussed.
Journal ArticleDOI
ATP-dependent unwinding of messenger RNA structure by eukaryotic initiation factors
B K Ray,T G Lawson,J C Kramer,M. H. Cladaras,J A Grifo,R D Abramson,William C. Merrick,Robert E. Thach +7 more
TL;DR: The results suggest that the unwinding activity of eIF-4F is located in the 46,000-dalton polypeptide of this complex, which has shown by others to be similar or identical to eif-4A.
Journal ArticleDOI
Primary structure and cellular localization of chicken brain myosin-V (p190), an unconventional myosin with calmodulin light chains.
Enilza Maria Espreáfico,Richard E. Cheney,Michela Matteoli,A A C Nascimento,P De Camilli,Roy E. Larson,Mark S. Mooseker +6 more
TL;DR: The p190-CM complex, named "myosin-V", is a novel structural class of unconventional myosins that includes the gene products encoded by the dilute locus of mouse and the MYO2 gene of Saccharomyces cerevisiae and an unusual distribution for this myosin in both neurons and nonneuronal cells is revealed.
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.
Journal ArticleDOI
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
TL;DR: Using an improved method of gel electrophoresis, many hitherto unknown proteins have been found in bacteriophage T4 and some of these have been identified with specific gene products.
Journal Article
Cleavage of structural proteins during the assemble of the head of bacterio-phage T4
TL;DR: Using an improved method of gel electrophoresis, many hitherto unknown proteins have been found in bacteriophage T4 and some of these have been identified with specific gene products as mentioned in this paper.
Journal ArticleDOI
The labelling of proteins to high specific radioactivities by conjugation to a 125I-containing acylating agent. Application to the radioimmunoassay
A. E. Bolton,William M. Hunter +1 more
TL;DR: With some antisera the immunoreactivity of the antigen was diminished by the introduction of a single I atom into the tyrosyl groups, whereas antigen containing a single (125)I-labelled 3-(4-hydroxyphenyl)propionamide group showed the same immunore activity as the unmodified antigen.
Journal ArticleDOI
Reversible binding of Pi by beef heart mitochondrial adenosine triphosphatase.
TL;DR: Aurovertin, an inhibitor of oxidative phosphorylation, enhanced Pi binding via a 4-fold increase in the affinity of the enzyme for Pi (KD = 20 micronM) but did not alter binding stoichiometry.
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