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Journal ArticleDOI

Major human erythrocyte glycoprotein spans the cell membrane.

Mark S. Bretscher
- 23 Jun 1971 - 
- Vol. 231, Iss: 25, pp 229-232
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TLDR
The polypeptide part of the principal glycoprotein on the surface of human erythrocytes extends through the membrane barrier to the interior surface of the cell membrane.
Abstract
The polypeptide part of the principal glycoprotein on the surface of human erythrocytes extends through the membrane barrier to the interior surface of the cell membrane.

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Citations
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Journal ArticleDOI

The fluid mosaic model of the structure of cell membranes.

TL;DR: Results strongly indicate that the bivalent antibodies produce an aggregation of the surface immunoglobulin molecules in the plane of the membrane, which can occur only if the immunoglOBulin molecules are free to diffuse in the membrane.
Journal ArticleDOI

Solubilization of membranes by detergents

TL;DR: This review focuses on work that deals with the mechanisms of detergent action in membrane solubilization including properties of detergents model lipid systems and detergent-protein interactions; in addition a possible sequence of events when deterGents interact with biological membranes receives attention.
Book ChapterDOI

Measurement of molecular weights by electrophoresis on SDS-acrylamide gel.

TL;DR: This chapter describes methods for sodium dodecyl sulfate gel electrophoresis and the characterization of proteins separated on SDS gels, designed to alkylate various functional groups of the proteins so as to maximize the likelihood of irreversible denaturation.
Journal ArticleDOI

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.
Journal ArticleDOI

The Purification and Mechanism of Action of Human Antithrombin-Heparin Cofactor

TL;DR: It is suggested that heparin binds to the inhibitor and causes a conformational change which results in a more favorable exposure of the arginine reactive site, allowing a rapid interaction with thrombin.
References
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Journal ArticleDOI

The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis

TL;DR: The results show that the polyacrylamide gel electrophoresis method can be used with great confidence to determine the molecular weights of polypeptide chains for a wide variety of proteins.
Journal ArticleDOI

The arrangement of proteins in the human erythrocyte membrane

TL;DR: When the iodination of intact human erythrocytes was catalyzed by the enzyme lactoperoxidase, only a single stroma protein was iodinated, and this protein component thus appears to be the only protein component exposed on the exterior of the human ERYthrocyte surface.
Journal ArticleDOI

Sulfanilic acid diazonium salt: a label for the outside of the human erythrocyte membrane.

TL;DR: The membrane contains protein complexes which can be dissociated by sodium dodecyl sulfate after exposure to salt, and the dissociation is less extensive when intact membranes are exposed to salt.
Journal ArticleDOI

Human erythrocyte membranes: specific labelling of surface proteins.

TL;DR: A very reactive, highly radioactive reagent designed to acylate amino groups has been synthesized: this compound, the sulphone of 35 S-labelled formylmethionyl methyl phosphate, cannot pass through the red blood cell membrane.
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