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Journal ArticleDOI

Proteolytic digestion of erythrocytes, resealed ghosts, and isolated membranes

Richard B. Triplett, +1 more
- 18 Jul 1972 - 
- Vol. 11, Iss: 15, pp 2897-2903
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This article is published in Biochemistry.The article was published on 1972-07-18. It has received 134 citations till now. The article focuses on the topics: Proteolytic enzymes & Membrane.

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Citations
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THE ORGANIZATION OF PROTEINS IN THE HUMAN RED BLOOD CELL MEMBRANE A Review

TL;DR: This article will focus on the localization and modes of association of individual major polypeptides within the human red cell membrane.
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Membrane proteins related to anion permeability of human red blood cells. I. Localization of disulfonic stilbene binding sites in proteins involved in permeation.

TL;DR: (3H)DIDS was used as a convalent label for membrane sites involved in anion permeability resulting in almost complete inhibition of anion exchange and because of the linear relationship of binding to inhibition and the unique architecture of the site, it is suggested that the (3H)'s-binding site is the substrate binding site of the anion transport system.
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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A simple efficient liquid scintillator for counting aqueous solutions in a liquid scintillation counter

TL;DR: A modification of the naphthalene-dioxane-PPO liquid scintillator has been described which will allow up to 3.0 ml of an aqueous solution to be counted as mentioned in this paper.
Journal ArticleDOI

The preparation and chemical characteristics of hemoglobin-free ghosts of human erythrocytes

TL;DR: The effects of the ionic strength and pH of the hemolyzing solution on the hemoglobin content of human erythrocyte ghosts were studied in phosphate buffers and suggest an electrophysical interaction of hemoglobin with membrane constituents.
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